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Conserved domains on  [gi|2024332955|ref|XP_040515141|]
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laminin subunit beta-4 isoform X2 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
31-266 1.41e-100

Laminin N-terminal (Domain VI);


:

Pssm-ID: 459653  Cd Length: 230  Bit Score: 322.22  E-value: 1.41e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955   31 CHPAVGDLLLGRskQLVASSTCGVNGPQKYCIIGYLEAEQKCFVCDSRYPynpytqHNSHMIENvITAFEPDRKKKWWQS 110
Cdd:pfam00055    1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDP------HNSHPPSN-LTDSNNGTNETWWQS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  111 ENGV---DHVSIRLDLETLFQFSHLILTFKTFRPAAMLVERSTDFGQTWKAFRYFAQDCAASFpNISSGPSKGVGD--VI 185
Cdd:pfam00055   72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIKDdeVI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  186 CDSRYSDIEPSTEGEVVLKAL--DPSFEIENpYVPYIQELITMTNLRINFTKLHTLGDALLGRRhgDPLEKYYYAVYEMV 263
Cdd:pfam00055  151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDP--SVLRKYYYAISDIS 227

                   ...
gi 2024332955  264 VRG 266
Cdd:pfam00055  228 VGG 230
cc_LAMB_C super family cl40438
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
1704-1773 1.14e-24

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 cd22301:

Pssm-ID: 424069 [Multi-domain]  Cd Length: 70  Bit Score: 98.58  E-value: 1.14e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1704 LQKVKQLKEEAEKLAEETEKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKYSTC 1773
Cdd:cd22301      1 NERLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
866-914 7.34e-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: 7.34e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024332955  866 CECHPQGSVSSLCDQVTGQCACLRDVDGRRCSQCLPGYFGFPHCRPCAC 914
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1129-1174 1.24e-11

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 1.24e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955  1129 CDCDLKNTQSNQCDQLTGQCQCKVGYGGKRCDECEENYFGNPQKHC 1174
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
457-506 5.18e-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: 5.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024332955  457 PCNCDAAGTLPfSVCDSTTGECLCQQFTTGRRCEKCVEGYWGLGKSVYGC 506
Cdd:cd00055      1 PCDCNGHGSLS-GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
508-551 1.58e-10

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


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 57.75  E-value: 1.58e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024332955  508 PCDCDIGGSQDNLCSPEDGQCKCLPNIVGRQCNEPAPGYFFLPL 551
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1071-1127 2.54e-10

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 57.36  E-value: 2.54e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955 1071 CKCNPAGVLPATCpggdatclcDPATGACLCQPNVVGTTCDQCAPGYWDLAGGKGCQ 1127
Cdd:pfam00053    1 CDCNPHGSLSDTC---------DPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
818-863 2.84e-10

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.94  E-value: 2.84e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955   818 CKCNPQGSLNASCSRLGGQCHCKANVVGRCCDTCSAGSYGFGFHGC 863
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1177-1221 7.93e-10

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.78  E-value: 7.93e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955  1177 CNCNPEGTSWPQCDKATGVCNCRAGVTGRFCDQCGRGF-EKDFPSC 1221
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYyGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
398-455 1.80e-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: 1.80e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024332955  398 CSCNPEGTLHhGACESHTdpvlgtvaGRCLCKENVEGVRCDKCKANHFRLRGSDPLGC 455
Cdd:pfam00053    1 CDCNPHGSLS-DTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1502-1769 1.41e-08

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


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 59.65  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1502 ELERAKNQIKidrevTKEfiKKVKNFlsdESVPPEDIEQVASYVLQINlpltprELRSMIGKIRSIMAHCESKAAKALPP 1581
Cdd:TIGR04523   41 KLKTIKNELK-----NKE--KELKNL---DKNLNKDEEKINNSNNKIK------ILEQQIKDLNDKLKKNKDKINKLNSD 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1582 VDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQT-KVLMNrnqat 1660
Cdd:TIGR04523  105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENeLNLLE----- 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1661 nvragaeaayKQAQKIDNEFADIKRKYAILQDKLkakgppkVTLQKVKQLKEEAEKLAEETEKKIRRITD-LEKKLQDLN 1739
Cdd:TIGR04523  180 ----------KEKLNIQKNIDKIKNKLLKLELLL-------SNLKKKIQKNKSLESQISELKKQNNQLKDnIEKKQQEIN 242
                          250       260       270
                   ....*....|....*....|....*....|...
gi 2024332955 1740 QTK---QDKAEQLRQLEEQVIAIKNEITEQESK 1769
Cdd:TIGR04523  243 EKTteiSNTQTQLNQLKDEQNKIKKQLSEKQKE 275
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
911-958 4.84e-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: 50.82  E-value: 4.84e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024332955  911 PCACHGFAEL---CHPVTGECLnCSRFTAGSHCERCIDGYYGNPSNREPCR 958
Cdd:cd00055      1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1018-1069 3.47e-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: 48.50  E-value: 3.47e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024332955 1018 PCPCNSNIDVtdPESCNRVTGECVkCLHNTHGANCQFCKPGYFGSALN-QDCR 1069
Cdd:cd00055      1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
268-323 7.76e-07

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


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 47.35  E-value: 7.76e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024332955  268 CFCNGHAS---HCDPiqnlrgdvfhqpgmVHGRCICHHNTEGLSCERCKDFYNDAPWRP 323
Cdd:cd00055      2 CDCNGHGSlsgQCDP--------------GTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
335-386 6.18e-06

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 45.04  E-value: 6.18e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024332955  335 CNCNGH---SGRCHFdmavyqasggvSGGVCeDCQHNTTGHHCDQCKLFFYQDPH 386
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQC-LCKPGVTGRHCDRCKPGYYGLPS 43
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
960-1016 6.99e-04

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 39.26  E-value: 6.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955  960 CMCPGVPTSkrffAHSCyqDSQTSQivCNCLEGYSGNRCDECPSGFYKIPGSPGEEC 1016
Cdd:pfam00053    1 CDCNPHGSL----SDTC--DPETGQ--CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
31-266 1.41e-100

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 322.22  E-value: 1.41e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955   31 CHPAVGDLLLGRskQLVASSTCGVNGPQKYCIIGYLEAEQKCFVCDSRYPynpytqHNSHMIENvITAFEPDRKKKWWQS 110
Cdd:pfam00055    1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDP------HNSHPPSN-LTDSNNGTNETWWQS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  111 ENGV---DHVSIRLDLETLFQFSHLILTFKTFRPAAMLVERSTDFGQTWKAFRYFAQDCAASFpNISSGPSKGVGD--VI 185
Cdd:pfam00055   72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIKDdeVI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  186 CDSRYSDIEPSTEGEVVLKAL--DPSFEIENpYVPYIQELITMTNLRINFTKLHTLGDALLGRRhgDPLEKYYYAVYEMV 263
Cdd:pfam00055  151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDP--SVLRKYYYAISDIS 227

                   ...
gi 2024332955  264 VRG 266
Cdd:pfam00055  228 VGG 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
26-266 1.21e-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: 234.18  E-value: 1.21e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955    26 CGAGSCHPAVGDLLLGRskQLVASSTCGVNGPQKYCI-IGYLEAEQKCFVCDSRYPynpytqHNSHMIENVITAFEPDrK 104
Cdd:smart00136    2 GRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNP------RRSHPAENLTDGNNPN-N 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955   105 KKWWQSEN---GVDHVSIRLDLETLFQFSHLILTFKTFRPAAMLVERStDFGQTWKAFRYFAQDCAASFPNISSGP-SKG 180
Cdd:smart00136   73 PTWWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPiTKG 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955   181 VG-DVICDSRYSDIEPSTEGEVVLKALDPSFEIEN-PYVPYIQELITMTNLRINFTKLHTLGDALLGRRHGDpLEKYYYA 258
Cdd:smart00136  152 NEdEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEV-TRRYYYA 230

                    ....*...
gi 2024332955   259 VYEMVVRG 266
Cdd:smart00136  231 ISDIAVGG 238
cc_LAMB4_C cd22301
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ...
1704-1773 1.14e-24

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


Pssm-ID: 411972 [Multi-domain]  Cd Length: 70  Bit Score: 98.58  E-value: 1.14e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1704 LQKVKQLKEEAEKLAEETEKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKYSTC 1773
Cdd:cd22301      1 NERLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
866-914 7.34e-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: 7.34e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024332955  866 CECHPQGSVSSLCDQVTGQCACLRDVDGRRCSQCLPGYFGFPHCRPCAC 914
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
865-907 3.23e-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: 62.76  E-value: 3.23e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024332955  865 PCECHPQGSVSSLCDQVTGQCACLRDVDGRRCSQCLPGYFGFP 907
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1129-1174 1.24e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 1.24e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955  1129 CDCDLKNTQSNQCDQLTGQCQCKVGYGGKRCDECEENYFGNPQKHC 1174
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1129-1177 1.45e-11

