|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1578-1833 |
3.50e-101 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
:
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 326.29 E-value: 3.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1578 VLSLN-LTGVSPAPYGILENLENTTKYFQRYLIKENAKKIRAEI---QLEGIAEQTENLQKELTRVLARHQKVNAEMERT 1653
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1654 SNGTQALATFIEQLHANIKEITEKVATLNQtarKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLL 1733
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1734 SRIQKRFQKPQEKLKALKEA-NSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEL 1812
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 148706391 1813 IAKGREWVDAAGTHTAAAQDT 1833
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
41-291 |
2.41e-94 |
|
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: 305.82 E-value: 2.41e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 41 QQRGLFPAILNLATNAHISANATCGEKGPEMFCKLVehvpGRPVRHAQCRVCDgnSTNPRERHPISHAIDGTN----NWW 116
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLV----GHTEQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 117 QSPSIQNGReyHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVDGVKFKPWQYYAvsdTECLTRYKITPRRGPPT 196
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 197 YrADNEVICTSYYSKLVPLEHGEIHTSLINGRPSADDP--SPQLLEFTSARYIRLRLQRIRTLNADLMtlshrdlrDLDP 274
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 148706391 275 IVTRRYYYSIKDISVGG 291
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2014-2148 |
1.69e-55 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
:
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 190.01 E-value: 1.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2014 ARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKT 2093
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 2094 LEEN---LSRNLSEIKLLISRARKQAASIKVAVSADRDCIRAYQPQTSSTNYNTLILN 2148
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1221-1363 |
1.63e-48 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 170.14 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1221 YWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGTGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQDYEVQMKEEFWKYf 1300
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148706391 1301 nsVSEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGRKAvelpAEGEAALLLE 1363
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG----GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
591-730 |
7.22e-44 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 156.66 E-value: 7.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 591 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSDLMSHADIIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 669
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148706391 670 DfNTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLaVAADVE 730
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2747-2876 |
3.32e-42 |
|
Laminin G domain;
:
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 151.70 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2747 IRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2826
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 2827 -VVGNATTLDVERKLYLGGLPSHYRARNIGTITHSIPACIGEIMVNGQQLD 2876
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2896-3049 |
3.46e-38 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
:
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 141.02 E-value: 3.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2896 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaar 2974
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 2975 aLCDGKWHTLQAHKSKHRIVLTVDGNAVRAESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3049
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2310-2466 |
3.78e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
:
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 138.32 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2310 SFHFDGSGYAMVEKTLRPTV-TQIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNG 2388
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 2389 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2466
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2491-2655 |
7.26e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
:
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 122.91 E-value: 7.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2491 SVSFLRGGYVEMPPKSL-SPESSLLATFATKNSSGILLVAlgkdaeeagGAQAHVPFFSIMLLEGRIEVHVNSGDGTslr 2569
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2570 kALLHAPTgSYSDGQEHSISLVRNRRVITIQVDENSPVEMKLgPLTEGKTIDISNLYIGGLPEDKATPMLKMRTSFHGCI 2649
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGS-PGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 148706391 2650 KNVVLD 2655
Cdd:cd00110 146 RDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2132-2281 |
2.88e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
:
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.59 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2132 AYQPQTSSTNYNTLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEfPEVSINNNRWHSIYITR 2211
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2212 FGNMGSLSVKeasaaENPPVRTSKSPGPskvLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2281
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGS---ALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
925-971 |
2.47e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.00 E-value: 2.47e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 925 CDCHENGSLSGVCHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGC 971
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
420-479 |
1.42e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.30 E-value: 1.42e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 420 CNCDPVGSLSSVCIKddrhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCIPCDC 479
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1512-1549 |
4.30e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 4.30e-12
10 20 30
....*....|....*....|....*....|....*...
gi 148706391 1512 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1549
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1093-1150 |
3.50e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.50e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 1093 CGCDLRGTLPDTCDLEQGlcscsedsgTCSCKENVVGPQCSKCQAGTFALRGDNPQGC 1150
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG---------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
764-812 |
1.23e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 1.23e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 148706391 764 PCECHGHAS---ECD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 812
Cdd:cd00055 1 PCDCNGHGSlsgQCDpGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1406-1452 |
2.81e-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: 57.75 E-value: 2.81e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 1406 CNCNNH---SDVCDPELGKCLsCRDHTSGDHCELCASGYYGKVTGLPGDC 1452
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
974-1018 |
2.91e-10 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.91e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 148706391 974 CNCSVEGSVSDNC-TEEGQCHCGPGVSGKQCDRCSHGFYAFQDGGC 1018
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
871-923 |
1.14e-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: 56.21 E-value: 1.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 148706391 871 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 923
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
477-523 |
2.72e-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: 2.72e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 477 CDCRTVGSLNeDPCIE---PCLCKKNVEGKNCDRCKPGFYNLKERNPEGC 523
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1021-1066 |
1.26e-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: 53.13 E-value: 1.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 148706391 1021 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPEQGCQC 1066
Cdd:pfam00053 1 CDCnphGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
814-869 |
2.48e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 2.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 148706391 814 CACPLSIDSnnfSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGGTC 869
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
293-340 |
3.07e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 3.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 293 CICYGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGT 340
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1707-2031 |
6.55e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
:
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1707 LGLIKERNFTEMQQNATLE-LKAAKDLLSRIQKRFQKPQEKLKALKE----ANSLLSNHSEKLQAAEELLKEAGSKTQES 1781
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREeleqLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1782 NLLLLLVKANLKEFQEKKLRVQEEqnvtseliakgrewvdaagthtaaaqdtLTQLEHHRDELLLWARKIRSHVDDLVMQ 1861
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEE----------------------------LEELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1862 MSKRRARdlvhraeqhASELQSRAGALDRDLENVRNvSLNATSAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLA 1941
Cdd:COG4372 145 IAEREEE---------LKELEEQLESLQEELAALEQ-ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1942 SRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDSLA-MLRESPGGMREKGRKARELAAA 2020
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdTEEEELEIAALELEALEEAALE 294
|
330
....*....|.
gi 148706391 2021 ANESAVKTLED 2031
Cdd:COG4372 295 LKLLALLLNLA 305
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1455-1509 |
1.99e-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: 46.96 E-value: 1.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 1455 CTCPHHPpfSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1509
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
731-755 |
4.93e-03 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 4.93e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1578-1833 |
3.50e-101 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 326.29 E-value: 3.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1578 VLSLN-LTGVSPAPYGILENLENTTKYFQRYLIKENAKKIRAEI---QLEGIAEQTENLQKELTRVLARHQKVNAEMERT 1653
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1654 SNGTQALATFIEQLHANIKEITEKVATLNQtarKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLL 1733
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1734 SRIQKRFQKPQEKLKALKEA-NSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEL 1812
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 148706391 1813 IAKGREWVDAAGTHTAAAQDT 1833
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
41-291 |
2.41e-94 |
|
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: 305.82 E-value: 2.41e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 41 QQRGLFPAILNLATNAHISANATCGEKGPEMFCKLVehvpGRPVRHAQCRVCDgnSTNPRERHPISHAIDGTN----NWW 116
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLV----GHTEQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 117 QSPSIQNGReyHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVDGVKFKPWQYYAvsdTECLTRYKITPRRGPPT 196
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 197 YrADNEVICTSYYSKLVPLEHGEIHTSLINGRPSADDP--SPQLLEFTSARYIRLRLQRIRTLNADLMtlshrdlrDLDP 274
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 148706391 275 IVTRRYYYSIKDISVGG 291
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
45-291 |
4.02e-86 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 281.78 E-value: 4.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 45 LFPAILNLATNAHISANATCGEKGPEMFCKLVEHVPGRpvrhaQCRVCDgnSTNPRERHPISHAIDGTNN----WWQSPS 120
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 121 IQngREYHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVD-GVKFKPWQYYAvsdTECLTRYKITPRrgPPTYRA 199
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 200 DNEVICTSYYSKLVPLEHGEIHTSLINGRPSA--DDPSPQLLEFTSARYIRLRLQRIRTLNADLMTlshrdlrdlDPIVT 277
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVL 216
|
250
....*....|....
gi 148706391 278 RRYYYSIKDISVGG 291
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2014-2148 |
1.69e-55 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 190.01 E-value: 1.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2014 ARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKT 2093
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 2094 LEEN---LSRNLSEIKLLISRARKQAASIKVAVSADRDCIRAYQPQTSSTNYNTLILN 2148
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1221-1363 |
1.63e-48 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 170.14 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1221 YWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGTGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQDYEVQMKEEFWKYf 1300
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148706391 1301 nsVSEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGRKAvelpAEGEAALLLE 1363
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG----GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
591-730 |
7.22e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 156.66 E-value: 7.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 591 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSDLMSHADIIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 669
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148706391 670 DfNTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLaVAADVE 730
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
588-718 |
1.16e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 155.88 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 588 STYYWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETVdsdLMSHADIIIKGNGLTISTRAEGlSLQPYEEYFNVVRLVPEN 667
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGT---HVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 668 FRDFNtRREIDRDQLMTVLANVTHLLIRANYnSAKMALYRLDSVSLDIASP 718
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATY-SQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2747-2876 |
3.32e-42 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 151.70 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2747 IRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2826
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 2827 -VVGNATTLDVERKLYLGGLPSHYRARNIGTITHSIPACIGEIMVNGQQLD 2876
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
1217-1347 |
5.99e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.10 E-value: 5.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1217 AEPFYWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGtGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQdyEVQMKEEF 1296
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLRISHPAEGPPLPDELTTV--EVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 1297 WKYFNsvsEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGR 1347
Cdd:smart00281 79 WQYYG---GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2896-3049 |
3.46e-38 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 141.02 E-value: 3.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2896 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaar 2974
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 2975 aLCDGKWHTLQAHKSKHRIVLTVDGNAVRAESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3049
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2310-2466 |
3.78e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 138.32 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2310 SFHFDGSGYAMVEKTLRPTV-TQIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNG 2388
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 2389 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2466
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2919-3051 |
2.79e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.08 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2919 NITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTV 2997
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP---LNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 2998 DG-NAVRAESPHTHsTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRLSR 3051
Cdd:smart00282 78 DGgNRVSGESPGGL-TILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2720-2871 |
7.49e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 131.77 E-value: 7.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2720 FGLSQNSHLVLPlNQSDVRKRLQVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDG 2799
Cdd:cd00110 2 VSFSGSSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148706391 2800 KWHTVKTEYIKRKAFMTVDGQESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVN 2871
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP-GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2742-2873 |
1.97e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 126.69 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2742 QVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPAL-LSDGKWHTVKTEYIKRKAFMTVDGQ 2820
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 148706391 2821 ESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVNGQ 2873
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-PLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2331-2468 |
7.74e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.14 E-value: 7.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2331 QIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfda 2409
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTsDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2410 ydtsDKETKQ-GETPGAASDLNRleKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEISR 2468
Cdd:smart00282 78 ----DGGNRVsGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2491-2655 |
7.26e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 122.91 E-value: 7.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2491 SVSFLRGGYVEMPPKSL-SPESSLLATFATKNSSGILLVAlgkdaeeagGAQAHVPFFSIMLLEGRIEVHVNSGDGTslr 2569
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2570 kALLHAPTgSYSDGQEHSISLVRNRRVITIQVDENSPVEMKLgPLTEGKTIDISNLYIGGLPEDKATPMLKMRTSFHGCI 2649
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGS-PGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 148706391 2650 KNVVLD 2655
Cdd:cd00110 146 RDLKVN 151
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2336-2468 |
1.22e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 115.88 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2336 FSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtSDK 2415
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV------DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 2416 ETKQGETP-GAASDLNrlEKDLIYVGGLPHSKAVRK-GVSSRSYVGCIKNLEISR 2468
Cdd:pfam00054 75 ARPTGESPlGATTDLD--VDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNG 127
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2924-3049 |
1.81e-29 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 115.21 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2924 FRTTSKNGVLLGISSAKVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTVDGNAVR 3003
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN---LNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 148706391 3004 AESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3049
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2132-2281 |
2.88e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.59 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2132 AYQPQTSSTNYNTLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEfPEVSINNNRWHSIYITR 2211
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2212 FGNMGSLSVKeasaaENPPVRTSKSPGPskvLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2281
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGS---ALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2144-2283 |
3.60e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 114.74 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2144 TLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVSINNNRWHSIYITRFGNMGSLSVkea 2223
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2224 saaENPPVRTSKSPGPSKVLDINnsTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2283
Cdd:smart00282 78 ---DGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2149-2286 |
1.70e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 109.71 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2149 VKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVsINNNRWHSIYITRFGNMGSLSVkeasaAEN 2228
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV-----DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 2229 PPVRTSKSPGPSKVLDINnsTLMFVGGLGGQI-KKSPAVKVTHFKGCMGEAFLNGKSIG 2286
Cdd:pfam00054 75 ARPTGESPLGATTDLDVD--GPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2516-2655 |
1.94e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.74 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2516 TFATKNSSGILLVALGKDaeeaggaqaHVPFFSIMLLEGRIEVHVNSGDGTslrkALLHAPTGSYSDGQEHSISLVRNRR 2595
Cdd:smart00282 5 SFRTTSPNGLLLYAGSKG---------GGDYLALELRDGRLVLRYDLGSGP----ARLTSDPTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2596 VITIQVDENSPVEMKLGPLTEGKTIDiSNLYIGGLPEDKATPMLKMRTSFHGCIKNVVLD 2655
Cdd:smart00282 72 SVTLSVDGGNRVSGESPGGLTILNLD-GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2517-2660 |
3.25e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 108.94 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2517 FATKNSSGILLValgkdaeeaGGAQAHVPFFSIMLLEGRIEVHVNSGDGtslrKALLHAPTGsYSDGQEHSISLVRNRRV 2596
Cdd:pfam00054 1 FRTTEPSGLLLY---------NGTQTERDFLALELRDGRLEVSYDLGSG----AAVVRSGDK-LNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148706391 2597 ITIQVDENSPV--EMKLGPLTEGKTIDisNLYIGGLPEDKATPMLK-MRTSFHGCIKNVVLDAQLLD 2660
Cdd:pfam00054 67 GTLSVDGEARPtgESPLGATTDLDVDG--PLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
925-971 |
2.47e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.00 E-value: 2.47e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 925 CDCHENGSLSGVCHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGC 971
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1594-2125 |
5.86e-15 |
|
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: 82.03 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1594 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKE 1673
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1674 ITEKVATLN---QTARKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLlsriQKRFQKPQEKLKAL 1750
Cdd:TIGR02168 391 LELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL----QEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1751 KEANSLLsnhSEKLQAAEELLKEAGSKTqesnLLLLLVKANLKEFQEKKLRVQEEQN-------VTSELIAKGREW---V 1820
Cdd:TIGR02168 467 REELEEA---EQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISVDEGYeaaI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1821 DAA-GTHTAA-----------AQDTLTQLEHHRDELL----LWARKIRShvDDLVMQMSKRRARDLVHRAEQHASELQ-- 1882
Cdd:TIGR02168 540 EAAlGGRLQAvvvenlnaakkAIAFLKQNELGRVTFLpldsIKGTEIQG--NDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1883 ------------SRAGALD---RDLENVRNVSLN-----------------ATSAAHVHSNIQTLTEEAEMLAADAHKTA 1930
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALElakKLRPGYRIVTLDgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1931 NKTDLISESLASRGKAVLQRssrfLKESVSTRRKQQGITMKLDELKNLTSQFQESMDnimkQANDSLAMLRESPGGMREK 2010
Cdd:TIGR02168 698 KALAELRKELEELEEELEQL----RKELEELSRQISALRKDLARLEAEVEQLEERIA----QLSKELTELEAEIEELEER 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2011 GRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKP 2090
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
570 580 590
....*....|....*....|....*....|....*
gi 148706391 2091 LKTLEENLSRNLSEIKLLISRARKQAASIKVAVSA 2125
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
924-972 |
6.98e-15 |
|
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: 70.85 E-value: 6.98e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 924 ACDCHENGSLSGVCHLETGLCDCKPHVTGQQCDQCLSGYYGLDT-GLGCV 972
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
925-971 |
1.80e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 69.65 E-value: 1.80e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 925 CDCHENGSLSGVCHLETGLCDCKPHVTGQQCDQCLSGYYGlDTGLGC 971
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
420-479 |
1.42e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.30 E-value: 1.42e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 420 CNCDPVGSLSSVCIKddrhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCIPCDC 479
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1512-1549 |
4.30e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 4.30e-12
10 20 30
....*....|....*....|....*....|....*...