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.83  E-value: 1.45e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024332955 1129 CDCDLKNTQSNQCDQLTGQCQCKVGYGGKRCDECEENYFGNPQKHCISC 1177
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
457-506 5.18e-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: 5.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024332955  457 PCNCDAAGTLPfSVCDSTTGECLCQQFTTGRRCEKCVEGYWGLGKSVYGC 506
Cdd:cd00055      1 PCDCNGHGSLS-GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
866-909 5.77e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 58.86  E-value: 5.77e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955   866 CECHPQGSVSSLCDQVTGQCACLRDVDGRRCSQCLPGYFG--FPHC 909
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
508-551 1.58e-10

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 57.75  E-value: 1.58e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024332955  508 PCDCDIGGSQDNLCSPEDGQCKCLPNIVGRQCNEPAPGYFFLPL 551
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1129-1172 1.72e-10

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 57.75  E-value: 1.72e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024332955 1129 CDCDLKNTQSNQCDQLTGQCQCKVGYGGKRCDECEENYFGNPQK 1172
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1071-1127 2.54e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 57.36  E-value: 2.54e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955 1071 CKCNPAGVLPATCpggdatclcDPATGACLCQPNVVGTTCDQCAPGYWDLAGGKGCQ 1127
Cdd:pfam00053    1 CDCNPHGSLSDTC---------DPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
818-863 2.84e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.94  E-value: 2.84e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955   818 CKCNPQGSLNASCSRLGGQCHCKANVVGRCCDTCSAGSYGFGFHGC 863
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1177-1221 7.93e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.78  E-value: 7.93e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955  1177 CNCNPEGTSWPQCDKATGVCNCRAGVTGRFCDQCGRGF-EKDFPSC 1221
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYyGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1071-1127 8.49e-10

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.82  E-value: 8.49e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024332955 1071 CKCNPAGVLPATCpggdatclcDPATGACLCQPNVVGTTCDQCAPGYWDLA-GGKGCQ 1127
Cdd:cd00055      2 CDCNGHGSLSGQC---------DPGTGQCECKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
818-868 8.79e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.82  E-value: 8.79e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024332955  818 CKCNPQGSLNASCSRLGGQCHCKANVVGRCCDTCSAGSYgfGFHGCYPCEC 868
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY--GLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
817-862 1.00e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.44  E-value: 1.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2024332955  817 ACKCNPQGSLNASCSRLGGQCHCKANVVGRCCDTCSAGSYGFGFHG 862
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
458-511 1.17e-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: 55.44  E-value: 1.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024332955  458 CNCDAAGTLPfSVCDSTTGECLCQQFTTGRRCEKCVEGYWGLGKsvygCSPCDC 511
Cdd:pfam00053    1 CDCNPHGSLS-DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS----DPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
398-455 1.80e-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: 1.80e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024332955  398 CSCNPEGTLHhGACESHTdpvlgtvaGRCLCKENVEGVRCDKCKANHFRLRGSDPLGC 455
Cdd:pfam00053    1 CDCNPHGSLS-DTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1176-1214 6.96e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 53.13  E-value: 6.96e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2024332955 1176 SCNCNPEGTSWPQCDKATGVCNCRAGVTGRFCDQCGRGF 1214
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
458-498 1.25e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.31  E-value: 1.25e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 2024332955   458 CNCDAAGTLPfSVCDSTTGECLCQQFTTGRRCEKCVEGYWG 498
Cdd:smart00180    1 CDCDPGGSAS-GTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
509-547 1.27e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.31  E-value: 1.27e-08
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 2024332955   509 CDCDIGGSQDNLCSPEDGQCKCLPNIVGRQCNEPAPGYF 547
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1502-1769 1.41e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 59.65  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1502 ELERAKNQIKidrevTKEfiKKVKNFlsdESVPPEDIEQVASYVLQINlpltprELRSMIGKIRSIMAHCESKAAKALPP 1581
Cdd:TIGR04523   41 KLKTIKNELK-----NKE--KELKNL---DKNLNKDEEKINNSNNKIK------ILEQQIKDLNDKLKKNKDKINKLNSD 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1582 VDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQT-KVLMNrnqat 1660
Cdd:TIGR04523  105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENeLNLLE----- 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1661 nvragaeaayKQAQKIDNEFADIKRKYAILQDKLkakgppkVTLQKVKQLKEEAEKLAEETEKKIRRITD-LEKKLQDLN 1739
Cdd:TIGR04523  180 ----------KEKLNIQKNIDKIKNKLLKLELLL-------SNLKKKIQKNKSLESQISELKKQNNQLKDnIEKKQQEIN 242
                          250       260       270
                   ....*....|....*....|....*....|...
gi 2024332955 1740 QTK---QDKAEQLRQLEEQVIAIKNEITEQESK 1769
Cdd:TIGR04523  243 EKTteiSNTQTQLNQLKDEQNKIKKQLSEKQKE 275
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1177-1214 1.77e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 51.97  E-value: 1.77e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2024332955 1177 CNCNPEGTSWPQCDKATGVCNCRAGVTGRFCDQCGRGF 1214
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1071-1126 2.64e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 2.64e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024332955  1071 CKCNPAGVLPATCpggdatclcDPATGACLCQPNVVGTTCDQCAPGYWDLAGGkGC 1126
Cdd:smart00180    1 CDCDPGGSASGTC---------DPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1592-1771 2.72e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.99  E-value: 2.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1592 AVSSQGRSKN--TLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQTKVLMNRNQATNVRAGAEAA 1669
Cdd:COG4372     27 AALSEQLRKAlfELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1670 YKQAQKIDNEFADIKRKYAILQDKLKAkgppkvtlqkvkqlkeeaeklaeetekkirritdLEKKLQDLNQTKQDKAEQL 1749
Cdd:COG4372    107 QEEAEELQEELEELQKERQDLEQQRKQ----------------------------------LEAQIAELQSEIAEREEEL 152
                          170       180
                   ....*....|....*....|..
gi 2024332955 1750 RQLEEQVIAIKNEITEQESKYS 1771
Cdd:COG4372    153 KELEEQLESLQEELAALEQELQ 174
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
911-958 4.84e-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: 50.82  E-value: 4.84e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024332955  911 PCACHGFAEL---CHPVTGECLnCSRFTAGSHCERCIDGYYGNPSNREPCR 958
Cdd:cd00055      1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
397-456 1.35e-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: 49.66  E-value: 1.35e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  397 PCSCNPEGTLHhGACESHTdpvlgtvaGRCLCKENVEGVRCDKCKANHFRLRgSDPLGCQ 456
Cdd:cd00055      1 PCDCNGHGSLS-GQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1018-1069 3.47e-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: 48.50  E-value: 3.47e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024332955 1018 PCPCNSNIDVtdPESCNRVTGECVkCLHNTHGANCQFCKPGYFGSALN-QDCR 1069
Cdd:cd00055      1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
509-552 5.02e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.12  E-value: 5.02e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024332955  509 CDCDIGGSQDNLCSPEDGQCKCLPNIVGRQCNEPAPGYFFLPLD 552
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
268-323 7.76e-07

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 47.35  E-value: 7.76e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024332955  268 CFCNGHAS---HCDPiqnlrgdvfhqpgmVHGRCICHHNTEGLSCERCKDFYNDAPWRP 323
Cdd:cd00055      2 CDCNGHGSlsgQCDP--------------GTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1019-1061 8.43e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 47.35  E-value: 8.43e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024332955 1019 CPCNSNIDVTDpeSCNRVTGECVkCLHNTHGANCQFCKPGYFG 1061
Cdd:pfam00053    1 CDCNPHGSLSD--TCDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
398-455 1.21e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 46.92  E-value: 1.21e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024332955   398 CSCNPEGTlHHGACESHTdpvlgtvaGRCLCKENVEGVRCDKCKANHFrlrGSDPLGC 455
Cdd:smart00180    1 CDCDPGGS-ASGTCDPDT--------GQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
335-386 6.18e-06

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 45.04  E-value: 6.18e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024332955  335 CNCNGH---SGRCHFdmavyqasggvSGGVCeDCQHNTTGHHCDQCKLFFYQDPH 386
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQC-LCKPGVTGRHCDRCKPGYYGLPS 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
334-388 1.12e-05

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 44.27  E-value: 1.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024332955  334 RCNCNGH---SGRCHFDmavyqasggvsGGVCEdCQHNTTGHHCDQCKLFFYQDPHKA 388
Cdd:cd00055      1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1021-1062 1.57e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 40.76  E-value: 1.57e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 2024332955  1021 CNSNIDVTDPESCNRVTGECVkCLHNTHGANCQFCKPGYFGS 1062
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
268-326 2.97e-04