gi 148706391 1512 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1549
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1512-1549 |
6.15e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 6.15e-12
10 20 30
....*....|....*....|....*....|....*...
gi 148706391 1512 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1549
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1512-1549 |
7.81e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.81e-12
10 20 30
....*....|....*....|....*....|....*...
gi 148706391 1512 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1549
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1093-1150 |
3.50e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.50e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 1093 CGCDLRGTLPDTCDLEQGlcscsedsgTCSCKENVVGPQCSKCQAGTFALRGDNPQGC 1150
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG---------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
764-812 |
1.23e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 1.23e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 148706391 764 PCECHGHAS---ECD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 812
Cdd:cd00055 1 PCDCNGHGSlsgQCDpGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1406-1452 |
2.81e-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: 57.75 E-value: 2.81e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 1406 CNCNNH---SDVCDPELGKCLsCRDHTSGDHCELCASGYYGKVTGLPGDC 1452
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
974-1018 |
2.91e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.91e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 148706391 974 CNCSVEGSVSDNC-TEEGQCHCGPGVSGKQCDRCSHGFYAFQDGGC 1018
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
419-472 |
5.65e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 5.65e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 148706391 419 PCNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRGFP 472
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT-----------GQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
974-1021 |
6.26e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 6.26e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 148706391 974 CNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFYAFQDGGCTPC 1021
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
871-923 |
1.14e-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: 56.21 E-value: 1.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 148706391 871 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 923
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1594-2120 |
1.50e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1594 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNG-------TQALATFIEQ 1666
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarleerRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1667 LHANIKEITEKVATLNQTARkdfqppvsALQSMHQNISSLLGLIKErnftEMQQNATLELKAAKDLLSRIQKRFQKPQEK 1746
Cdd:COG1196 321 LEEELAELEEELEELEEELE--------ELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1747 LKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREwvdaAGTH 1826
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1827 TAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQ--SRAGALDRDLENVRNVSLnATS 1904
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAAL-EAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1905 AAHVHSNIQTLTEEAEMLAADAHKTANK---TDLISESLASRGKAVLQRSSRFLKESV----STRRKQQGITMKLDELKN 1977
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVdlvaSDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1978 LTSQFQESMDNIMKQAND--------SLAMLRESPGGMREKGRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRV 2049
Cdd:COG1196 624 GRTLVAARLEAALRRAVTlagrlrevTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148706391 2050 NATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIkLLISRARKQAASIK 2120
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLE 773
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
872-918 |
1.97e-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: 1.97e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 872 CNCSGNVDPleAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVT 918
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
477-523 |
2.72e-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: 2.72e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 477 CDCRTVGSLNeDPCIE---PCLCKKNVEGKNCDRCKPGFYNLKERNPEGC 523
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1405-1453 |
3.59e-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: 54.67 E-value: 3.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 148706391 1405 PCNCNNHSDV---CDPELGKCLsCRDHTSGDHCELCASGYYGkVTGLPGDCT 1453
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1093-1150 |
4.08e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 4.08e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 1093 CGCDLRGTLPDTCDLeqglcscseDSGTCSCKENVVGPQCSKCQAGTFalrGDNPQGC 1150
Cdd:smart00180 1 CDCDPGGSASGTCDP---------DTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
765-811 |
6.06e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.90 E-value: 6.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 765 CECHGHAS---ECDIH-GICsVCTHNTTGDHCEQCLPGFYGTPSrGTPGDC 811
Cdd:pfam00053 1 CDCNPHGSlsdTCDPEtGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
973-1019 |
8.42e-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: 53.51 E-value: 8.42e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 973 PCNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFY--AFQDGGCT 1019
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYglPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
420-474 |
1.14e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148706391 420 CNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRG--FPNC 474
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1021-1066 |
1.26e-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: 53.13 E-value: 1.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 148706391 1021 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPEQGCQC 1066
Cdd:pfam00053 1 CDCnphGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1020-1065 |
1.46e-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: 53.13 E-value: 1.46e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 1020 PCDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPE-QGCQ 1065
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
814-869 |
2.48e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 2.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 148706391 814 CACPLSIDSnnfSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGGTC 869
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
293-340 |
3.07e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 3.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 293 CICYGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGT 340
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1021-1064 |
5.85e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 5.85e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 1021 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGlDPEQGC 1064
Cdd:smart00180 1 CDCdpgGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1609-2134 |
6.49e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1609 IKENAKKIRAEIQ-LEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITE--KVATLNQTA 1685
Cdd:PRK03918 219 LREELEKLEKEVKeLEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1686 RKDFQPPVSALQSMHQNISSLLGLIK--ERNFTEmqqnatLELKAAKdlLSRIQKRFQKPQEKLKALKEANSLLSNHSEK 1763
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINgiEERIKE------LEEKEER--LEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1764 LQAAEELLKEAGSKTQESnlllllVKANLKEFQEKKLRVQEEqnvTSELIAKGREWVDAAGTHTAA------AQDT---- 1833
Cdd:PRK03918 371 KEELERLKKRLTGLTPEK------LEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAieelkkAKGKcpvc 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1834 ---LTqlEHHRDELLlwarkirshvddlvmqmskRRARDLVHRAEQHASELQSRAGALDRDLENVRNVslnatsaahvhs 1910
Cdd:PRK03918 442 greLT--EEHRKELL-------------------EEYTAELKRIEKELKEIEEKERKLRKELRELEKV------------ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1911 niqtLTEEAEMLAadAHKTANKTDLISESLASRGKAVLQRSS---RFLKESVSTRRKQQGITM----KLDELKNLTSQFQ 1983
Cdd:PRK03918 489 ----LKKESELIK--LKELAEQLKELEEKLKKYNLEELEKKAeeyEKLKEKLIKLKGEIKSLKkeleKLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1984 ESMDNIMKQANDSLAMLRE-SPGGMREKGRKARELAAAANE-----SAVKTLEDVL----ALSLRVFNTSEDLSRVNATV 2053
Cdd:PRK03918 563 KKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEylelkDAEKELEREEkelkKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2054 QET----NDLLHN-STMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKL---LISRARKQAASIKVA--- 2122
Cdd:PRK03918 643 EELrkelEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEeleEREKAKKELEKLEKAler 722
|
570
....*....|..
gi 148706391 2123 VSADRDCIRAYQ 2134
Cdd:PRK03918 723 VEELREKVKKYK 734
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1092-1150 |
7.40e-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: 7.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 1092 PCGCDLRGTLPDTCDLEqglcscsedSGTCSCKENVVGPQCSKCQAGTFALRgDNPQGC 1150
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
476-523 |
9.37e-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: 9.37e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 476 PCDCRTVGSLNEDpCIEP---CLCKKNVEGKNCDRCKPGFYNLKERnPEGC 523
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGtgqCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1406-1452 |
1.51e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 1406 CNCN---NHSDVCDPELGKCLsCRDHTSGDHCELCASGYYGKVtglPGDC 1452
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
765-806 |
6.14e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 6.14e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 148706391 765 CECH--GHASE-CD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRG 806
Cdd:smart00180 1 CDCDpgGSASGtCDpDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1707-2031 |
6.55e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1707 LGLIKERNFTEMQQNATLE-LKAAKDLLSRIQKRFQKPQEKLKALKE----ANSLLSNHSEKLQAAEELLKEAGSKTQES 1781
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREeleqLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1782 NLLLLLVKANLKEFQEKKLRVQEEqnvtseliakgrewvdaagthtaaaqdtLTQLEHHRDELLLWARKIRSHVDDLVMQ 1861
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEE----------------------------LEELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1862 MSKRRARdlvhraeqhASELQSRAGALDRDLENVRNvSLNATSAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLA 1941
Cdd:COG4372 145 IAEREEE---------LKELEEQLESLQEELAALEQ-ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1942 SRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDSLA-MLRESPGGMREKGRKARELAAA 2020
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdTEEEELEIAALELEALEEAALE 294
|
330
....*....|.
gi 148706391 2021 ANESAVKTLED 2031
Cdd:COG4372 295 LKLLALLLNLA 305
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
477-523 |
8.66e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 8.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 477 CDCRTVGSLNeDPCIEP---CLCKKNVEGKNCDRCKPGFYNlkeRNPEGC 523
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
871-915 |
1.61e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.61e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 148706391 871 PCNCSGNVDPleagHCDSVTGECLkCLWNTDGAHCERCADGFYGD 915
Cdd:smart00180 2 DCDPGGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1455-1509 |
1.99e-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: 46.96 E-value: 1.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 1455 CTCPHHPpfSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1509
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1597-2129 |
3.87e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.13 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1597 LENTTKYFQ-RYLIKENAKKiraeiQLEGIAEQT-ENLQKELTRVLARHQKVNAEMERTSNGTQALatfIEQLHANIKEI 1674
Cdd:TIGR00606 267 LDNEIKALKsRKKQMEKDNS-----ELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1675 T-EKVATLNQTARKDFQPPVSALQSMHQNISSL-LGLIKERNFTEMQQNATLELKAAKDLLSRIQKRfqkpqeklKAlKE 1752
Cdd:TIGR00606 339 NqEKTELLVEQGRLQLQADRHQEHIRARDSLIQsLATRLELDGFERGPFSERQIKNFHTLVIERQED--------EA-KT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1753 ANSLLSNhsekLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKlrVQEEQNVTSELiakgrewvdaagthtaaaqd 1832
Cdd:TIGR00606 410 AAQLCAD----LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK--QEELKFVIKEL-------------------- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1833 tlTQLEHHRDELLLWARKIRSHVDDLvmqmSKRRARDLVHRAEQHASELQSRAGALDRDL--ENVRNVSLNAtsaaHVHS 1910
Cdd:TIGR00606 464 --QQLEGSSDRILELDQELRKAEREL----SKAEKNSLTETLKKEVKSLQNEKADLDRKLrkLDQEMEQLNH----HTTT 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1911 NIQTLTEEAEMLAADAHKTANK----------------TDLISESLASRGKAVLQRSSRFLKESVSTRRKQQGITMKLDE 1974
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQIRKIKsrhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1975 LKNLTSQFQESMDNIMK----QANDS-LAMLRESpggmREKGRKARE-LAAAAN--ESAVKTLED----VLALSLRVFNT 2042
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDvcgsQDEESdLERLKEE----IEKSSKQRAmLAGATAvySQFITQLTDenqsCCPVCQRVFQT 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2043 SEDLSRVNATVQETNDLL---HNSTMTTLLAGRKMKD-----MEMQANLLLDRLKPLKTLEE---NLSRNLSEIKLLISR 2111
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLApdkLKSTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNklqKVNRDIQRLKNDIEE 769
|
570
....*....|....*...