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.03  E-value: 2.97e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024332955  268 CFCNGHAS---HCDPIQnlrgdvfhqpgmvhGRCICHHNTEGLSCERCKDFYNDAPWRPAEG 326
Cdd:pfam00053    1 CDCNPHGSlsdTCDPET--------------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
912-951 4.25e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.60  E-value: 4.25e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2024332955   912 CACHG---FAELCHPVTGECLnCSRFTAGSHCERCIDGYYGNP 951
Cdd:smart00180    1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
960-1016 6.99e-04

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 39.26  E-value: 6.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955  960 CMCPGVPTSkrffAHSCyqDSQTSQivCNCLEGYSGNRCDECPSGFYKIPGSPGEEC 1016
Cdd:pfam00053    1 CDCNPHGSL----SDTC--DPETGQ--CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
1669-1771 9.54e-04

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 41.41  E-value: 9.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1669 AYKQAQ-KIDNEFADIKRKYAILQDKLKAKgppKVTLQKVKQLKEEAeklaeeTEKKIRRITDLEKKLQDLNQTKQDKAE 1747
Cdd:pfam03938   16 EGKAAQaQLEKKFKKRQAELEAKQKELQKL---YEELQKDGALLEEE------REEKEQELQKKEQELQQLQQKAQQELQ 86
                           90       100
                   ....*....|....*....|....*...
gi 2024332955 1748 QLRQLEEQVI--AIKNEITE--QESKYS 1771
Cdd:pfam03938   87 KKQQELLQPIqdKINKAIKEvaKEKGYD 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1464-1771 1.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1464 LLTNLTTQLQDPENQYLQVEHIRRMAEDTK-----LKGSHfnGELERAKnqikidreVTKEFIKKVKNFLSDEsvPPEDI 1538
Cdd:PRK03918   322 EINGIEERIKELEEKEERLEELKKKLKELEkrleeLEERH--ELYEEAK--------AKKEELERLKKRLTGL--TPEKL 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1539 EQVASYVLQINLPLTP--RELRSMIGKIRSIM-----AHCESKAAKALPPVDK--INDELKnavssqgrsKNTLMKLNEG 1609
Cdd:PRK03918   390 EKELEELEKAKEEIEEeiSKITARIGELKKEIkelkkAIEELKKAKGKCPVCGreLTEEHR---------KELLEEYTAE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1610 IQGIRAQITQAGNQMNKTSN---KLNDFSAKQSRLEDEITTL-QTKVLMNRNQATNVRAgAEAAYKQAQKIDNEFADIKR 1685
Cdd:PRK03918   461 LKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLKELAeQLKELEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKG 539
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1686 KYAILQDKLKAKGPPKVTLQKVKQLKEEAEKLAEETEKKIRR-----ITDLEKKLQDLN-------------QTKQDKAE 1747
Cdd:PRK03918   540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKELEpfyneylelkdaeKELEREEK 619
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2024332955 1748 QLRQLEEQVIA--------------IKNEITEQESKYS 1771
Cdd:PRK03918   620 ELKKLEEELDKafeelaetekrleeLRKELEELEKKYS 657
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
1471-1774 1.25e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 1.25e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  1471 QLQDpenqYLQVEHIRRMaEDTKLKGSHFNgeleraknqikidrevtkeFIKKVKNFLSDESVPPEDIeQVASYvlqINL 1550
Cdd:smart00787   11 SLQD----FLNMTGIRFM-ELLTTKRRHTP-------------------APAISLNRISEEDCSLDQY-VVAGY---CTV 62
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  1551 PL------TPRELRSMIGKIRSIMAHCESKAAKALPPVDK------------INDELKNaVSSQGR--SKNT----LMKL 1606
Cdd:smart00787   63 PLlelyqfSCKELKKYISEGRDLFKEIEEETLINNPPLFKeyfsaspdvkllMDKQFQL-VKTFARleAKKMwyewRMKL 141
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  1607 NEGIQ----GIRAQITQAGNQMNKTSNKLNDF----SAKQSRLEDEITTLQtkvlmnrnqatnvragaeaaykqaqKIDN 1678
Cdd:smart00787  142 LEGLKegldENLEGLKEDYKLLMKELELLNSIkpklRDRKDALEEELRQLK-------------------------QLED 196
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  1679 EFADIKRKyaiLQDKLKAKgppkvtLQKVKQLkeeaeklaeetekkirrITDLEKKLQDLNQTKQDKAEQLRQLEEQVIA 1758
Cdd:smart00787  197 ELEDCDPT---ELDRAKEK------LKKLLQE-----------------IMIKVKKLEELEEELQELESKIEDLTNKKSE 250
                           330
                    ....*....|....*.
gi 2024332955  1759 IKNEITEQESKYSTCK 1774
Cdd:smart00787  251 LNTEIAEAEKKLEQCR 266
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
1583-1696 1.28e-03

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


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 42.40  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1583 DKINDELKNAVSSQGRSKNtlmKLNEGIQGIRAQITQAGNQMNKTSNKLNDFsakQSRLEDEITTLQTKV---------- 1652
Cdd:cd21116     76 PDLIELADNLIKGDQGAKQ---QLLQGLEALQSQVTKKQTSVTSFINELTTF---KNDLDDDSRNLQTDAtkaqaqvavl 149
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024332955 1653 -LMNrNQATNVRAGAEAAYKQAQKIDNEFADIKRKYAILQDKLKA 1696
Cdd:cd21116    150 nALK-NQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLED 193
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
282-321 1.72e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 1.72e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 2024332955   282 NLRGDVFHQPGMVHGRCICHHNTEGLSCERCKDFYNDAPW 321
Cdd:smart00180    4 DPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1459-1760 2.28e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.79  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1459 EETAVLLTNLTTQLqdpENQYLQVEHIRRMAEDTKLKgSHFNGELERAKNQiKIDREVTKEFIKKVK--NFLSDESVPPE 1536
Cdd:pfam05483  179 EETRQVYMDLNNNI---EKMILAFEELRVQAENARLE-MHFKLKEDHEKIQ-HLEEEYKKEINDKEKqvSLLLIQITEKE 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1537 DIEQVASYVLQinlpltprELRSMIGKIRSIMAHCESKAAKALPPVDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQ 1616
Cdd:pfam05483  254 NKMKDLTFLLE--------ESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1617 ITQAGNQMNKTSNKLNDFSAKQSRL--EDEITTLQTKVLMNRNQATnvragAEAAYKQAQKIDNEfadIKRKYAILQDKL 1694
Cdd:pfam05483  326 ICQLTEEKEAQMEELNKAKAAHSFVvtEFEATTCSLEELLRTEQQR-----LEKNEDQLKIITME---LQKKSSELEEMT 397
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955 1695 KAKGPPKVTLQKVKQLKEEAEKLAEEtEKKIRRITD-LEKKLQDLNQTKQDKAEQLRQLEEQVIAIK 1760
Cdd:pfam05483  398 KFKNNKEVELEELKKILAEDEKLLDE-KKQFEKIAEeLKGKEQELIFLLQAREKEIHDLEIQLTAIK 463
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
335-385 2.57e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 2.57e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2024332955   335 CNCNG---HSGRCHFDmavyqasggvsGGVCEdCQHNTTGHHCDQCKLFFYQDP 385
Cdd:smart00180    1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
TNFRSF4 cd13406
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ...
921-1006 4.85e-03

Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.


Pssm-ID: 276911 [Multi-domain]  Cd Length: 142  Bit Score: 39.30  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  921 CHPVTGECLNCSRfTAGSHCERCIDGYYGNPSNREPCRPC-MCPGVPTSKRFFAHSCYQDSqtsqiVCNCLEGY------ 993
Cdd:cd13406     18 CPPGEGMESRCTG-TQDTVCSPCEPGFYNEAVNYEPCKPCtQCNQRSGSEEKQKCTKTSDT-----VCRCRPGTqpldsy 91
                           90
                   ....*....|....
gi 2024332955  994 -SGNRCDECPSGFY 1006
Cdd:cd13406     92 kPGVDCVPCPPGHF 105
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
31-266 1.41e-100

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 322.22  E-value: 1.41e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955   31 CHPAVGDLLLGRskQLVASSTCGVNGPQKYCIIGYLEAEQKCFVCDSRYPynpytqHNSHMIENvITAFEPDRKKKWWQS 110
Cdd:pfam00055    1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDP------HNSHPPSN-LTDSNNGTNETWWQS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  111 ENGV---DHVSIRLDLETLFQFSHLILTFKTFRPAAMLVERSTDFGQTWKAFRYFAQDCAASFpNISSGPSKGVGD--VI 185
Cdd:pfam00055   72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRGIKDdeVI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  186 CDSRYSDIEPSTEGEVVLKAL--DPSFEIENpYVPYIQELITMTNLRINFTKLHTLGDALLGRRhgDPLEKYYYAVYEMV 263
Cdd:pfam00055  151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDP--SVLRKYYYAISDIS 227

                   ...
gi 2024332955  264 VRG 266
Cdd:pfam00055  228 VGG 230
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
26-266 1.21e-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: 234.18  E-value: 1.21e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955    26 CGAGSCHPAVGDLLLGRskQLVASSTCGVNGPQKYCI-IGYLEAEQKCFVCDSRYPynpytqHNSHMIENVITAFEPDrK 104
Cdd:smart00136    2 GRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNP------RRSHPAENLTDGNNPN-N 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955   105 KKWWQSEN---GVDHVSIRLDLETLFQFSHLILTFKTFRPAAMLVERStDFGQTWKAFRYFAQDCAASFPNISSGP-SKG 180
Cdd:smart00136   73 PTWWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPiTKG 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955   181 VG-DVICDSRYSDIEPSTEGEVVLKALDPSFEIEN-PYVPYIQELITMTNLRINFTKLHTLGDALLGRRHGDpLEKYYYA 258
Cdd:smart00136  152 NEdEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEV-TRRYYYA 230

                    ....*...
gi 2024332955   259 VYEMVVRG 266
Cdd:smart00136  231 ISDIAVGG 238
cc_LAMB4_C cd22301
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ...
1704-1773 1.14e-24

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


Pssm-ID: 411972 [Multi-domain]  Cd Length: 70  Bit Score: 98.58  E-value: 1.14e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1704 LQKVKQLKEEAEKLAEETEKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKYSTC 1773
Cdd:cd22301      1 NERLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
cc_LAMB_C cd22295
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ...
1704-1773 4.11e-15

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: 71.54  E-value: 4.11e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1704 LQKVKQLKEEAEKLAEETEKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKYSTC 1773
Cdd:cd22295      1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
866-914 7.34e-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: 7.34e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024332955  866 CECHPQGSVSSLCDQVTGQCACLRDVDGRRCSQCLPGYFGFPHCRPCAC 914
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
865-907 3.23e-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: 62.76  E-value: 3.23e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024332955  865 PCECHPQGSVSSLCDQVTGQCACLRDVDGRRCSQCLPGYFGFP 907
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1129-1174 1.24e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 1.24e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955  1129 CDCDLKNTQSNQCDQLTGQCQCKVGYGGKRCDECEENYFGNPQKHC 1174
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1129-1177 1.45e-11

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 60.83  E-value: 1.45e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2024332955 1129 CDCDLKNTQSNQCDQLTGQCQCKVGYGGKRCDECEENYFGNPQKHCISC 1177
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
457-506 5.18e-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: 5.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024332955  457 PCNCDAAGTLPfSVCDSTTGECLCQQFTTGRRCEKCVEGYWGLGKSVYGC 506
Cdd:cd00055      1 PCDCNGHGSLS-GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
866-909 5.77e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 58.86  E-value: 5.77e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955   866 CECHPQGSVSSLCDQVTGQCACLRDVDGRRCSQCLPGYFG--FPHC 909
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
508-551 1.58e-10

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 57.75  E-value: 1.58e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024332955  508 PCDCDIGGSQDNLCSPEDGQCKCLPNIVGRQCNEPAPGYFFLPL 551
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1129-1172 1.72e-10

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 57.75  E-value: 1.72e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024332955 1129 CDCDLKNTQSNQCDQLTGQCQCKVGYGGKRCDECEENYFGNPQK 1172
Cdd:cd00055      2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1071-1127 2.54e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 57.36  E-value: 2.54e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955 1071 CKCNPAGVLPATCpggdatclcDPATGACLCQPNVVGTTCDQCAPGYWDLAGGKGCQ 1127
Cdd:pfam00053    1 CDCNPHGSLSDTC---------DPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
818-863 2.84e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.94  E-value: 2.84e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955   818 CKCNPQGSLNASCSRLGGQCHCKANVVGRCCDTCSAGSYGFGFHGC 863
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1177-1221 7.93e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 55.78  E-value: 7.93e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2024332955  1177 CNCNPEGTSWPQCDKATGVCNCRAGVTGRFCDQCGRGF-EKDFPSC 1221
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYyGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1071-1127 8.49e-10

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.82  E-value: 8.49e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024332955 1071 CKCNPAGVLPATCpggdatclcDPATGACLCQPNVVGTTCDQCAPGYWDLA-GGKGCQ 1127
Cdd:cd00055      2 CDCNGHGSLSGQC---------DPGTGQCECKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
818-868 8.79e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.82  E-value: 8.79e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024332955  818 CKCNPQGSLNASCSRLGGQCHCKANVVGRCCDTCSAGSYgfGFHGCYPCEC 868
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY--GLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
817-862 1.00e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 55.44  E-value: 1.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2024332955  817 ACKCNPQGSLNASCSRLGGQCHCKANVVGRCCDTCSAGSYGFGFHG 862
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
458-511 1.17e-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: 55.44  E-value: 1.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024332955  458 CNCDAAGTLPfSVCDSTTGECLCQQFTTGRRCEKCVEGYWGLGKsvygCSPCDC 511
Cdd:pfam00053    1 CDCNPHGSLS-DTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPS----DPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
398-455 1.80e-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: 1.80e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024332955  398 CSCNPEGTLHhGACESHTdpvlgtvaGRCLCKENVEGVRCDKCKANHFRLRGSDPLGC 455
Cdd:pfam00053    1 CDCNPHGSLS-DTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1176-1214 6.96e-09

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 53.13  E-value: 6.96e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2024332955 1176 SCNCNPEGTSWPQCDKATGVCNCRAGVTGRFCDQCGRGF 1214
Cdd:cd00055      1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
458-498 1.25e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.31  E-value: 1.25e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 2024332955   458 CNCDAAGTLPfSVCDSTTGECLCQQFTTGRRCEKCVEGYWG 498
Cdd:smart00180    1 CDCDPGGSAS-GTCDPDTGQCECKPNVTGRRCDRCAPGYYG 40
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
509-547 1.27e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 52.31  E-value: 1.27e-08
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 2024332955   509 CDCDIGGSQDNLCSPEDGQCKCLPNIVGRQCNEPAPGYF 547
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1502-1769 1.41e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 59.65  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1502 ELERAKNQIKidrevTKEfiKKVKNFlsdESVPPEDIEQVASYVLQINlpltprELRSMIGKIRSIMAHCESKAAKALPP 1581
Cdd:TIGR04523   41 KLKTIKNELK-----NKE--KELKNL---DKNLNKDEEKINNSNNKIK------ILEQQIKDLNDKLKKNKDKINKLNSD 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1582 VDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQT-KVLMNrnqat 1660
Cdd:TIGR04523  105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENeLNLLE----- 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1661 nvragaeaayKQAQKIDNEFADIKRKYAILQDKLkakgppkVTLQKVKQLKEEAEKLAEETEKKIRRITD-LEKKLQDLN 1739
Cdd:TIGR04523  180 ----------KEKLNIQKNIDKIKNKLLKLELLL-------SNLKKKIQKNKSLESQISELKKQNNQLKDnIEKKQQEIN 242
                          250       260       270
                   ....*....|....*....|....*....|...
gi 2024332955 1740 QTK---QDKAEQLRQLEEQVIAIKNEITEQESK 1769
Cdd:TIGR04523  243 EKTteiSNTQTQLNQLKDEQNKIKKQLSEKQKE 275
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1177-1214 1.77e-08

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 51.97  E-value: 1.77e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2024332955 1177 CNCNPEGTSWPQCDKATGVCNCRAGVTGRFCDQCGRGF 1214
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1465-1775 1.80e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 59.65  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1465 LTNLTTQLQDPENQYLQV----EHIRRMAEDTKLKGSHFNG---ELERAKNQIKIDREVTK-----EFIKKVKNFLSDES 1532
Cdd:TIGR04523  241 INEKTTEISNTQTQLNQLkdeqNKIKKQLSEKQKELEQNNKkikELEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQE 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1533 vppEDIEQVASYVLQINLPLTprELRSMIGKIRSIMAHCESKAAKALPPVDKINDELKNAVSSQGRSKNTLMKLNEGIQG 1612
Cdd:TIGR04523  321 ---KKLEEIQNQISQNNKIIS--QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1613 IRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQTKVLMNRNQA---TNVRAGAEAAYK--------QAQKIDnefa 1681
Cdd:TIGR04523  396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkdlTNQDSVKELIIKnldntresLETQLK---- 471
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1682 DIKRKYAILQDKLKakgppkvtlQKVKQLKEEAEKLAEETEKKirriTDLEKKLQDLNQtkqdkaeQLRQLEEQVIAIKN 1761
Cdd:TIGR04523  472 VLSRSINKIKQNLE---------QKQKELKSKEKELKKLNEEK----KELEEKVKDLTK-------KISSLKEKIEKLES 531
                          330
                   ....*....|....
gi 2024332955 1762 EITEQESKYSTCKS 1775
Cdd:TIGR04523  532 EKKEKESKISDLED 545
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1071-1126 2.64e-08