gi 148706391 2112 ARKQAASIKVAVSADRDC 2129
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVC 787
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
813-867 |
5.27e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.81 E-value: 5.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 813 PCACPLSIDSNnfsPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGG 867
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTG---QC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1834-2088 |
6.18e-06 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 50.49 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1834 LTQLEHHRDELLLWARKIRSHVDDlvMQMSKRRARDLvhraEQHASELQSRAGALDRDLENVRNVSlNATSaahvhSNIQ 1913
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQ--IEILEKELSSL----AQETEELQKKATQTLAKAQQVNAES-ERTL-----GHAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1914 TLTEEAEMLAADAHKTANKTDLISE--SLASRGK--AVLQRSSRFLKE--SVSTRRKQQGITMKLDELKNLTSQFQESMD 1987
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGEndFALPSSDlsRMLAEAQRMLGEirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1988 NIMKQANDSLAMLRESPGGMREKGRKARELaaaANESAVKTlEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNstmtT 2067
Cdd:pfam06008 166 SPQEENKALANALRDSLAEYEAKLSDLREL---LREAAAKT-RDANRLNLANQANLREFQRKKEEVSEQKNQLEE----T 237
|
250 260
....*....|....*....|.
gi 148706391 2068 LLAGRkmkDMEMQANLLLDRL 2088
Cdd:pfam06008 238 LKTAR---DSLDAANLLLQEI 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1454-1510 |
1.43e-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: 44.65 E-value: 1.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148706391 1454 PCTCPHHPpfSFSPTCVVEgdsDFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGsCQ 1510
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
732-926 |
1.80e-05 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 47.30 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 732 CECPQGY---TGTSCEACLPGyyrvdgilfggicqpcechghasecdiHGICSVCTHNTTGdhCEQCLPGFYGTPSRGTP 808
Cdd:cd13416 1 EACPSGQytsSGECCEQCPPG---------------------------EGVARPCGDNQTV--CEPCLDGVTFSDVVSHT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 809 GDCQPCA-CPLSIdsnnfSPTCHLTDGEEVVCdqcapgysgswceRCADGYYgnPTVPGGTCVPCNCsgnvdpleaghCD 887
Cdd:cd13416 52 EPCQPCTrCPGLM-----SMRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCEPCTV-----------CP 100
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148706391 888 SVTGECLKCLWNTDgAHCERCADGFYGDAVTAKN----CRACD 926
Cdd:cd13416 101 PGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDpclpCTVCE 142
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
814-862 |
3.17e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.45 E-value: 3.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 148706391 814 CACPLSidsNNFSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNP 862
Cdd:smart00180 1 CDCDPG---GSASGTCDPDTG---QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
293-336 |
8.73e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 8.73e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 293 CICY--GHAS-SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPW 336
Cdd:smart00180 1 CDCDpgGSASgTC----DPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1609-2120 |
3.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1609 IKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNgtqalatFIEQLHANIKEITEKVATLNQTA--R 1686
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE-------EINGIEERIKELEEKEERLEELKkkL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1687 KDFQPPVSALQSMHQNISSLLGLIKE-RNFTEMQQNATLElKAAKDLLSrIQKRFQKPQEKLKALKEANSLLSNHSEKLQ 1765
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEElERLKKRLTGLTPE-KLEKELEE-LEKAKEEIEEEISKITARIGELKKEIKELK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1766 AAEELLKEAGSK--------TQESNLL--------LLLVKANLKEF--QEKKLRVqEEQNVTSELiakgrewvdaagtht 1827
Cdd:PRK03918 426 KAIEELKKAKGKcpvcgrelTEEHRKElleeytaeLKRIEKELKEIeeKERKLRK-ELRELEKVL--------------- 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1828 aAAQDTLTQLEHHRDELllwaRKIRSHVDDLVMQMSKRRARDLvHRAEQHASELQSRAGALDRDLEnvRNVSLNATSAAh 1907
Cdd:PRK03918 490 -KKESELIKLKELAEQL----KELEEKLKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELE--KLEELKKKLAE- 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1908 VHSNIQTLTEE-AEMLaadaHKTANKTDLISESLASRgkavLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESM 1986
Cdd:PRK03918 561 LEKKLDELEEElAELL----KELEELGFESVEELEER----LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1987 DNIMKQANDsLAMLREspggmrekgrKARELAAAANESAVKTLEDvLALSLrvfntSEDLSRVNATVQETNDLLhNSTMT 2066
Cdd:PRK03918 633 EELAETEKR-LEELRK----------ELEELEKKYSEEEYEELRE-EYLEL-----SRELAGLRAELEELEKRR-EEIKK 694
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 148706391 2067 TLlagrkmKDMEMQanllLDRLKPLKTLEENLSRNLSEIKLLISRARKQAASIK 2120
Cdd:PRK03918 695 TL------EKLKEE----LEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1455-1502 |
1.05e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 148706391 1455 CTCphHPPFSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNP 1502
Cdd:smart00180 1 CDC--DPGGSASGTCDPDT---GQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
293-339 |
2.03e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.49 E-value: 2.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 293 CICYGHASSCPwDEEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPG 339
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
731-755 |
4.93e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 4.93e-03
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
731-763 |
8.09e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 36.95 E-value: 8.09e-03
10 20 30
....*....|....*....|....*....|...
gi 148706391 731 HCECPQGYTGTSCEACLPGYYRVDGILFGgiCQ 763
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1578-1833 |
3.50e-101 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 326.29 E-value: 3.50e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1578 VLSLN-LTGVSPAPYGILENLENTTKYFQRYLIKENAKKIRAEI---QLEGIAEQTENLQKELTRVLARHQKVNAEMERT 1653
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1654 SNGTQALATFIEQLHANIKEITEKVATLNQtarKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLL 1733
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1734 SRIQKRFQKPQEKLKALKEA-NSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEL 1812
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 148706391 1813 IAKGREWVDAAGTHTAAAQDT 1833
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
41-291 |
2.41e-94 |
|
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: 305.82 E-value: 2.41e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 41 QQRGLFPAILNLATNAHISANATCGEKGPEMFCKLVehvpGRPVRHAQCRVCDgnSTNPRERHPISHAIDGTN----NWW 116
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLV----GHTEQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 117 QSPSIQNGReyHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVDGVKFKPWQYYAvsdTECLTRYKITPRRGPPT 196
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 197 YrADNEVICTSYYSKLVPLEHGEIHTSLINGRPSADDP--SPQLLEFTSARYIRLRLQRIRTLNADLMtlshrdlrDLDP 274
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 148706391 275 IVTRRYYYSIKDISVGG 291
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
45-291 |
4.02e-86 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 281.78 E-value: 4.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 45 LFPAILNLATNAHISANATCGEKGPEMFCKLVEHVPGRpvrhaQCRVCDgnSTNPRERHPISHAIDGTNN----WWQSPS 120
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 121 IQngREYHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVD-GVKFKPWQYYAvsdTECLTRYKITPRrgPPTYRA 199
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 200 DNEVICTSYYSKLVPLEHGEIHTSLINGRPSA--DDPSPQLLEFTSARYIRLRLQRIRTLNADLMTlshrdlrdlDPIVT 277
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVL 216
|
250
....*....|....
gi 148706391 278 RRYYYSIKDISVGG 291
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2014-2148 |
1.69e-55 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 190.01 E-value: 1.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2014 ARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKT 2093
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 2094 LEEN---LSRNLSEIKLLISRARKQAASIKVAVSADRDCIRAYQPQTSSTNYNTLILN 2148
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1221-1363 |
1.63e-48 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 170.14 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1221 YWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGTGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQDYEVQMKEEFWKYf 1300
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148706391 1301 nsVSEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGRKAvelpAEGEAALLLE 1363
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG----GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
591-730 |
7.22e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 156.66 E-value: 7.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 591 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSDLMSHADIIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 669
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148706391 670 DfNTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLaVAADVE 730
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
588-718 |
1.16e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 155.88 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 588 STYYWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETVdsdLMSHADIIIKGNGLTISTRAEGlSLQPYEEYFNVVRLVPEN 667
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGT---HVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 668 FRDFNtRREIDRDQLMTVLANVTHLLIRANYnSAKMALYRLDSVSLDIASP 718
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATY-SQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2747-2876 |
3.32e-42 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 151.70 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2747 IRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2826
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 2827 -VVGNATTLDVERKLYLGGLPSHYRARNIGTITHSIPACIGEIMVNGQQLD 2876
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
1217-1347 |
5.99e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.10 E-value: 5.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1217 AEPFYWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGtGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQdyEVQMKEEF 1296
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLRISHPAEGPPLPDELTTV--EVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 1297 WKYFNsvsEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGR 1347
Cdd:smart00281 79 WQYYG---GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2896-3049 |
3.46e-38 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 141.02 E-value: 3.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2896 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaar 2974
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 2975 aLCDGKWHTLQAHKSKHRIVLTVDGNAVRAESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3049
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2310-2466 |
3.78e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 138.32 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2310 SFHFDGSGYAMVEKTLRPTV-TQIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNG 2388
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 2389 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2466
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2919-3051 |
2.79e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.08 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2919 NITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTV 2997
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP---LNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 2998 DG-NAVRAESPHTHsTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRLSR 3051
Cdd:smart00282 78 DGgNRVSGESPGGL-TILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2720-2871 |
7.49e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 131.77 E-value: 7.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2720 FGLSQNSHLVLPlNQSDVRKRLQVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDG 2799
Cdd:cd00110 2 VSFSGSSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148706391 2800 KWHTVKTEYIKRKAFMTVDGQESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVN 2871
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP-GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2742-2873 |
1.97e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 126.69 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2742 QVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPAL-LSDGKWHTVKTEYIKRKAFMTVDGQ 2820
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 148706391 2821 ESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVNGQ 2873
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-PLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2331-2468 |
7.74e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.14 E-value: 7.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2331 QIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfda 2409
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTsDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2410 ydtsDKETKQ-GETPGAASDLNRleKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEISR 2468
Cdd:smart00282 78 ----DGGNRVsGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2491-2655 |
7.26e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 122.91 E-value: 7.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2491 SVSFLRGGYVEMPPKSL-SPESSLLATFATKNSSGILLVAlgkdaeeagGAQAHVPFFSIMLLEGRIEVHVNSGDGTslr 2569
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2570 kALLHAPTgSYSDGQEHSISLVRNRRVITIQVDENSPVEMKLgPLTEGKTIDISNLYIGGLPEDKATPMLKMRTSFHGCI 2649
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGS-PGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 148706391 2650 KNVVLD 2655
Cdd:cd00110 146 RDLKVN 151
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2336-2468 |
1.22e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 115.88 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2336 FSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtSDK 2415
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV------DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 2416 ETKQGETP-GAASDLNrlEKDLIYVGGLPHSKAVRK-GVSSRSYVGCIKNLEISR 2468
Cdd:pfam00054 75 ARPTGESPlGATTDLD--VDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNG 127
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2924-3049 |
1.81e-29 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 115.21 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2924 FRTTSKNGVLLGISSAKVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTVDGNAVR 3003
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN---LNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 148706391 3004 AESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3049
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2132-2281 |
2.88e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.59 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2132 AYQPQTSSTNYNTLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEfPEVSINNNRWHSIYITR 2211
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2212 FGNMGSLSVKeasaaENPPVRTSKSPGPskvLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2281
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGS---ALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2144-2283 |
3.60e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 114.74 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2144 TLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVSINNNRWHSIYITRFGNMGSLSVkea 2223
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2224 saaENPPVRTSKSPGPSKVLDINnsTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2283
Cdd:smart00282 78 ---DGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2924-3054 |
4.61e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 114.34 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2924 FRTTSKNGVLL-GISSAKVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaaraLCDGKWHTLQAHKSKHRIVLTVDGNAV 3002
Cdd:pfam00054 1 FRTTEPSGLLLyNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK----LNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 148706391 3003 -RAESPHTHSTSADTNDPIYVGGYPAHIKQN-CLSSRASFRGCVRNLRLSRGSQ 3054
Cdd:pfam00054 77 pTGESPLGATTDLDVDGPLYVGGLPSLGVKKrRLAISPSFDGCIRDVIVNGKPL 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2149-2286 |
1.70e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 109.71 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2149 VKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVsINNNRWHSIYITRFGNMGSLSVkeasaAEN 2228