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 2.64e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024332955  1071 CKCNPAGVLPATCpggdatclcDPATGACLCQPNVVGTTCDQCAPGYWDLAGGkGC 1126
Cdd:smart00180    1 CDCDPGGSASGTC---------DPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1592-1771 2.72e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.99  E-value: 2.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1592 AVSSQGRSKN--TLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQTKVLMNRNQATNVRAGAEAA 1669
Cdd:COG4372     27 AALSEQLRKAlfELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1670 YKQAQKIDNEFADIKRKYAILQDKLKAkgppkvtlqkvkqlkeeaeklaeetekkirritdLEKKLQDLNQTKQDKAEQL 1749
Cdd:COG4372    107 QEEAEELQEELEELQKERQDLEQQRKQ----------------------------------LEAQIAELQSEIAEREEEL 152
                          170       180
                   ....*....|....*....|..
gi 2024332955 1750 RQLEEQVIAIKNEITEQESKYS 1771
Cdd:COG4372    153 KELEEQLESLQEELAALEQELQ 174
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
911-958 4.84e-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: 50.82  E-value: 4.84e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024332955  911 PCACHGFAEL---CHPVTGECLnCSRFTAGSHCERCIDGYYGNPSNREPCR 958
Cdd:cd00055      1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
397-456 1.35e-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: 49.66  E-value: 1.35e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  397 PCSCNPEGTLHhGACESHTdpvlgtvaGRCLCKENVEGVRCDKCKANHFRLRgSDPLGCQ 456
Cdd:cd00055      1 PCDCNGHGSLS-GQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1499-1768 1.67e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 56.18  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1499 FNGELERAKNQIKIDREVTKEFIKKVKNFLSDESVPPEDIEQVASYVLQINLPLTPRE-----LRSMIGKIRSImahcES 1573
Cdd:TIGR04523  143 FLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllsnLKKKIQKNKSL----ES 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1574 KAAKalppVDKINDELKNAVSSQGRSKNtlmKLNEGIQGIRAQITQAGNQMNKTSNKLND-------FSAKQSRLEDEIT 1646
Cdd:TIGR04523  219 QISE----LKKQNNQLKDNIEKKQQEIN---EKTTEISNTQTQLNQLKDEQNKIKKQLSEkqkeleqNNKKIKELEKQLN 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1647 TLQTKVLMNRNQA-----TNVRAGAEAAYKQAQKIDNEFA-------DIKRKYAILQDKLKAKGPPKVTLQ--------K 1706
Cdd:TIGR04523  292 QLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISqnnkiisQLNEQISQLKKELTNSESENSEKQreleekqnE 371
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024332955 1707 VKQLKEEAEKLAEETEKKIRRITDLEKKLQD---LNQTKQDKAEQLRQ----LEEQVIAIKNEITEQES 1768
Cdd:TIGR04523  372 IEKLKKENQSYKQEIKNLESQINDLESKIQNqekLNQQKDEQIKKLQQekelLEKEIERLKETIIKNNS 440
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1018-1069 3.47e-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: 48.50  E-value: 3.47e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024332955 1018 PCPCNSNIDVtdPESCNRVTGECVkCLHNTHGANCQFCKPGYFGSALN-QDCR 1069
Cdd:cd00055      1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
509-552 5.02e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 48.12  E-value: 5.02e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024332955  509 CDCDIGGSQDNLCSPEDGQCKCLPNIVGRQCNEPAPGYFFLPLD 552
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1591-1772 5.23e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 54.64  E-value: 5.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1591 NAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMN--KTSNKLNDFSAKQSRLEDEITTLQTKvlmnRNQATNVRAGAEA 1668
Cdd:COG3206    165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQ----LAEARAELAEAEA 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1669 AYKQAQK--------------------IDNEFADIKRKYAILQDKLKAKGPPKVTLQkvkqlkeeaeklaeetekkiRRI 1728
Cdd:COG3206    241 RLAALRAqlgsgpdalpellqspviqqLRAQLAELEAELAELSARYTPNHPDVIALR--------------------AQI 300
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2024332955 1729 TDLEKKLQDLNQTKQDKAE-QLRQLEEQVIAIKNEITEQESKYST 1772
Cdd:COG3206    301 AALRAQLQQEAQRILASLEaELEALQAREASLQAQLAQLEARLAE 345
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
268-323 7.76e-07

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 47.35  E-value: 7.76e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024332955  268 CFCNGHAS---HCDPiqnlrgdvfhqpgmVHGRCICHHNTEGLSCERCKDFYNDAPWRP 323
Cdd:cd00055      2 CDCNGHGSlsgQCDP--------------GTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1019-1061 8.43e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 47.35  E-value: 8.43e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024332955 1019 CPCNSNIDVTDpeSCNRVTGECVkCLHNTHGANCQFCKPGYFG 1061
Cdd:pfam00053    1 CDCNPHGSLSD--TCDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
398-455 1.21e-06

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 46.92  E-value: 1.21e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024332955   398 CSCNPEGTlHHGACESHTdpvlgtvaGRCLCKENVEGVRCDKCKANHFrlrGSDPLGC 455
Cdd:smart00180    1 CDCDPGGS-ASGTCDPDT--------GQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1555-1765 1.70e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 51.84  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1555 RELRSMIGKIRSIMahceskaakalppvDKINDELKnavssqgRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDF 1634
Cdd:COG1340     53 KELREEAQELREKR--------------DELNEKVK-------ELKEERDELNEKLNELREELDELRKELAELNKAGGSI 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1635 SAKQSRLEDEITTLQTKVLM----NR--NQATNVRAGAEAAyKQAQKIDNEFADIKRKYAILQDKLKAKGppkvtlQKVK 1708
Cdd:COG1340    112 DKLRKEIERLEWRQQTEVLSpeeeKElvEKIKELEKELEKA-KKALEKNEKLKELRAELKELRKEAEEIH------KKIK 184
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955 1709 QLKEEAEKLAEETEKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITE 1765
Cdd:COG1340    185 ELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1598-1769 5.54e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.54  E-value: 5.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1598 RSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQTKVLMNRNQATNVRagaeaAYKQAQKID 1677
Cdd:COG1579     21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NNKEYEALQ 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1678 NEFADIKRKYAILQDKLKAKgppkvtLQKVkqlkeeaeklaeetEKKIRRITDLEKKLQDLnqtKQDKAEQLRQLEEQVI 1757
Cdd:COG1579     96 KEIESLKRRISDLEDEILEL------MERI--------------EELEEELAELEAELAEL---EAELEEKKAELDEELA 152
                          170
                   ....*....|..
gi 2024332955 1758 AIKNEITEQESK 1769
Cdd:COG1579    153 ELEAELEELEAE 164
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
335-386 6.18e-06

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 45.04  E-value: 6.18e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024332955  335 CNCNGH---SGRCHFdmavyqasggvSGGVCeDCQHNTTGHHCDQCKLFFYQDPH 386
Cdd:pfam00053    1 CDCNPHgslSDTCDP-----------ETGQC-LCKPGVTGRHCDRCKPGYYGLPS 43
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1555-1767 6.77e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 6.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1555 RELRSMIGKIRSIMAHCESKAAKalppVDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDF 1634
Cdd:COG4372     31 EQLRKALFELDKLQEELEQLREE----LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1635 SAKQSRLEDEITTLQtkvlmnrNQATNVRAGAEAAYKQAQKIDNEFADIKRKYAILQDKLKAkgppkvTLQKVKQlkeea 1714
Cdd:COG4372    107 QEEAEELQEELEELQ-------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES------LQEELAA----- 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024332955 1715 eklaEETEKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQE 1767
Cdd:COG4372    169 ----LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
cc_LAMB1_C cd22300
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ...
1723-1773 7.54e-06

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


Pssm-ID: 411971 [Multi-domain]  Cd Length: 73  Bit Score: 45.54  E-value: 7.54e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024332955 1723 KKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKYSTC 1773
Cdd:cd22300     22 SKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
334-388 1.12e-05

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 44.27  E-value: 1.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024332955  334 RCNCNGH---SGRCHFDmavyqasggvsGGVCEdCQHNTTGHHCDQCKLFFYQDPHKA 388
Cdd:cd00055      1 PCDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1575-1768 1.14e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1575 AAKALPPVDKINDELKNAVSSQGRSKNTLMKLNEgiqgiraQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQTKVLM 1654
Cdd:COG3883     11 PAFADPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1655 NRNQATNVragAEAAYKQAQKID--------NEFAD-IKRKYAI--LQDKLKAkgppkvTLQKVKQLKEEAEKLAEETEK 1723
Cdd:COG3883     84 RREELGER---ARALYRSGGSVSyldvllgsESFSDfLDRLSALskIADADAD------LLEELKADKAELEAKKAELEA 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2024332955 1724 KIRRI----TDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQES 1768
Cdd:COG3883    155 KLAELealkAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1502-1765 2.10e-05

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: 49.67  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1502 ELERAKNQIKIDREVTKEFIKKVKNFLSDESVPPEDIEQVASYVLQINLPLTP-----RELRSMIGKIRSIMAHCESKAA 1576
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeiEELEERLEEAEEELAEAEAEIE 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1577 KALPPVDKINDELKnAVSSQGRSKNT--------LMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTL 1648
Cdd:TIGR02168  786 ELEAQIEQLKEELK-ALREALDELRAeltllneeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1649 QT---KVLMNRNQATNVRAGAEAAYKQA-----------QKIDNEFADIKRKYAILQDKLKAKgppKVTLQKVKQLKeea 1714
Cdd:TIGR02168  865 EElieELESELEALLNERASLEEALALLrseleelseelRELESKRSELRRELEELREKLAQL---ELRLEGLEVRI--- 938
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024332955 1715 eklaeetEKKIRRITDLEKKLQDLNQTKQDKAE-QLRQLEEQVIAIKNEITE 1765
Cdd:TIGR02168  939 -------DNLQERLSEEYSLTLEEAEALENKIEdDEEEARRRLKRLENKIKE 983
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1465-1771 4.41e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 4.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1465 LTNLTTQLQDPENQYLQVEHIRRMaEDTKLKGSHFNGE-LERAKNQIKIDREVTKEFIKKVKNFLSDESVPPEDIEQVAS 1543
Cdd:TIGR04523  386 IKNLESQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKElLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1544 YvLQINLPLTPRELRSMIGKIRSIMAHCESKAAKalppVDKINDE-------LKNAVSSQGRSKNTLMKLNegiqgirAQ 1616
Cdd:TIGR04523  465 S-LETQLKVLSRSINKIKQNLEQKQKELKSKEKE----LKKLNEEkkeleekVKDLTKKISSLKEKIEKLE-------SE 532
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1617 ITQAGNQMNKTSNKLN--DFSAKQSRLEDEITTLQTKVLMNRNQATNVRAGAEAAYKQAQKIDNEFADIKR---KYAILQ 1691
Cdd:TIGR04523  533 KKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKeieEKEKKI 612
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1692 DKLKakgppkvtlqkvkqlkeeaeklaeetekkiRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKYS 1771
Cdd:TIGR04523  613 SSLE------------------------------KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1572-1767 4.77e-05

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: 48.51  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1572 ESKAAKALPPVDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQTK 1651
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1652 VLMNRNQATNVRAGAEAAYKQAQKIDNEFADIKRKYAILQDKLKAKGPPKVTLQKvkqlkeeaeklaeetekkirRITDL 1731
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE--------------------QIEEL 850
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024332955 1732 EKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQE 1767
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLNERASLE 886
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1582-1770 6.89e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 6.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1582 VDKINDELKNAVSSQGRskNTLMKLNEgIQGIRAQITQAGNQM---NKTSNKLNDFSAKQSRLEDEITTLQTKVlmnrnQ 1658
Cdd:COG4717     48 LERLEKEADELFKPQGR--KPELNLKE-LKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREEL-----E 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1659 ATNVRAGAEAAYKQAQKIDNEFADIKRKYAILQDKLKAkgppkvtLQKVKQLKEEAEKLAEETEKKIRRITDL-----EK 1733
Cdd:COG4717    120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE-------LRELEEELEELEAELAELQEELEELLEQlslatEE 192
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2024332955 1734 KLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKY 1770
Cdd:COG4717    193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1555-1769 7.27e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 7.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1555 RELRSMIGKIRSIMAHCESKAAKALPPVDKINDELKNAvssqgrsKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNdf 1634
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-------ARRIRALEQELAALEAELAELEKEIAELRAELE-- 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1635 sAKQSRLEDEITTLQT-------KVLMNRNQ-------ATNVRAGAEAAYKQAQKIDNEFADIKRKYAILQDKLKAKgpp 1700
Cdd:COG4942    101 -AQKEELAELLRALYRlgrqpplALLLSPEDfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL--- 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024332955 1701 KVTLQKVKQLkeeAEKLAEETEKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESK 1769
Cdd:COG4942    177 EALLAELEEE---RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1466-1736 7.67e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.83  E-value: 7.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1466 TNLTTQLQDPENQylqVEHIRRMAEDTKLKGSHFNGELERAKNQIKIDREVTKEFIKKVKNFLSDESvppEDIEQVASY- 1544
Cdd:COG1340      4 DELSSSLEELEEK---IEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRD---ELNEKVKELk 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1545 --VLQINLPLtpRELRSMIGKIRSIMAhcesKAAKALPPVDKINDELK-------NAVSSQGRSKN-------------- 1601
Cdd:COG1340     78 eeRDELNEKL--NELREELDELRKELA----ELNKAGGSIDKLRKEIErlewrqqTEVLSPEEEKElvekikelekelek 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1602 --TLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLqtkvlmnRNQATNVRAGAEAAYKQ------- 1672
Cdd:COG1340    152 akKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL-------YKEADELRKEADELHKEiveaqek 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024332955 1673 AQKIDNEFADIKRKYAILQDKLKAKGPPKVTLQKVKQLkeeaeklaeetEKKIRRITDLEKKLQ 1736
Cdd:COG1340    225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-----------EELEEKAEEIFEKLK 277
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1582-1771 1.26e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1582 VDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQTKVLMNRNQATN 1661
Cdd:COG4372     82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1662 VRAGAEAAYKQAQKIDNEFADIKRKYAILQDKLKAKGPPKVTLQKVKQLKEEAEKLAeetEKKIRRITDLEKKLQDLNQT 1741
Cdd:COG4372    162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE---ELLEAKDSLEAKLGLALSAL 238
                          170       180       190
                   ....*....|....*....|....*....|
gi 2024332955 1742 KQDKAEQLRQLEEQVIAIKNEITEQESKYS 1771
Cdd:COG4372    239 LDALELEEDKEELLEEVILKEIEELELAIL 268
cc_LAMB3_C cd22303
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ...
1704-1774 1.56e-04

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: 41.66  E-value: 1.56e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024332955 1704 LQKVKQLKEEaekLAEETEKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKYSTCK 1774
Cdd:cd22303      4 VANIKKEAES---LFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1021-1062 1.57e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 40.76  E-value: 1.57e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 2024332955  1021 CNSNIDVTDPESCNRVTGECVkCLHNTHGANCQFCKPGYFGS 1062
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1588-1769 1.63e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1588 ELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRL-EDEITTLQTKV--------LMNRNQ 1658
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIgeleaeiaSLERSI 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1659 ATNVRAGAEAAYKQAQ------KIDNEFADIKRK---YAILQDKLKA-----KGPPKVTLQKVKQLKEEAEKLAEETEKK 1724
Cdd:TIGR02169  311 AEKERELEDAEERLAKleaeidKLLAEIEELEREieeERKRRDKLTEeyaelKEELEDLRAELEEVDKEFAETRDELKDY 390
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2024332955 1725 IRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESK 1769
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1501-1769 1.75e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1501 GELERAKNQIKIDREVTKEFIKKVKNFLSD---------------ESVPPEDIEQVASYVLQIN----------LPLTPR 1555
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSleqeienvkselkelEARIEELEEDLHKLEEALNdlearlshsrIPEIQA 798
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1556 ELRSM---IGKIRSIMAHCESKAAKALPPVDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLN 1632
Cdd:TIGR02169  799 ELSKLeeeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1633 DFSAKQSRLEDEITTLQTKVlmnRNQATNVRAgAEAAYKQAQKIDNEfadIKRKYAILQDKLKAKGPPKVTLQKVKQLKE 1712
Cdd:TIGR02169  879 DLESRLGDLKKERDELEAQL---RELERKIEE-LEAQIEKKRKRLSE---LKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024332955 1713 EAEKLAEETEKKIRRITDLE----KKLQDLNQTKQ---DKAEQLRQLEEQVIAIKNEITEQESK 1769
Cdd:TIGR02169  952 SLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKrldELKEKRAKLEEERKAILERIEEYEKK 1015
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1583-1769 2.20e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1583 DKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQTKvlMNRNQATNV 1662
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER--LANLERQLE 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1663 RAGAEAAYKQAQKIDnefadikrkyaiLQDKLKAKGPPKVTLQKVKQLKEEaeklaeetekkirRITDLEKKLQDLNQTK 1742
Cdd:TIGR02168  320 ELEAQLEELESKLDE------------LAEELAELEEKLEELKEELESLEA-------------ELEELEAELEELESRL 374
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2024332955 1743 QDKAEQLR-------QLEEQVIAIKNEITEQESK 1769
Cdd:TIGR02168  375 EELEEQLEtlrskvaQLELQIASLNNEIERLEAR 408
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
268-326 2.97e-04