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV-----DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 2229 PPVRTSKSPGPSKVLDINnsTLMFVGGLGGQI-KKSPAVKVTHFKGCMGEAFLNGKSIG 2286
Cdd:pfam00054 75 ARPTGESPLGATTDLDVD--GPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2516-2655 |
1.94e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.74 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2516 TFATKNSSGILLVALGKDaeeaggaqaHVPFFSIMLLEGRIEVHVNSGDGTslrkALLHAPTGSYSDGQEHSISLVRNRR 2595
Cdd:smart00282 5 SFRTTSPNGLLLYAGSKG---------GGDYLALELRDGRLVLRYDLGSGP----ARLTSDPTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2596 VITIQVDENSPVEMKLGPLTEGKTIDiSNLYIGGLPEDKATPMLKMRTSFHGCIKNVVLD 2655
Cdd:smart00282 72 SVTLSVDGGNRVSGESPGGLTILNLD-GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2517-2660 |
3.25e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 108.94 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2517 FATKNSSGILLValgkdaeeaGGAQAHVPFFSIMLLEGRIEVHVNSGDGtslrKALLHAPTGsYSDGQEHSISLVRNRRV 2596
Cdd:pfam00054 1 FRTTEPSGLLLY---------NGTQTERDFLALELRDGRLEVSYDLGSG----AAVVRSGDK-LNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148706391 2597 ITIQVDENSPV--EMKLGPLTEGKTIDisNLYIGGLPEDKATPMLK-MRTSFHGCIKNVVLDAQLLD 2660
Cdd:pfam00054 67 GTLSVDGEARPtgESPLGATTDLDVDG--PLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2336-2466 |
1.55e-26 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 106.74 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2336 FSTFSPNGLLFYlASNGTKDFLSIELVRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtsD 2414
Cdd:pfam02210 1 FRTRQPNGLLLY-AGGGGSDFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTLSV-------D 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 148706391 2415 KETKQGETPGAASDLNRLEKDLiYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2466
Cdd:pfam02210 73 GQTVVSSLPPGESLLLNLNGPL-YLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2517-2657 |
9.59e-23 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 95.95 E-value: 9.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2517 FATKNSSGILLVALGKDAEeaggaqahvpFFSIMLLEGRIEVHVNSGDGTslrkALLHAPTGSYSDGQEHSISLVRNRRV 2596
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD----------FLALELVNGRLVLRYDLGSGP----ESLLSSGKNLNDGQWHSVRVERNGNT 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148706391 2597 ITIQVDENSPVEMKLGPLTEGKTIDiSNLYIGGLPEDKATPMLKMRTSFHGCIKNVVLDAQ 2657
Cdd:pfam02210 67 LTLSVDGQTVVSSLPPGESLLLNLN-GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2149-2283 |
1.73e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 95.18 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2149 VKTQEPDNLLFYLGSSSSsDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVSINNNRWHSIYITRFGNMGSLSVKEasaaen 2228
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDG------ 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 2229 ppVRTSKSPGPSKVLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2283
Cdd:pfam02210 74 --QTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2747-2873 |
2.29e-21 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 92.10 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2747 IRTFASSGLIYYVAHQNQmDYATLQLQEGRLHFMFDLGKGRTKV-SHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSV 2825
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLlSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 148706391 2826 TVVGNATTLDVERKLYLGGLPSHYRARNIGTiTHSIPACIGEIMVNGQ 2873
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPV-RAGFVGCIRDVRVNGE 126
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
925-971 |
2.47e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.00 E-value: 2.47e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 925 CDCHENGSLSGVCHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGC 971
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1594-2125 |
5.86e-15 |
|
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: 82.03 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1594 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKE 1673
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1674 ITEKVATLN---QTARKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLlsriQKRFQKPQEKLKAL 1750
Cdd:TIGR02168 391 LELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL----QEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1751 KEANSLLsnhSEKLQAAEELLKEAGSKTqesnLLLLLVKANLKEFQEKKLRVQEEQN-------VTSELIAKGREW---V 1820
Cdd:TIGR02168 467 REELEEA---EQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISVDEGYeaaI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1821 DAA-GTHTAA-----------AQDTLTQLEHHRDELL----LWARKIRShvDDLVMQMSKRRARDLVHRAEQHASELQ-- 1882
Cdd:TIGR02168 540 EAAlGGRLQAvvvenlnaakkAIAFLKQNELGRVTFLpldsIKGTEIQG--NDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1883 ------------SRAGALD---RDLENVRNVSLN-----------------ATSAAHVHSNIQTLTEEAEMLAADAHKTA 1930
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALElakKLRPGYRIVTLDgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1931 NKTDLISESLASRGKAVLQRssrfLKESVSTRRKQQGITMKLDELKNLTSQFQESMDnimkQANDSLAMLRESPGGMREK 2010
Cdd:TIGR02168 698 KALAELRKELEELEEELEQL----RKELEELSRQISALRKDLARLEAEVEQLEERIA----QLSKELTELEAEIEELEER 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2011 GRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKP 2090
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
570 580 590
....*....|....*....|....*....|....*
gi 148706391 2091 LKTLEENLSRNLSEIKLLISRARKQAASIKVAVSA 2125
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
924-972 |
6.98e-15 |
|
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: 70.85 E-value: 6.98e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 924 ACDCHENGSLSGVCHLETGLCDCKPHVTGQQCDQCLSGYYGLDT-GLGCV 972
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
925-971 |
1.80e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 69.65 E-value: 1.80e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 925 CDCHENGSLSGVCHLETGLCDCKPHVTGQQCDQCLSGYYGlDTGLGC 971
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1608-2157 |
1.55e-13 |
|
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: 77.14 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1608 LIKENAKKIRAEIQLEGIAEQTENLQKE---LTRVLARHQKVNAEME----RTSNGTQALATFIEQLHANIKEITEKVAT 1680
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEknaLQEQLQAETELCAEAEemraRLAARKQELEEILHELESRLEEEEERSQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1681 LnQTARKDFQPPV-----------SALQSMHQNISSLLGLIK---ERNFTEMQQNATL--ELKAAKDLLSRIQKRFQKPQ 1744
Cdd:pfam01576 94 L-QNEKKKMQQHIqdleeqldeeeAARQKLQLEKVTTEAKIKkleEDILLLEDQNSKLskERKLLEERISEFTSNLAEEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1745 EKLKALkeaNSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEK--KLRVQEEQnVTSELIAKGREwvda 1822
Cdd:pfam01576 173 EKAKSL---SKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaELQAQIAE-LRAQLAKKEEE---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1823 agthTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQM-SKRRARDlvhRAEQHASELQSRAGALDRDLENvrnvSLN 1901
Cdd:pfam01576 245 ----LQAALARLEEETAQKNNALKKIRELEAQISELQEDLeSERAARN---KAEKQRRDLGEELEALKTELED----TLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1902 ATSA---------AHVHSNIQTLTEEAEM----LAADAHKTANKTDLISESL--ASRGKAVLQRSSRFLKE-----SVST 1961
Cdd:pfam01576 314 TTAAqqelrskreQEVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLeqAKRNKANLEKAKQALESenaelQAEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1962 RRKQQGITMKLDELKNLTSQFQEsmdnIMKQANDSlamlrespggMREKGRKARELAAAANE--SAVKTLEDVLALSLRV 2039
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQE----LQARLSES----------ERQRAELAEKLSKLQSEleSVSSLLNEAEGKNIKL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2040 fntSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKLLISRARKQAASI 2119
Cdd:pfam01576 460 ---SKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590
....*....|....*....|....*....|....*...
gi 148706391 2120 KVAVSADRDCIRAYQPQTSSTnynTLILNVKTQEPDNL 2157
Cdd:pfam01576 537 AGTLEALEEGKKRLQRELEAL---TQQLEEKAAAYDKL 571
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
420-479 |
1.42e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.30 E-value: 1.42e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 420 CNCDPVGSLSSVCIKddrhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCIPCDC 479
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1512-1549 |
4.30e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.14 E-value: 4.30e-12
10 20 30
....*....|....*....|....*....|....*...
gi 148706391 1512 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1549
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1512-1549 |
6.15e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 6.15e-12
10 20 30
....*....|....*....|....*....|....*...
gi 148706391 1512 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1549
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1512-1549 |
7.81e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 7.81e-12
10 20 30
....*....|....*....|....*....|....*...
gi 148706391 1512 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1549
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1093-1150 |
3.50e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.50e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 1093 CGCDLRGTLPDTCDLEQGlcscsedsgTCSCKENVVGPQCSKCQAGTFALRGDNPQGC 1150
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG---------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
764-812 |
1.23e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.90 E-value: 1.23e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 148706391 764 PCECHGHAS---ECD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 812
Cdd:cd00055 1 PCDCNGHGSlsgQCDpGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1406-1452 |
2.81e-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: 57.75 E-value: 2.81e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 1406 CNCNNH---SDVCDPELGKCLsCRDHTSGDHCELCASGYYGKVTGLPGDC 1452
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
974-1018 |
2.91e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.91e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 148706391 974 CNCSVEGSVSDNC-TEEGQCHCGPGVSGKQCDRCSHGFYAFQDGGC 1018
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
419-472 |
5.65e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 5.65e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 148706391 419 PCNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRGFP 472
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT-----------GQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
974-1021 |
6.26e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.98 E-value: 6.26e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 148706391 974 CNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFYAFQDGGCTPC 1021
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
871-923 |
1.14e-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: 56.21 E-value: 1.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 148706391 871 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 923
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1594-2120 |
1.50e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1594 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNG-------TQALATFIEQ 1666
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarleerRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1667 LHANIKEITEKVATLNQTARkdfqppvsALQSMHQNISSLLGLIKErnftEMQQNATLELKAAKDLLSRIQKRFQKPQEK 1746
Cdd:COG1196 321 LEEELAELEEELEELEEELE--------ELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1747 LKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREwvdaAGTH 1826
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1827 TAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQ--SRAGALDRDLENVRNVSLnATS 1904
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAAL-EAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1905 AAHVHSNIQTLTEEAEMLAADAHKTANK---TDLISESLASRGKAVLQRSSRFLKESV----STRRKQQGITMKLDELKN 1977
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVdlvaSDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1978 LTSQFQESMDNIMKQAND--------SLAMLRESPGGMREKGRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRV 2049
Cdd:COG1196 624 GRTLVAARLEAALRRAVTlagrlrevTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148706391 2050 NATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIkLLISRARKQAASIK 2120
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLE 773
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
872-918 |
1.97e-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: 1.97e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 872 CNCSGNVDPleAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVT 918
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
477-523 |
2.72e-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: 2.72e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 477 CDCRTVGSLNeDPCIE---PCLCKKNVEGKNCDRCKPGFYNLKERNPEGC 523
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1405-1453 |
3.59e-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: 54.67 E-value: 3.59e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 148706391 1405 PCNCNNHSDV---CDPELGKCLsCRDHTSGDHCELCASGYYGkVTGLPGDCT 1453
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1093-1150 |
4.08e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 4.08e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 1093 CGCDLRGTLPDTCDLeqglcscseDSGTCSCKENVVGPQCSKCQAGTFalrGDNPQGC 1150
Cdd:smart00180 1 CDCDPGGSASGTCDP---------DTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1618-1823 |
5.75e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1618 AEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQ---TARKDFQPPVS 1694
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1695 ALQSMHQNISSLLGLIKERNFTEMQQNATL---ELKAAKDLLSRIQKRfqkpQEKLKALK-EANSLLSNHSEKLQAAEEL 1770
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFSDFLDRLSAlskIADADADLLEELKAD----KAELEAKKaELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148706391 1771 LKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAA 1823
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
765-811 |
6.06e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.90 E-value: 6.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 765 CECHGHAS---ECDIH-GICsVCTHNTTGDHCEQCLPGFYGTPSrGTPGDC 811
Cdd:pfam00053 1 CDCNPHGSlsdTCDPEtGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1651-2017 |
7.79e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1651 ERTSNGTQALATFIEQLHANIKEITEKVATLNQTarkdfqppVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAK 1730
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKA--------LAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1731 dLLSRIQKRFQKPQEKLKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTS 1810
Cdd:TIGR02168 738 -LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1811 ELIAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRAR-----DLVHRAEQHASELQSRA 1885
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleallNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1886 GALDRDLENVRNvslnatsaaHVHSNIQTLTEEAEMLAA---DAHKTANKTDLISESLASRGK----AVLQRSSRFLKES 1958
Cdd:TIGR02168 897 EELSEELRELES---------KRSELRRELEELREKLAQlelRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDE 967
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 1959 VSTRRKQQGITMKLDELK--NLTS-----QFQESMDNIMKQAND---SLAMLRESpggMREKGRKAREL 2017
Cdd:TIGR02168 968 EEARRRLKRLENKIKELGpvNLAAieeyeELKERYDFLTAQKEDlteAKETLEEA---IEEIDREARER 1033
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
973-1019 |
8.42e-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: 53.51 E-value: 8.42e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 973 PCNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFY--AFQDGGCT 1019
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYglPSQGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1616-1953 |
9.46e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 9.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1616 IRAEI--QLEGIAEQTEnlqkeltrVLARHQKVNAEMERTSNgtQALATFIEQLHANIKEITEKVATLNQTARkdfqppv 1693
Cdd:COG1196 194 ILGELerQLEPLERQAE--------KAERYRELKEELKELEA--ELLLLKLRELEAELEELEAELEELEAELE------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1694 sALQSMHQNISSLLGLIKERnftemQQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEansllsnhseKLQAAEELLKE 1773
Cdd:COG1196 257 -ELEAELAELEAELEELRLE-----LEELELELEEAQAEEYELLAELARLEQDIARLEE----------RRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1774 AGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRS 1853
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1854 HVDDLvmqmsKRRARDLVHRAEQHASELQSRAGALDRDLENVRNVSLNATSAAHVHSNIQTLTEEAE-MLAADAHKTANK 1932
Cdd:COG1196 401 QLEEL-----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLeLLAELLEEAALL 475
|
330 340
....*....|....*....|.