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.03  E-value: 2.97e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024332955  268 CFCNGHAS---HCDPIQnlrgdvfhqpgmvhGRCICHHNTEGLSCERCKDFYNDAPWRPAEG 326
Cdd:pfam00053    1 CDCNPHGSlsdTCDPET--------------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1483-1767 3.92e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1483 EHIRRMAEDTklkgshfnGELERAKNQIKIDREVTKEFIKKVKNFLSDESVPPEDIEQVASYVLQINLPLTPR--ELRSM 1560
Cdd:TIGR02169  674 AELQRLRERL--------EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleELEED 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1561 IGKI-------RSIMAHCESKAAKALPPVDKINDELKNAVSSQGRSK-----NTLMKLNEGIQGIRAQItqagnqmNKTS 1628
Cdd:TIGR02169  746 LSSLeqeienvKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqAELSKLEEEVSRIEARL-------REIE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1629 NKLNDFSAKQSRLEDEITTLQTKVLMNRNQATNVRAGAEAAYKQAQKIDNEFADIKRKYAILQDKLKAkgppkvtLQKvk 1708
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD-------LKK-- 889
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024332955 1709 qlkeeaekLAEETEKKIRritDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQE 1767
Cdd:TIGR02169  890 --------ERDELEAQLR---ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
912-951 4.25e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.60  E-value: 4.25e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2024332955   912 CACHG---FAELCHPVTGECLnCSRFTAGSHCERCIDGYYGNP 951
Cdd:smart00180    1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
cc_LAMB2_C cd22299
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ...
1724-1774 5.97e-04

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


Pssm-ID: 411970 [Multi-domain]  Cd Length: 72  Bit Score: 40.12  E-value: 5.97e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024332955 1724 KIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKYSTCK 1774
Cdd:cd22299     22 KLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
960-1016 6.99e-04

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 39.26  E-value: 6.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955  960 CMCPGVPTSkrffAHSCyqDSQTSQivCNCLEGYSGNRCDECPSGFYKIPGSPGEEC 1016
Cdd:pfam00053    1 CDCNPHGSL----SDTC--DPETGQ--CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
bZIP_Jun cd14696
Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and ...
1723-1765 9.33e-04

Basic leucine zipper (bZIP) domain of Jun proteins and similar proteins: a DNA-binding and dimerization domain; Jun is a member of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are three Jun proteins: c-Jun, JunB, and JunD. c-Jun is the most potent transcriptional activator of the AP-1 proteins. Both c-Jun and JunB are essential during development; deletion of either results in embryonic lethality in mice. c-Jun is essential in hepatogenesis and liver erythropoiesis, while JunB is required in vasculogenesis and angiogenesis in extraembryonic tissues. While JunD is dispensable in embryonic development, it is involved in transcription regulation of target genes that help cells to cope with environmental signals. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269844 [Multi-domain]  Cd Length: 61  Bit Score: 39.10  E-value: 9.33e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024332955 1723 KKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITE 1765
Cdd:cd14696     19 RKLERIARLEDKVKELKNQNSELTSTASLLREQVCQLKQKVME 61
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
1669-1771 9.54e-04

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 41.41  E-value: 9.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1669 AYKQAQ-KIDNEFADIKRKYAILQDKLKAKgppKVTLQKVKQLKEEAeklaeeTEKKIRRITDLEKKLQDLNQTKQDKAE 1747
Cdd:pfam03938   16 EGKAAQaQLEKKFKKRQAELEAKQKELQKL---YEELQKDGALLEEE------REEKEQELQKKEQELQQLQQKAQQELQ 86
                           90       100
                   ....*....|....*....|....*...
gi 2024332955 1748 QLRQLEEQVI--AIKNEITE--QESKYS 1771
Cdd:pfam03938   87 KKQQELLQPIqdKINKAIKEvaKEKGYD 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1464-1771 1.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1464 LLTNLTTQLQDPENQYLQVEHIRRMAEDTK-----LKGSHfnGELERAKnqikidreVTKEFIKKVKNFLSDEsvPPEDI 1538
Cdd:PRK03918   322 EINGIEERIKELEEKEERLEELKKKLKELEkrleeLEERH--ELYEEAK--------AKKEELERLKKRLTGL--TPEKL 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1539 EQVASYVLQINLPLTP--RELRSMIGKIRSIM-----AHCESKAAKALPPVDK--INDELKnavssqgrsKNTLMKLNEG 1609
Cdd:PRK03918   390 EKELEELEKAKEEIEEeiSKITARIGELKKEIkelkkAIEELKKAKGKCPVCGreLTEEHR---------KELLEEYTAE 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1610 IQGIRAQITQAGNQMNKTSN---KLNDFSAKQSRLEDEITTL-QTKVLMNRNQATNVRAgAEAAYKQAQKIDNEFADIKR 1685
Cdd:PRK03918   461 LKRIEKELKEIEEKERKLRKelrELEKVLKKESELIKLKELAeQLKELEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKG 539
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1686 KYAILQDKLKAKGPPKVTLQKVKQLKEEAEKLAEETEKKIRR-----ITDLEKKLQDLN-------------QTKQDKAE 1747
Cdd:PRK03918   540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKELEpfyneylelkdaeKELEREEK 619
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2024332955 1748 QLRQLEEQVIA--------------IKNEITEQESKYS 1771
Cdd:PRK03918   620 ELKKLEEELDKafeelaetekrleeLRKELEELEKKYS 657
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
1471-1774 1.25e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 1.25e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  1471 QLQDpenqYLQVEHIRRMaEDTKLKGSHFNgeleraknqikidrevtkeFIKKVKNFLSDESVPPEDIeQVASYvlqINL 1550
Cdd:smart00787   11 SLQD----FLNMTGIRFM-ELLTTKRRHTP-------------------APAISLNRISEEDCSLDQY-VVAGY---CTV 62
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  1551 PL------TPRELRSMIGKIRSIMAHCESKAAKALPPVDK------------INDELKNaVSSQGR--SKNT----LMKL 1606
Cdd:smart00787   63 PLlelyqfSCKELKKYISEGRDLFKEIEEETLINNPPLFKeyfsaspdvkllMDKQFQL-VKTFARleAKKMwyewRMKL 141
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  1607 NEGIQ----GIRAQITQAGNQMNKTSNKLNDF----SAKQSRLEDEITTLQtkvlmnrnqatnvragaeaaykqaqKIDN 1678
Cdd:smart00787  142 LEGLKegldENLEGLKEDYKLLMKELELLNSIkpklRDRKDALEEELRQLK-------------------------QLED 196
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  1679 EFADIKRKyaiLQDKLKAKgppkvtLQKVKQLkeeaeklaeetekkirrITDLEKKLQDLNQTKQDKAEQLRQLEEQVIA 1758
Cdd:smart00787  197 ELEDCDPT---ELDRAKEK------LKKLLQE-----------------IMIKVKKLEELEEELQELESKIEDLTNKKSE 250
                           330
                    ....*....|....*.
gi 2024332955  1759 IKNEITEQESKYSTCK 1774
Cdd:smart00787  251 LNTEIAEAEKKLEQCR 266
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
1583-1696 1.28e-03

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


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 42.40  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1583 DKINDELKNAVSSQGRSKNtlmKLNEGIQGIRAQITQAGNQMNKTSNKLNDFsakQSRLEDEITTLQTKV---------- 1652
Cdd:cd21116     76 PDLIELADNLIKGDQGAKQ---QLLQGLEALQSQVTKKQTSVTSFINELTTF---KNDLDDDSRNLQTDAtkaqaqvavl 149
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024332955 1653 -LMNrNQATNVRAGAEAAYKQAQKIDNEFADIKRKYAILQDKLKA 1696
Cdd:cd21116    150 nALK-NQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLED 193
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1556-1775 1.44e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1556 ELRSMIGKIRSIMAHCESKAakalppvDKINDELKNAVSSQGRSKNtlmkLNEGIQGIRAQITQAGNQMNKTSNKLNDFS 1635
Cdd:TIGR04523   34 EEKQLEKKLKTIKNELKNKE-------KELKNLDKNLNKDEEKINN----SNNKIKILEQQIKDLNDKLKKNKDKINKLN 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1636 AKQSRLEDEITTlqtkvlmnrnqatnvragaeaayKQAQKIDNEFADIKRKYAILQDKLKAKgppkvtlqkvkqlkeeae 1715
Cdd:TIGR04523  103 SDLSKINSEIKN-----------------------DKEQKNKLEVELNKLEKQKKENKKNID------------------ 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1716 klaeeteKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQESKYSTCKS 1775
Cdd:TIGR04523  142 -------KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
282-321 1.72e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 1.72e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 2024332955   282 NLRGDVFHQPGMVHGRCICHHNTEGLSCERCKDFYNDAPW 321
Cdd:smart00180    4 DPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1459-1760 2.28e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.79  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1459 EETAVLLTNLTTQLqdpENQYLQVEHIRRMAEDTKLKgSHFNGELERAKNQiKIDREVTKEFIKKVK--NFLSDESVPPE 1536
Cdd:pfam05483  179 EETRQVYMDLNNNI---EKMILAFEELRVQAENARLE-MHFKLKEDHEKIQ-HLEEEYKKEINDKEKqvSLLLIQITEKE 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1537 DIEQVASYVLQinlpltprELRSMIGKIRSIMAHCESKAAKALPPVDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQ 1616
Cdd:pfam05483  254 NKMKDLTFLLE--------ESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1617 ITQAGNQMNKTSNKLNDFSAKQSRL--EDEITTLQTKVLMNRNQATnvragAEAAYKQAQKIDNEfadIKRKYAILQDKL 1694
Cdd:pfam05483  326 ICQLTEEKEAQMEELNKAKAAHSFVvtEFEATTCSLEELLRTEQQR-----LEKNEDQLKIITME---LQKKSSELEEMT 397
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955 1695 KAKGPPKVTLQKVKQLKEEAEKLAEEtEKKIRRITD-LEKKLQDLNQTKQDKAEQLRQLEEQVIAIK 1760
Cdd:pfam05483  398 KFKNNKEVELEELKKILAEDEKLLDE-KKQFEKIAEeLKGKEQELIFLLQAREKEIHDLEIQLTAIK 463
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
335-385 2.57e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 2.57e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2024332955   335 CNCNG---HSGRCHFDmavyqasggvsGGVCEdCQHNTTGHHCDQCKLFFYQDP 385
Cdd:smart00180    1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1588-1767 4.53e-03