gi 148706391 1933 TDLISESLASRGKAVLQRSSR 1953
Cdd:COG1196 476 EAALAELLEELAEAAARLLLL 496
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1593-2002 |
1.06e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.22 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1593 ILENLENTTKYF---QRYLIKENAKKIRAEIQLEGIAEQTENL----QKELTRVLARHQKVNAEMERTSNGTQALATFIE 1665
Cdd:TIGR00606 696 FISDLQSKLRLApdkLKSTESELKKKEKRRDEMLGLAPGRQSIidlkEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1666 QLHAniKEITEKVATLNQTARKDFQPPVSALQ-SMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLLSRI---QKRFQ 1741
Cdd:TIGR00606 776 TIMP--EEESAKVCLTDVTIMERFQMELKDVErKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIelnRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1742 KPQEKLKALKEANSLLSnhSEKLQAAEElLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVD 1821
Cdd:TIGR00606 854 DQQEQIQHLKSKTNELK--SEKLQIGTN-LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1822 AAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQhASELQSRAGALDRDLENVRnvsln 1901
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQ-LEECEKHQEKINEDMRLMR----- 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1902 atsaahvhSNIQTlTEEAEMLAADAHKTANKTDLISEslasrgkavlqrssrfLKESVSTRRKQQGiTMKLDELKNLTSQ 1981
Cdd:TIGR00606 1005 --------QDIDT-QKIQERWLQDNLTLRKRENELKE----------------VEEELKQHLKEMG-QMQVLQMKQEHQK 1058
|
410 420
....*....|....*....|.
gi 148706391 1982 FQESMDNIMKQANDSLAMLRE 2002
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKG 1079
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
420-474 |
1.14e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148706391 420 CNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRG--FPNC 474
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1021-1066 |
1.26e-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: 53.13 E-value: 1.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 148706391 1021 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPEQGCQC 1066
Cdd:pfam00053 1 CDCnphGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1594-2111 |
1.32e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.01 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1594 LENLENTTKYFQryliKENAKKIRAEI-QLEGIAEQTENLQKELTRVLARHQKVNAEME-RTSNGTQALATFIEQLHANI 1671
Cdd:pfam12128 324 LEALEDQHGAFL----DADIETAAADQeQLPSWQSELENLEERLKALTGKHQDVTAKYNrRRSKIKEQNNRDIAGIKDKL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1672 KEITEKVATLNQTARKDFQPPVSALQSMHQ----NISSLLGLIKER----NFTEMQQNATLELK---AAKDLL-----SR 1735
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESELREQLEagklEFNEEEYRLKSRlgelKLRLNQATATPELLlqlENFDERierarEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1736 IQKRFQKPQEKLKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFqekkLRVQeeqnvtseliAK 1815
Cdd:pfam12128 480 QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF----LRKE----------AP 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1816 GreWVDAAGTHTAAAQDTLTQL------EHHRDELLLWARKIR----SHVDDLVMQMSKRRARDLVHRAEQHASELQSRA 1885
Cdd:pfam12128 546 D--WEQSIGKVISPELLHRTDLdpevwdGSVGGELNLYGVKLDlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1886 ----GALDRDLENV-RNVSLNATSAAHVHSNIQTLTEEAEMLAadahktanktDLISESLASRGKAVLQRSSRFLKESVS 1960
Cdd:pfam12128 624 eeqlVQANGELEKAsREETFARTALKNARLDLRRLFDEKQSEK----------DKKNKALAERKDSANERLNSLEAQLKQ 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1961 TRRKQQGITMKLDE-LKNLTSQFQESMDNIMKQANDSLAMLRESPGGmREKGRKA----------RELAA--------AA 2021
Cdd:pfam12128 694 LDKKHQAWLEEQKEqKREARTEKQAYWQVVEGALDAQLALLKAAIAA-RRSGAKAelkaletwykRDLASlgvdpdviAK 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2022 NESAVKTLEDVL---------ALSLRVF----------NTSEDLSRVNATVQETNDLLhnstmttllaGRKMKDMEMQAN 2082
Cdd:pfam12128 773 LKREIRTLERKIeriavrrqeVLRYFDWyqetwlqrrpRLATQLSNIERAISELQQQL----------ARLIADTKLRRA 842
|
570 580
....*....|....*....|....*....
gi 148706391 2083 LLLDRLKPLKTLEENLSRNLSEIKLLISR 2111
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRGLRCEMSK 871
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1020-1065 |
1.46e-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: 53.13 E-value: 1.46e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 1020 PCDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPE-QGCQ 1065
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
814-869 |
2.48e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 2.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 148706391 814 CACPLSIDSnnfSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGGTC 869
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
293-340 |
3.07e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 3.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 293 CICYGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGT 340
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1021-1064 |
5.85e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 5.85e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 1021 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGlDPEQGC 1064
Cdd:smart00180 1 CDCdpgGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1609-2134 |
6.49e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1609 IKENAKKIRAEIQ-LEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITE--KVATLNQTA 1685
Cdd:PRK03918 219 LREELEKLEKEVKeLEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1686 RKDFQPPVSALQSMHQNISSLLGLIK--ERNFTEmqqnatLELKAAKdlLSRIQKRFQKPQEKLKALKEANSLLSNHSEK 1763
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINgiEERIKE------LEEKEER--LEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1764 LQAAEELLKEAGSKTQESnlllllVKANLKEFQEKKLRVQEEqnvTSELIAKGREWVDAAGTHTAA------AQDT---- 1833
Cdd:PRK03918 371 KEELERLKKRLTGLTPEK------LEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAieelkkAKGKcpvc 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1834 ---LTqlEHHRDELLlwarkirshvddlvmqmskRRARDLVHRAEQHASELQSRAGALDRDLENVRNVslnatsaahvhs 1910
Cdd:PRK03918 442 greLT--EEHRKELL-------------------EEYTAELKRIEKELKEIEEKERKLRKELRELEKV------------ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1911 niqtLTEEAEMLAadAHKTANKTDLISESLASRGKAVLQRSS---RFLKESVSTRRKQQGITM----KLDELKNLTSQFQ 1983
Cdd:PRK03918 489 ----LKKESELIK--LKELAEQLKELEEKLKKYNLEELEKKAeeyEKLKEKLIKLKGEIKSLKkeleKLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1984 ESMDNIMKQANDSLAMLRE-SPGGMREKGRKARELAAAANE-----SAVKTLEDVL----ALSLRVFNTSEDLSRVNATV 2053
Cdd:PRK03918 563 KKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEylelkDAEKELEREEkelkKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2054 QET----NDLLHN-STMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKL---LISRARKQAASIKVA--- 2122
Cdd:PRK03918 643 EELrkelEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEeleEREKAKKELEKLEKAler 722
|
570
....*....|..
gi 148706391 2123 VSADRDCIRAYQ 2134
Cdd:PRK03918 723 VEELREKVKKYK 734
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1092-1150 |
7.40e-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: 7.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 1092 PCGCDLRGTLPDTCDLEqglcscsedSGTCSCKENVVGPQCSKCQAGTFALRgDNPQGC 1150
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1664-1995 |
9.20e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1664 IEQLHANIKEITEKVATLNQTARK--DFQPPVSALQSMHqnISSLLGLIKERNftEMQQNATLELKAAKDLLSRIQKRFQ 1741
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKaeRYKELKAELRELE--LALLVLRLEELR--EELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1742 KPQEKL------------------KALKEANSLLSN-------HSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQ 1796
Cdd:TIGR02168 264 ELEEKLeelrlevseleeeieelqKELYALANEISRleqqkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1797 EKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVddlvmqmskRRARDLVHRAEQ 1876
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---------ERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1877 HASELQSRAGALDRDLENVRnvslnatsAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLASRGKAVLQRSSRFlk 1956
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAE--------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-- 484
|
330 340 350
....*....|....*....|....*....|....*....
gi 148706391 1957 esvstRRKQQGITMkLDELKNLTSQFQESMDNIMKQAND 1995
Cdd:TIGR02168 485 -----AQLQARLDS-LERLQENLEGFSEGVKALLKNQSG 517
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
476-523 |
9.37e-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: 9.37e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 148706391 476 PCDCRTVGSLNEDpCIEP---CLCKKNVEGKNCDRCKPGFYNLKERnPEGC 523
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGtgqCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1605-1830 |
9.85e-08 |
|
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: 57.08 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1605 QRYLIKENAKKIRA-EIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQ 1683
Cdd:COG4942 18 QADAAAEAEAELEQlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1684 ---TARKDFQPPVSALQSMHQNiSSLLGLIKERNFTEMQQNATLelkaAKDLLSRIQKRFQKPQEKLKALKEANSLLSNH 1760
Cdd:COG4942 98 eleAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148706391 1761 SEKLQAA----EELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAA 1830
Cdd:COG4942 173 RAELEALlaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1697-2117 |
1.15e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1697 QSMhqnISSLLGLIKERNFTEMQQNATLelkAAKDLLSRIQKRFQKPQEKLKAlKEANSLlsnHsEKLQAAEELLKEags 1776
Cdd:PRK02224 152 QDM---IDDLLQLGKLEEYRERASDARL---GVERVLSDQRGSLDQLKAQIEE-KEEKDL---H-ERLNGLESELAE--- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1777 ktqesnlllllVKANLKEFQEKKLRVQEEQNVTSELIA---KGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRS 1853
Cdd:PRK02224 218 -----------LDEEIERYEEQREQARETRDEADEVLEeheERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1854 HVDDLVMQMSKRRARDLVHRA-----EQHASELQSRAGALDRDLENVRnvslnaTSAAHVHSNIQTLTEEAEMLAADAHK 1928
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDAdaeavEARREELEDRDEELRDRLEECR------VAAQAHNEEAESLREDADDLEERAEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1929 TANKTDLISESLASRGKAVLQRSSRF--LKESVSTRRKQ-QGITMKLDELKNLTSQFQESMDNIMKQANDSLAMLREspg 2005
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIeeLEEEIEELRERfGDAPVDLGNAEDFLEELREERDELREREAELEATLRT--- 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2006 gMREKGRKARELAAAAN----------ESAVKTLED----VLALSLRVFNTSEDLSRVNATVQETNDLlhnstmttllag 2071
Cdd:PRK02224 438 -ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdrerVEELEAELEDLEEEVEEVEERLERAEDL------------ 504
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 148706391 2072 rkmKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKLLISRARKQAA 2117
Cdd:PRK02224 505 ---VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1406-1452 |
1.51e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 1.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 1406 CNCN---NHSDVCDPELGKCLsCRDHTSGDHCELCASGYYGKVtglPGDC 1452
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1608-1927 |
1.56e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1608 LIKENAKKIRAEI-QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLN---- 1682
Cdd:COG4372 25 LIAALSEQLRKALfELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeele 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1683 --QTARKDFQPPVSALQSMHQNissllgLIKERNFTEMQQNATLELKAAKD-LLSRIQKRFQKPQEKLKALKEANSLLSN 1759
Cdd:COG4372 105 slQEEAEELQEELEELQKERQD------LEQQRKQLEAQIAELQSEIAEREeELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1760 HsEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEliakGREWVDAAGTHTAAAQDTLTQLEH 1839
Cdd:COG4372 179 A-EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA----KLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1840 HRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQSRAGALDRDLENVRNVSLNATSAAHVHSNIQTLTEEA 1919
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
....*...