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: 42.08  E-value: 4.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1588 ELKNAVSSQGRSKNTLMklnegiQGIRAQITQAGNQMNKT-----SNKLNDFSAKQSrLEDEITTLQT--KVLMNRNQAT 1660
Cdd:pfam01576  331 ELKKALEEETRSHEAQL------QEMRQKHTQALEELTEQleqakRNKANLEKAKQA-LESENAELQAelRTLQQAKQDS 403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1661 -NVRAGAEAaykQAQKIDNEFADIKRKYAILQDKLkakgppkvtlQKVKQLKEEAEKLAEETEKKIRRIT----DLEKKL 1735
Cdd:pfam01576  404 eHKRKKLEG---QLQELQARLSESERQRAELAEKL----------SKLQSELESVSSLLNEAEGKNIKLSkdvsSLESQL 470
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2024332955 1736 QDLNQTKQDKAEQ-------LRQLEEQVIAIKNEITEQE 1767
Cdd:pfam01576  471 QDTQELLQEETRQklnlstrLRQLEDERNSLQEQLEEEE 509
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1600-1765 4.61e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 4.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1600 KNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDFSAKQSRLEDEITTLQTKVLMNRNQATNVRAGAEAAYKQAQKIDNE 1679
Cdd:COG1340     14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1680 FADIKRKYailqDKLKAKGPPKVTLQK-VKQlkeeaeklaeeTEKK--------------IRRITDLEKKLQ------DL 1738
Cdd:COG1340     94 LDELRKEL----AELNKAGGSIDKLRKeIER-----------LEWRqqtevlspeeekelVEKIKELEKELEkakkalEK 158
                          170       180
                   ....*....|....*....|....*..
gi 2024332955 1739 NQTKQDKAEQLRQLEEQVIAIKNEITE 1765
Cdd:COG1340    159 NEKLKELRAELKELRKEAEEIHKKIKE 185
TNFRSF4 cd13406
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ...
921-1006 4.85e-03

Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.


Pssm-ID: 276911 [Multi-domain]  Cd Length: 142  Bit Score: 39.30  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  921 CHPVTGECLNCSRfTAGSHCERCIDGYYGNPSNREPCRPC-MCPGVPTSKRFFAHSCYQDSqtsqiVCNCLEGY------ 993
Cdd:cd13406     18 CPPGEGMESRCTG-TQDTVCSPCEPGFYNEAVNYEPCKPCtQCNQRSGSEEKQKCTKTSDT-----VCRCRPGTqpldsy 91
                           90
                   ....*....|....
gi 2024332955  994 -SGNRCDECPSGFY 1006
Cdd:cd13406     92 kPGVDCVPCPPGHF 105
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1555-1774 5.46e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 5.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1555 RELRSMIGKIRSIMAHCESKAAKALPPVDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDF 1634
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1635 SAKQSRLEDEITTLQTKVLMNRNQATNVRAgaEAAYKQAQKIDNEFADIK----RKYAILQD---KLKAKGPPKVTLQKV 1707
Cdd:TIGR02169  757 KSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEeevsRIEARLREieqKLNRLTLEKEYLEKE 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1708 KQLKEEAEKLAEETEKKIRR----------------------ITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITE 1765
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKeienlngkkeeleeeleeleaaLRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914

                   ....*....
gi 2024332955 1766 QESKYSTCK 1774
Cdd:TIGR02169  915 KRKRLSELK 923
VSP pfam03302
Giardia variant-specific surface protein;
940-1239 5.90e-03

Giardia variant-specific surface protein;


Pssm-ID: 146106 [Multi-domain]  Cd Length: 397  Bit Score: 41.11  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955  940 CERCIDGYYGNPSNREPCRPCMCPGVptskrfFAHSCYQDSQTSQ--IVCNCLEGYSGNRCDECPSGFYKipgsPGEECA 1017
Cdd:pfam03302   39 CEECNSNNYLTPTSQCIDDCAKIGNY------YYTTNANNKKICKecTVANCKTCEDQGQCQACNDGFYK----SGDACS 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1018 PC--PCNSNIDVTDPESCNRVTGECVK-------------CLHNTHGANCQFCKPGYFGSALNQDCRICKCNPA-GVLPA 1081
Cdd:pfam03302  109 PCheSCKTCSGGTASDCTECLTGKALRygndgtkgtcgegCTTGTGAGACKTCGLTIDGTSYCSECATETEYPQnGVCTS 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1082 TCPGGDATCLCDPATGAclcqpnvvgtTCDQCAPGYWDLAGGkgcqlcdcdlkntqSNQCDQLTGQCQCKVGYGGKRCDE 1161
Cdd:pfam03302  189 TAARATATCKASSVANG----------MCSSCANGYFRMNGG--------------CYETTKFPGKSVCEEANSGGTCQK 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1162 CEENYFGNP------QKHCISCNCN-----------PEGTSWPQCDKATGVCNCRAGVtgrfCDQCGRGFEKDFPSCRQC 1224
Cdd:pfam03302  245 EAPGYKLNNgdlvtcSPGCKTCTSNtvcttcmdgyvKTSDSCTKCDSSCETCTGATTT----CKTCATGYYKSGTGCVSC 320
                          330
                   ....*....|....*
gi 2024332955 1225 HLCfdEWDTEITALA 1239
Cdd:pfam03302  321 TSS--ESDNGITGVK 333
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1503-1765 8.21e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 8.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1503 LERA-KNQIKIDREVTKEfIKKVKNFLSDEsvppEDIEQVASYVLQiNLPLTPRELRSMIGKIRSIMAHCEsKAAKALPP 1581
Cdd:PRK03918   160 YENAyKNLGEVIKEIKRR-IERLEKFIKRT----ENIEELIKEKEK-ELEEVLREINEISSELPELREELE-KLEKEVKE 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1582 VDKINDELKNAVSSQGRSKNTLMKLNEGIQGIRAQITQA---------------------------GNQMNKTSNKLNDF 1634
Cdd:PRK03918   233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeleekvkelkelkekaeeyiklSEFYEEYLDELREI 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1635 SAKQSRLEDEITTLQTKVlmnrnqatnvrAGAEAAYKQAQKIDNEFADIKRKYAILQ------DKLKAKgppKVTLQKVK 1708
Cdd:PRK03918   313 EKRLSRLEEEINGIEERI-----------KELEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAK---KEELERLK 378
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024332955 1709 QLKEEAEKlaeetEKKIRRITDLEKKlqdlnqtKQDKAEQLRQLEEQVIAIKNEITE 1765
Cdd:PRK03918   379 KRLTGLTP-----EKLEKELEELEKA-------KEEIEEEISKITARIGELKKEIKE 423
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1555-1768 8.57e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 8.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1555 RELRSMIGKIRSIMAHCESKAAKAlppvDKINDELKNAVSsqgrsknTLMKLNEGIQGIRAQITQAGNQMNKTSNKLNDF 1634
Cdd:COG1196    225 LEAELLLLKLRELEAELEELEAEL----EELEAELEELEA-------ELAELEAELEELRLELEELELELEEAQAEEYEL 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024332955 1635 SAKQSRLEDEITTLQTKvlMNRNQATNVRAGAEAA--YKQAQKIDNEFADIKRKYAILQDKLKAKgppkvtLQKVKQLKE 1712
Cdd:COG1196    294 LAELARLEQDIARLEER--RRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEEA------EAELAEAEE 365
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024332955 1713 EAEKLAEETEKKIRRITDLEKKLQDLNQTKQDKAEQLRQLEEQVIAIKNEITEQES 1768
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
 
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.
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