gi 148706391 1920 EMLAADAH 1927
Cdd:COG4372 334 ILLAELAD 341
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1611-2127 |
1.80e-07 |
|
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: 57.11 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1611 ENAKKIRAEIQLEGIAEQTEN--LQKELtRVLARhQKVNAEMERTSNGTQalatfIEQLHANIKEiTEKvatlnqtARKD 1688
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENaeLQAEL-RTLQQ-AKQDSEHKRKKLEGQ-----LQELQARLSE-SER-------QRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1689 FQPPVSALQSMHQNISSLLGLIKERNftemqqnatleLKAAKDLlSRIQKRFQKPQE--------------KLKALK-EA 1753
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKN-----------IKLSKDV-SSLESQLQDTQEllqeetrqklnlstRLRQLEdER 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1754 NSLLsnhsEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEF-------QEKKLRVQEE-QNVTSELIAKGREWVDAAGT 1825
Cdd:pfam01576 499 NSLQ----EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDagtlealEEGKKRLQRElEALTQQLEEKAAAYDKLEKT 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1826 HTAAAQ---DTLTQLEHHRdELLLWARKIRSHVDDLVMQ---MSKRRA--RDlvhRAEQHASELQSRAGALDRDLENVR- 1896
Cdd:pfam01576 575 KNRLQQeldDLLVDLDHQR-QLVSNLEKKQKKFDQMLAEekaISARYAeeRD---RAEAEAREKETRALSLARALEEALe 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1897 --------NVSLNA------TSAAHVHSNI-----------QTLTE--------EAEMLAAD-----------AHKTANK 1932
Cdd:pfam01576 651 akeelertNKQLRAemedlvSSKDDVGKNVhelerskraleQQVEEmktqleelEDELQATEdaklrlevnmqALKAQFE 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1933 TDLIS-ESLASRGKAVLQRSSRFLKESVSTRRKQQGITM----KLD-ELKNLTSQfqesMDNIMKQANDSLAMLRESPGG 2006
Cdd:pfam01576 731 RDLQArDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVaakkKLElDLKELEAQ----IDAANKGREEAVKQLKKLQAQ 806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2007 MREKGRKARELAAA---------ANESAVKTLE-DVLALslrvfntSEDLS---RVNATVQETNDLLHNStmttLLAGRK 2073
Cdd:pfam01576 807 MKDLQRELEEARASrdeilaqskESEKKLKNLEaELLQL-------QEDLAaseRARRQAQQERDELADE----IASGAS 875
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148706391 2074 MKdmemqaNLLLDRLKPLKT----LEENLSRNLSEIKLLISRARK---QAASIKVAVSADR 2127
Cdd:pfam01576 876 GK------SALQDEKRRLEAriaqLEEELEEEQSNTELLNDRLRKstlQVEQLTTELAAER 930
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1613-1889 |
1.92e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1613 AKKIRAEIQLEGIAEQTENLQKEL----TRVLARHQKVNA-EMERTSNGTQALA-----TFIEQLHANIKEITEKVATLN 1682
Cdd:PRK04863 383 ARAEAAEEEVDELKSQLADYQQALdvqqTRAIQYQQAVQAlERAKQLCGLPDLTadnaeDWLEEFQAKEQEATEELLSLE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1683 Q------TARKDFQ----------PPVSALQSMHQNISSLLGLIKERNftEMQQNATLELKaakdlLSRIQKRFQKPQEK 1746
Cdd:PRK04863 463 QklsvaqAAHSQFEqayqlvrkiaGEVSRSEAWDVARELLRRLREQRH--LAEQLQQLRMR-----LSELEQRLRQQQRA 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1747 LKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNllllLVKANLKEfQEKKLRVQEEQ--NVTSELIAKGREWVdaag 1824
Cdd:PRK04863 536 ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS----ESVSEARE-RRMALRQQLEQlqARIQRLAARAPAWL---- 606
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1825 thtaAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQM-SKRRARDLVHRA----EQHASELQSRAGALD 1889
Cdd:PRK04863 607 ----AAQDALARLREQSGEEFEDSQDVTEYMQQLLERErELTVERDELAARkqalDEEIERLSQPGGSED 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1725-2117 |
2.34e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1725 ELKAAKDLLSRIQKRfqKPQEKLKALKEANSLLS-------------NHSEKLQAAEELLKEAGSKTQESNLLLLLVKAN 1791
Cdd:COG4717 50 RLEKEADELFKPQGR--KPELNLKELKELEEELKeaeekeeeyaelqEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1792 ---LKEFQEKKLRVQEEQNVTSELIAKGREWVDAAgTHTAAAQDTLTQLEHHRDELL-LWARKIRSHVDDLVMQMSKRRA 1867
Cdd:COG4717 128 lplYQELEALEAELAELPERLEELEERLEELRELE-EELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1868 RdlVHRAEQHASELQSRAGALDRDLENVRNVSLNATSAAHVHSNIQTLTEEAEM--LAADAHKTANKTDLISESLASRGK 1945
Cdd:COG4717 207 R--LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlaLLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1946 AVLQRSSRFLKESVSTRRKQQGITmKLDELKNLTSQ-FQESMDNIMKQANDSLAMLRESPGGMREKGRKARELAAAANES 2024
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQ-ALPALEELEEEeLEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2025 AVKTLEDVLALSLRVFNTS---------EDLSRVNATVQETNDL-----LHNSTMTTLLAGRKMKDMEMQANLLLDRLKP 2090
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEdeeelraalEQAEEYQELKEELEELeeqleELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420
....*....|....*....|....*..
gi 148706391 2091 LKTLEENLSRNLSEIKLLISRARKQAA 2117
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGE 470
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1613-2029 |
2.90e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1613 AKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVatlnQTARKDFQPP 1692
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL----EECRVAAQAH 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1693 VSALQSMHQNISSLlgliKERNFTEMQQNATLE--LKAAKDLLSRIQKRFQKPQEKLKALKEAnslLSNHSEKLQAAEEL 1770
Cdd:PRK02224 341 NEEAESLREDADDL----EERAEELREEAAELEseLEEAREAVEDRREEIEELEEEIEELRER---FGDAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1771 LKEAGSKTQESNLLLLLVKANLKEFQEkklRVQEEQnvtsELIAKGR-----EWVDAAGtHTAAAQDTLTQLEHHRDELL 1845
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARE---RVEEAE----ALLEAGKcpecgQPVEGSP-HVETIEEDRERVEELEAELE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1846 lwarKIRSHVDDLvmqmSKR--RARDLVhRAEQHASELQSRAGALDRDLENVRNvSLNATSAAhvhsnIQTLTEEAEMLA 1923
Cdd:PRK02224 486 ----DLEEEVEEV----EERleRAEDLV-EAEDRIERLEERREDLEELIAERRE-TIEEKRER-----AEELRERAAELE 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1924 ADA---HKTANKTDLISESLASRGKAVLQRssrfLKESVSTRRKQQGITMKLDELKNLTSQFQ------ESMDNIMKQAN 1994
Cdd:PRK02224 551 AEAeekREAAAEAEEEAEEAREEVAELNSK----LAELKERIESLERIRTLLAAIADAEDEIErlrekrEALAELNDERR 626
|
410 420 430
....*....|....*....|....*....|....*
gi 148706391 1995 DSLAMLREspggmrekgRKaRELAAAANESAVKTL 2029
Cdd:PRK02224 627 ERLAEKRE---------RK-RELEAEFDEARIEEA 651
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1595-1873 |
4.91e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1595 ENLENTTKYFQRylIKENAKKIRAEI-----QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHA 1669
Cdd:COG4372 80 EELEELNEQLQA--AQAELAQAQEELeslqeEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1670 NIKEITEKVATLNQTARKdfqppvsalQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLLSRIQKRFQKPQEKLKA 1749
Cdd:COG4372 158 QLESLQEELAALEQELQA---------LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1750 LKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAkgrEWVDAAGTHTAA 1829
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL---ELKLLALLLNLA 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 148706391 1830 AQDTLTQLEHHRDELLLW-ARKIRSHVDDLVMQMSKRRARDLVHR 1873
Cdd:COG4372 306 ALSLIGALEDALLAALLElAKKLELALAILLAELADLLQLLLVGL 350
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
765-806 |
6.14e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.46 E-value: 6.14e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 148706391 765 CECH--GHASE-CD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRG 806
Cdd:smart00180 1 CDCDpgGSASGtCDpDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1707-2031 |
6.55e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1707 LGLIKERNFTEMQQNATLE-LKAAKDLLSRIQKRFQKPQEKLKALKE----ANSLLSNHSEKLQAAEELLKEAGSKTQES 1781
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREeleqLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1782 NLLLLLVKANLKEFQEKKLRVQEEqnvtseliakgrewvdaagthtaaaqdtLTQLEHHRDELLLWARKIRSHVDDLVMQ 1861
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEE----------------------------LEELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1862 MSKRRARdlvhraeqhASELQSRAGALDRDLENVRNvSLNATSAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLA 1941
Cdd:COG4372 145 IAEREEE---------LKELEEQLESLQEELAALEQ-ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1942 SRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDSLA-MLRESPGGMREKGRKARELAAA 2020
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdTEEEELEIAALELEALEEAALE 294
|
330
....*....|.
gi 148706391 2021 ANESAVKTLED 2031
Cdd:COG4372 295 LKLLALLLNLA 305
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
477-523 |
8.66e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 8.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148706391 477 CDCRTVGSLNeDPCIEP---CLCKKNVEGKNCDRCKPGFYNlkeRNPEGC 523
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1613-1894 |
1.34e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1613 AKKIRAEIQLEGIAEQTENLQKEL----TRVLARHQKVNAeMERTSNGTQA-------LATFIEQLHANIKEITEKVATL 1681
Cdd:COG3096 382 ARLEAAEEEVDSLKSQLADYQQALdvqqTRAIQYQQAVQA-LEKARALCGLpdltpenAEDYLAAFRAKEQQATEEVLEL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1682 NQ------TARKDFQPPVSALQSM---------HQNISSLLglikeRNFTEmQQNATLELKAAKDLLSRIQKRFQKpQEK 1746
Cdd:COG3096 461 EQklsvadAARRQFEKAYELVCKIageversqaWQTARELL-----RRYRS-QQALAQRLQQLRAQLAELEQRLRQ-QQN 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1747 LKALkeANSLLSNHSEKLQAAEEL--LKEAGSKTQESnlllllVKANLKEFQEKK--LRVQEEQNVT--SELIAKGREWV 1820
Cdd:COG3096 534 AERL--LEEFCQRIGQQLDAAEELeeLLAELEAQLEE------LEEQAAEAVEQRseLRQQLEQLRAriKELAARAPAWL 605
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148706391 1821 daagthtaAAQDTLTQLEHHRDELLLWARKIRSHvddlvMQMSKRRARDlvhrAEQHASELQSRAGALDRDLEN 1894
Cdd:COG3096 606 --------AAQDALERLREQSGEALADSQEVTAA-----MQQLLERERE----ATVERDELAARKQALESQIER 662
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
871-915 |
1.61e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.61e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 148706391 871 PCNCSGNVDPleagHCDSVTGECLkCLWNTDGAHCERCADGFYGD 915
Cdd:smart00180 2 DCDPGGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1455-1509 |
1.99e-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: 46.96 E-value: 1.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 1455 CTCPHHPpfSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1509
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1610-2055 |
3.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1610 KENAKKIRAEIQ-LEGIAEQTENLQKELTRVLARHQKVN---------AEMERTSNGTQALATFIEQLHANIKEITEKVA 1679
Cdd:COG4717 84 EEKEEEYAELQEeLEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1680 TLNQTARKdfqppvsaLQSMHQNISSLLGLIKERNFTEMQQNATlELKAAKDLLSRIQKRFQKPQEKLKALKEANSLLSN 1759
Cdd:COG4717 164 ELEELEAE--------LAELQEELEELLEQLSLATEEELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1760 HSEKLQAAEELLKEAGSKTQESnlLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAAQDTLTQLEH 1839
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAA--ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1840 HRDellLWARKIRSHVDDLVM--QMSKRRARDLVHRAEQhASELQSRAGALDRDL-----ENVRNVSLNATSAahvhSNI 1912
Cdd:COG4717 313 LEE---LEEEELEELLAALGLppDLSPEELLELLDRIEE-LQELLREAEELEEELqleelEQEIAALLAEAGV----EDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1913 QTLTEEAEmLAADAHKTANKTDLISESLASRGKAVLQRSSRFLKESVSTRRKQqgITMKLDELKNLTSQFQESM---DNI 1989
Cdd:COG4717 385 EELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE--LEEELEELEEELEELREELaelEAE 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 1990 MKQA--NDSLAMLREspggmrEKGRKARELAAAANE-SAVKTLEDVLALSLRVFnTSEDLSRVNATVQE 2055
Cdd:COG4717 462 LEQLeeDGELAELLQ------ELEELKAELRELAEEwAALKLALELLEEAREEY-REERLPPVLERASE 523
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1597-2129 |
3.87e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.13 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1597 LENTTKYFQ-RYLIKENAKKiraeiQLEGIAEQT-ENLQKELTRVLARHQKVNAEMERTSNGTQALatfIEQLHANIKEI 1674
Cdd:TIGR00606 267 LDNEIKALKsRKKQMEKDNS-----ELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1675 T-EKVATLNQTARKDFQPPVSALQSMHQNISSL-LGLIKERNFTEMQQNATLELKAAKDLLSRIQKRfqkpqeklKAlKE 1752
Cdd:TIGR00606 339 NqEKTELLVEQGRLQLQADRHQEHIRARDSLIQsLATRLELDGFERGPFSERQIKNFHTLVIERQED--------EA-KT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1753 ANSLLSNhsekLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKlrVQEEQNVTSELiakgrewvdaagthtaaaqd 1832
Cdd:TIGR00606 410 AAQLCAD----LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK--QEELKFVIKEL-------------------- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1833 tlTQLEHHRDELLLWARKIRSHVDDLvmqmSKRRARDLVHRAEQHASELQSRAGALDRDL--ENVRNVSLNAtsaaHVHS 1910
Cdd:TIGR00606 464 --QQLEGSSDRILELDQELRKAEREL----SKAEKNSLTETLKKEVKSLQNEKADLDRKLrkLDQEMEQLNH----HTTT 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1911 NIQTLTEEAEMLAADAHKTANK----------------TDLISESLASRGKAVLQRSSRFLKESVSTRRKQQGITMKLDE 1974
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQIRKIKsrhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1975 LKNLTSQFQESMDNIMK----QANDS-LAMLRESpggmREKGRKARE-LAAAAN--ESAVKTLED----VLALSLRVFNT 2042
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDvcgsQDEESdLERLKEE----IEKSSKQRAmLAGATAvySQFITQLTDenqsCCPVCQRVFQT 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2043 SEDLSRVNATVQETNDLL---HNSTMTTLLAGRKMKD-----MEMQANLLLDRLKPLKTLEE---NLSRNLSEIKLLISR 2111
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLApdkLKSTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNklqKVNRDIQRLKNDIEE 769
|
570
....*....|....*...
gi 148706391 2112 ARKQAASIKVAVSADRDC 2129
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVC 787
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
813-867 |
5.27e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 45.81 E-value: 5.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 813 PCACPLSIDSNnfsPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGG 867
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTG---QC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1594-2117 |
5.35e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1594 LENLENTTKYFQRYLIKENAKKiraeiQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNG------TQALATFIEQL 1667
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQL-----KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAaplaahIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1668 HANIKEITEKVATLNQtARKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLLSRIQKRFQKPQEKL 1747
Cdd:TIGR00618 310 QRIHTELQSKMRSRAK-LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1748 KALKEANSLLSNHSEKLQaaEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEE---QNVTSELIAKGREWVDAAG 1824
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQ--REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAaaiTCTAQCEKLEKIHLQESAQ 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1825 THTAAAQ-----DTLTQ-------------LEHHRDELLLWARKIRSH---VDDLVMQMSKRRARDLVHRAEQHASELQS 1883
Cdd:TIGR00618 467 SLKEREQqlqtkEQIHLqetrkkavvlarlLELQEEPCPLCGSCIHPNparQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1884 RAGALDRDLENVRNVSLNATSAAHvhsNIQTLTEEAEMLAADAHKTANKTDLI-----SESLASRGKAVLQRSS-RFLKE 1957
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQ---SFSILTQCDNRSKEDIPNLQNITVRLqdlteKLSEAEDMLACEQHALlRKLQP 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1958 SVSTRRKQQGITMKLDEL-KNLTSQFQESMDNIMKQANDSLAMLRESPggMREKGRKARELAAAANE------------- 2023
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELaLKLTALHALQLTLTQERVREHALSIRVLP--KELLASRQLALQKMQSEkeqltywkemlaq 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2024 --SAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKdmeMQANLLLD-RLKPLKTLEENLSR 2100
Cdd:TIGR00618 702 cqTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTV---LKARTEAHfNNNEEVTAALQTGA 778
|
570
....*....|....*..
gi 148706391 2101 NLSEIKLLISRARKQAA 2117
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLRE 795
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1834-2088 |
6.18e-06 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 50.49 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1834 LTQLEHHRDELLLWARKIRSHVDDlvMQMSKRRARDLvhraEQHASELQSRAGALDRDLENVRNVSlNATSaahvhSNIQ 1913
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQ--IEILEKELSSL----AQETEELQKKATQTLAKAQQVNAES-ERTL-----GHAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1914 TLTEEAEMLAADAHKTANKTDLISE--SLASRGK--AVLQRSSRFLKE--SVSTRRKQQGITMKLDELKNLTSQFQESMD 1987
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGEndFALPSSDlsRMLAEAQRMLGEirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1988 NIMKQANDSLAMLRESPGGMREKGRKARELaaaANESAVKTlEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNstmtT 2067
Cdd:pfam06008 166 SPQEENKALANALRDSLAEYEAKLSDLREL---LREAAAKT-RDANRLNLANQANLREFQRKKEEVSEQKNQLEE----T 237
|
250 260
....*....|....*....|.
gi 148706391 2068 LLAGRkmkDMEMQANLLLDRL 2088
Cdd:pfam06008 238 LKTAR---DSLDAANLLLQEI 255
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1593-2106 |
9.34e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1593 ILENLENTTKYFQRYLIKEN-AKKIRAEIQleGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFI------- 1664
Cdd:TIGR04523 133 KKENKKNIDKFLTEIKKKEKeLEKLNNKYN--DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkki 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1665 ---EQLHANIKEITEKVATLNQTARK---DFQPPVSALQSMHQNISSLLGLiKERNFTEMQQNaTLELKAAKDLLSRIQK 1738
Cdd:TIGR04523 211 qknKSLESQISELKKQNNQLKDNIEKkqqEINEKTTEISNTQTQLNQLKDE-QNKIKKQLSEK-QKELEQNNKKIKELEK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1739 RFQKPQEKLKAL---KEANsLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLvkanLKEfQEKKLRvQEEQNVTSELIAK 1815
Cdd:TIGR04523 289 QLNQLKSEISDLnnqKEQD-WNKELKSELKNQEKKLEEIQNQISQNNKIISQ----LNE-QISQLK-KELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1816 GREwvdaagthTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKrrARDLVHRAEQHASELQSRAGALDRDLENV 1895
Cdd:TIGR04523 362 QRE--------LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN--QEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1896 R--NVSLNATsaahvhsnIQTLTEEaemlaaDAHKtanktDLISESLASRGKAVLQRSSRFLKESVSTRR----KQQGIT 1969
Cdd:TIGR04523 432 KetIIKNNSE--------IKDLTNQ------DSVK-----ELIIKNLDNTRESLETQLKVLSRSINKIKQnleqKQKELK 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1970 MKLDELKNLTSQFQESMDNImKQANDSLAMLREspggmrekgrKARELAAAAN--ESAVKTLEDVLaLSLRVFNTSEDLS 2047
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKV-KDLTKKISSLKE----------KIEKLESEKKekESKISDLEDEL-NKDDFELKKENLE 560
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 2048 RVNATVQETNDLLHNsTMTTLLAGRKMKDmEMQANLLLDRLKPLKTLEE------NLSRNLSEIK 2106
Cdd:TIGR04523 561 KEIDEKNKEIEELKQ-TQKSLKKKQEEKQ-ELIDQKEKEKKDLIKEIEEkekkisSLEKELEKAK 623
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1037-1095 |
1.08e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.04 E-value: 1.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 1037 CLCPPHtqGLKCEECeeaywglDPEQGcQCPCKKGFGGQSCHQCSLGYRSFPDCVPCGC 1095
Cdd:pfam00053 1 CDCNPH--GSLSDTC-------DPETG-QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1454-1510 |
1.43e-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: 44.65 E-value: 1.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148706391 1454 PCTCPHHPpfSFSPTCVVEgdsDFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGsCQ 1510
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1605-1895 |
1.53e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1605 QRYLIKENAKKIRA-EIQLEGIAEQTENLQKELTRVLARHQKVNAEMERtsngtqalatfIEQLhanIKEITEKVATLNQ 1683
Cdd:TIGR02169 221 REYEGYELLKEKEAlERQKEAIERQLASLEEELEKLTEEISELEKRLEE-----------IEQL---LEELNKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1684 TARKDFQppvSALQSMHQNISSLLGLIKERNftEMQQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEANSLLSNHSEK 1763
Cdd:TIGR02169 287 EEQLRVK---EKIGELEAEIASLERSIAEKE--RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1764 LQAAEELLKeagSKTQESNLLLLLVKANLKEFQEKKLRVQEEQN----VTSELIAKGREWVDAAGTHTAA---AQDTLTQ 1836
Cdd:TIGR02169 362 LKEELEDLR---AELEEVDKEFAETRDELKDYREKLEKLKREINelkrELDRLQEELQRLSEELADLNAAiagIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 1837 LEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQhaSELQSRAGALDRDLENV 1895
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY--DRVEKELSKLQRELAEA 495
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
732-926 |
1.80e-05 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 47.30 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 732 CECPQGY---TGTSCEACLPGyyrvdgilfggicqpcechghasecdiHGICSVCTHNTTGdhCEQCLPGFYGTPSRGTP 808
Cdd:cd13416 1 EACPSGQytsSGECCEQCPPG---------------------------EGVARPCGDNQTV--CEPCLDGVTFSDVVSHT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 809 GDCQPCA-CPLSIdsnnfSPTCHLTDGEEVVCdqcapgysgswceRCADGYYgnPTVPGGTCVPCNCsgnvdpleaghCD 887
Cdd:cd13416 52 EPCQPCTrCPGLM-----SMRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCEPCTV-----------CP 100
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148706391 888 SVTGECLKCLWNTDgAHCERCADGFYGDAVTAKN----CRACD 926
Cdd:cd13416 101 PGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDpclpCTVCE 142
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1619-2116 |
1.97e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 50.41 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1619 EIQLEGIAEQTENLQKELtrVLARHQKVNA--EMERTSNgtqalatFIEQLHANIkeitEKVATLNQTARKDFQPPVSAL 1696
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQS--EAAEAAKAQVleELESTKR-------LIEELKLNL----ERAQTEEAQAKQDSELAKLRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1697 QSMHQNISS--------LLGLIKERnftemQQNATLELKAAKDLLSRIQKrfqkpqeklkalkEANSLLSnhsEKlQAAE 1768
Cdd:pfam05701 108 EEMEQGIADeasvaakaQLEVAKAR-----HAAAVAELKSVKEELESLRK-------------EYASLVS---ER-DIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1769 ELLKEAGSKTQESnlllllvkanlkefqEKklRVQEeqnVTSELIAKgREWVDAAgtHTA----------AA----QDTL 1834
Cdd:pfam05701 166 KRAEEAVSASKEI---------------EK--TVEE---LTIELIAT-KESLESA--HAAhleaeehrigAAlareQDKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1835 T---QLEHHRDEL------LLWARKIRSHVDDLVMQMSKRRArDLVHRAEQHASELQSRAGALDRDlenvrNVSLNATSA 1905
Cdd:pfam05701 223 NwekELKQAEEELqrlnqqLLSAKDLKSKLETASALLLDLKA-ELAAYMESKLKEEADGEGNEKKT-----STSIQAALA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1906 A------HVHSNIQTLTEEAEML--AADAHKT---ANKTDLIS----ESLASRGKAVLQ---RSSRFLKESVSTRRKQQG 1967
Cdd:pfam05701 297 SakkeleEVKANIEKAKDEVNCLrvAAASLRSeleKEKAELASlrqrEGMASIAVSSLEaelNRTKSEIALVQAKEKEAR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1968 itmklDELKNLTSQFQESMdnimKQAND--SLAMLrespggMREKGRKARELAAAANeSAVKTLEDVLALSLR---VFNT 2042
Cdd:pfam05701 377 -----EKMVELPKQLQQAA----QEAEEakSLAQA------AREELRKAKEEAEQAK-AAASTVESRLEAVLKeieAAKA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2043 SEDLSRVNAT-VQETNDLLHNST------MTTLLA------GRKMKDMEMQANLLLDR-LKPLKTLEENLSRNLSEIKLL 2108
Cdd:pfam05701 441 SEKLALAAIKaLQESESSAESTNqedsprGVTLSLeeyyelSKRAHEAEELANKRVAEaVSQIEEAKESELRSLEKLEEV 520
|
570
....*....|
gi 148706391 2109 I--SRARKQA 2116
Cdd:pfam05701 521 NreMEERKEA 530
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
743-1093 |
2.48e-05 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 49.58 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 743 CEACLPGYyrvdGILFGGICQPCechghASECDIHGiCSVCThNTTGDHCEQCLPGFYGTPSRGTPGDCQPCAcplsids 822
Cdd:pfam03302 1 CDECKPGY----ELSADKTKCTS-----SAPCKTEN-CKACS-NDKREVCEECNSNNYLTPTSQCIDDCAKIG------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 823 NNFSPTChltDGEEVVCDQCAPGY-----SGSWCERCADGYYGNptvpGGTCVPC--NCSGNVDPLEAGHCDSVTGECLK 895
Cdd:pfam03302 63 NYYYTTN---ANNKKICKECTVANcktceDQGQCQACNDGFYKS----GDACSPCheSCKTCSGGTASDCTECLTGKALR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 896 -------------CLWNTDGAHCERCADGFYGdavtAKNCRACDCHENGSLSGVCH----LETGLCDCKPHVTGqQCDQC 958
Cdd:pfam03302 136 ygndgtkgtcgegCTTGTGAGACKTCGLTIDG----TSYCSECATETEYPQNGVCTstaaRATATCKASSVANG-MCSSC 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 959 LSGYYgldtglgcvpcncSVEGSVSDNCTEEGQCHCGPGVSGKQCDRCSHGfYAFQDGGCTPCDCAhtqnncdpasgecl 1038
Cdd:pfam03302 211 ANGYF-------------RMNGGCYETTKFPGKSVCEEANSGGTCQKEAPG-YKLNNGDLVTCSPG-------------- 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 148706391 1039 CPPHTQGLKCEECEEAYWGL-DPEQGCQCPCKKGFGG-QSCHQCSLG-YRSFPDCVPC 1093
Cdd:pfam03302 263 CKTCTSNTVCTTCMDGYVKTsDSCTKCDSSCETCTGAtTTCKTCATGyYKSGTGCVSC 320
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
814-862 |
3.17e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.45 E-value: 3.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 148706391 814 CACPLSidsNNFSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNP 862
Cdd:smart00180 1 CDCDPG---GSASGTCDPDTG---QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
293-336 |
8.73e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 8.73e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 293 CICY--GHAS-SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPW 336
Cdd:smart00180 1 CDCDpgGSASgTC----DPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
839-1154 |
2.08e-04 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 46.50 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 839 CDQCAPGYSGSwCERCADGYYGNPTvpgGTCVP-CNCSGNVDPLEAGHCDSVTGECL--KCLWNTDGAHCERCADGFYgd 915
Cdd:pfam03302 28 CKACSNDKREV-CEECNSNNYLTPT---SQCIDdCAKIGNYYYTTNANNKKICKECTvaNCKTCEDQGQCQACNDGFY-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 916 avtaKNCRACD-CHENgslsgvchletglCDCKPHVTGQQCDQCLSG---YYGLDTGLGCVPCNCsVEGSVSDNCTEegq 991
Cdd:pfam03302 102 ----KSGDACSpCHES-------------CKTCSGGTASDCTECLTGkalRYGNDGTKGTCGEGC-TTGTGAGACKT--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 992 chCGPGVSG-KQCDRCSHGFYAFQDGGCTPcdcahtqnNCDPASGECLCPPHTQGLkCEECEEAYwgLDPEQGC------ 1064
Cdd:pfam03302 161 --CGLTIDGtSYCSECATETEYPQNGVCTS--------TAARATATCKASSVANGM-CSSCANGY--FRMNGGCyettkf 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1065 --QCPCKKGFGGQSCHQCSLGYRsfpdcvpcgcdLRGTLPDTCDLEQGLCSCSEDSGTCSCKENVVGPQCSKCQAGTFAL 1142
Cdd:pfam03302 228 pgKSVCEEANSGGTCQKEAPGYK-----------LNNGDLVTCSPGCKTCTSNTVCTTCMDGYVKTSDSCTKCDSSCETC 296
|
330
....*....|..
gi 148706391 1143 RGdNPQGCSPCF 1154
Cdd:pfam03302 297 TG-ATTTCKTCA 307
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1595-1815 |
2.40e-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: 46.98 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1595 ENLENttkyfQRYLIKENAKKIRAEI-----QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHA 1669
Cdd:TIGR02169 836 QELQE-----QRIDLKEQIKSIEKEIenlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1670 NIKEITEKVATLNQTarkdfqppvsaLQSMHQNISSLlglikERNFTEMQQNATLELKAAKdllsrIQKRFQKPQEKLKA 1749
Cdd:TIGR02169 911 QIEKKRKRLSELKAK-----------LEALEEELSEI-----EDPKGEDEEIPEEELSLED-----VQAELQRVEEEIRA 969
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148706391 1750 LKEANSLlsnhseklqaAEELLKEagsktqesnlllllVKANLKEFQEKKLRVQEEQNVTSELIAK 1815
Cdd:TIGR02169 970 LEPVNML----------AIQEYEE--------------VLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1609-2120 |
3.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1609 IKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNgtqalatFIEQLHANIKEITEKVATLNQTA--R 1686
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE-------EINGIEERIKELEEKEERLEELKkkL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1687 KDFQPPVSALQSMHQNISSLLGLIKE-RNFTEMQQNATLElKAAKDLLSrIQKRFQKPQEKLKALKEANSLLSNHSEKLQ 1765
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEElERLKKRLTGLTPE-KLEKELEE-LEKAKEEIEEEISKITARIGELKKEIKELK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1766 AAEELLKEAGSK--------TQESNLL--------LLLVKANLKEF--QEKKLRVqEEQNVTSELiakgrewvdaagtht 1827
Cdd:PRK03918 426 KAIEELKKAKGKcpvcgrelTEEHRKElleeytaeLKRIEKELKEIeeKERKLRK-ELRELEKVL--------------- 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1828 aAAQDTLTQLEHHRDELllwaRKIRSHVDDLVMQMSKRRARDLvHRAEQHASELQSRAGALDRDLEnvRNVSLNATSAAh 1907
Cdd:PRK03918 490 -KKESELIKLKELAEQL----KELEEKLKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELE--KLEELKKKLAE- 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1908 VHSNIQTLTEE-AEMLaadaHKTANKTDLISESLASRgkavLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESM 1986
Cdd:PRK03918 561 LEKKLDELEEElAELL----KELEELGFESVEELEER----LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1987 DNIMKQANDsLAMLREspggmrekgrKARELAAAANESAVKTLEDvLALSLrvfntSEDLSRVNATVQETNDLLhNSTMT 2066
Cdd:PRK03918 633 EELAETEKR-LEELRK----------ELEELEKKYSEEEYEELRE-EYLEL-----SRELAGLRAELEELEKRR-EEIKK 694
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 148706391 2067 TLlagrkmKDMEMQanllLDRLKPLKTLEENLSRNLSEIKLLISRARKQAASIK 2120
Cdd:PRK03918 695 TL------EKLKEE----LEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1593-1807 |
4.44e-04 |
|
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: 46.17 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1593 ILENLENTTKYFQRYLikenaKKIRAEIQlegIAEQT-ENLQKELTRVLARHQKVNAEmertsngtqalatfIEQLHANI 1671
Cdd:TIGR04523 455 IIKNLDNTRESLETQL-----KVLSRSIN---KIKQNlEQKQKELKSKEKELKKLNEE--------------KKELEEKV 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1672 KEITEKVATLNQTARKdfqppvsaLQS----MHQNISSLlglikERNFTEMQQNATLELkaakdllsrIQKRFQKPQEKL 1747
Cdd:TIGR04523 513 KDLTKKISSLKEKIEK--------LESekkeKESKISDL-----EDELNKDDFELKKEN---------LEKEIDEKNKEI 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148706391 1748 KALKEAN-SLLSNHSEKlqaaEELLKEagsKTQESNLLLLLV--KANLKEFQEKKLRVQEEQN 1807
Cdd:TIGR04523 571 EELKQTQkSLKKKQEEK----QELIDQ---KEKEKKDLIKEIeeKEKKISSLEKELEKAKKEN 626
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1594-1866 |
5.63e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1594 LENLENTTKYFQRYL--IKENAKKIRAE-------IQLEGIAEQTENLQKELTRV-LARHQKVNAEMERTSNGTQALATF 1663
Cdd:PRK03918 461 LKRIEKELKEIEEKErkLRKELRELEKVlkkeselIKLKELAEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1664 IEQLHANIKEITE---KVATLNqtarkdfqppvSALQSMHQNISSLLGLIKERNFTEMQQ------------NATLELKA 1728
Cdd:PRK03918 541 IKSLKKELEKLEElkkKLAELE-----------KKLDELEEELAELLKELEELGFESVEEleerlkelepfyNEYLELKD 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1729 AKDLLSRIQKRFQKPQEKL-KALKEANsllsnhsEKLQAAEELLKEagsktqesnlllllvkanLKEFqEKKLRVQEEQN 1807
Cdd:PRK03918 610 AEKELEREEKELKKLEEELdKAFEELA-------ETEKRLEELRKE------------------LEEL-EKKYSEEEYEE 663
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 1808 VTSELIAKGREWvdaagthtAAAQDTLTQLEHHRDElllwarkIRSHVDDLVMQMSKRR 1866
Cdd:PRK03918 664 LREEYLELSREL--------AGLRAELEELEKRREE-------IKKTLEKLKEELEERE 707
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1593-2150 |
8.24e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.59 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1593 ILENLENTTKYFQRYLIKENAKKIRAEI-QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQ------ALATFIE 1665
Cdd:PTZ00440 1155 TLNEVNEIEIEYERILIDHIVEQINNEAkKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAyydkatASYENIE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1666 QL--HAN--------------IKEITEKVATLNQTARKDFQPPVSALQSMHqNISSLLGLIKERNFTE-----MQQNATL 1724
Cdd:PTZ00440 1235 ELttEAKglkgeanrstnvdeLKEIKLQVFSYLQQVIKENNKMENALHEIK-NMYEFLISIDSEKILKeilnsTKKAEEF 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1725 ELKAAKDL--LSRIQKRFQKPQEKLKALKEANSLLSNHS---EKLQAAEELLKEAGSKTQESNLLLLLVKANlKEFQEKK 1799
Cdd:PTZ00440 1314 SNDAKKELekTDNLIKQVEAKIEQAKEHKNKIYGSLEDKqidDEIKKIEQIKEEISNKRKEINKYLSNIKSN-KEKCDLH 1392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1800 LRV---------------QEEQNVTSEL-IAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVDD-LVMQM 1862
Cdd:PTZ00440 1393 VRNasrgkdkidflnkheAIEPSNSKEVnIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNILNNsSILGK 1472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1863 S------KRRARDLVHRAEQHASELQSRAGALDRDLENVRNvslnatsaahvHSNIqtlTEEAEMLAADAHKTANKTDLI 1936
Cdd:PTZ00440 1473 KtklekkKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNE-----------QPNI---KREGDVLNNDKSTIAYETIQY 1538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1937 S-----------ESLASRGKAVLQRSSrFLKESVStRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDslamlrespg 2005
Cdd:PTZ00440 1539 NlgrvkhnllniLNIKDEIETILNKAQ-DLMRDIS-KISKIVENKNLENLNDKEADYVKYLDNILKEKQL---------- 1606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2006 gMREKGRKARELaaaanESAVKTLEDVL---------ALSLRVFNTSEDL-SRVNATVQETNDLLHNstMTTLLAGRKMK 2075
Cdd:PTZ00440 1607 -MEAEYKKLNEI-----YSDVDNIEKELkkhkknyeiGLLEKVIEINKNIkLYMDSTKESLNSLVNN--FSSLFNNFYLN 1678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 2076 DMEMQANLLLDRLK----------PLKTLEENLSR------NLSEIKLLISRARKQAASIKVAVsadrDCIRAYQPQTSS 2139
Cdd:PTZ00440 1679 KYNINENLEKYKKKlneiynefmeSYNIIQEKMKEvsnddvDYNEAKTLREEAQKEEVNLNNKE----EEAKKYLNDIKK 1754
|
650
....*....|.
gi 148706391 2140 TNYNTLILNVK 2150
Cdd:PTZ00440 1755 QESFRFILYMK 1765
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1912-2033 |
8.34e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 45.04 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1912 IQTLTEEAEMLAADAHKTANKTDLIS---ESLASRGKAVLQRSSRFLKESVSTRRKQ----QGITMKLDELKNLTSQFQE 1984
Cdd:pfam10168 577 LQSLEEERKSLSERAEKLAEKYEEIKdkqEKLMRRCKKVLQRLNSQLPVLSDAEREMkkelETINEQLKHLANAIKQAKK 656
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 148706391 1985 SMDnimKQAndslamlRESPGGMREKGRKARELaaaaNESAVKTLEDVL 2033
Cdd:pfam10168 657 KMN---YQR-------YQIAKSQSIRKKSSLSL----SEKQRKTIKEIL 691
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1455-1502 |
1.05e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 148706391 1455 CTCphHPPFSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNP 1502
Cdd:smart00180 1 CDC--DPGGSASGTCDPDT---GQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
293-339 |
2.03e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.49 E-value: 2.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148706391 293 CICYGHASSCPwDEEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPG 339
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1625-1896 |
2.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1625 IAEQTENLQKELTRVLARHQkvnaEMERTSNGTQALATfIEQLHANIKEITEKVATLNQTArkdfqppvSALQsmHQNIS 1704
Cdd:COG4913 223 TFEAADALVEHFDDLERAHE----ALEDAREQIELLEP-IRELAERYAAARERLAELEYLR--------AALR--LWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1705 SLLGLIKERnftemQQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEAnsLLSNHSEKLQAAEELLKEAGSKTQEsnll 1784
Cdd:COG4913 288 RRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNGGDRLEQLEREIERLERELEE---- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1785 lllVKANLKEFQEKkLRVQEEQNVTSEliakgREWVDAAgthtAAAQDTLTQLEHHRDELllwarkiRSHVDDLvmqmsK 1864
Cdd:COG4913 357 ---RERRRARLEAL-LAALGLPLPASA-----EEFAALR----AEAAALLEALEEELEAL-------EEALAEA-----E 411
|
250 260 270
....*....|....*....|....*....|....*
gi 148706391 1865 RRARDLVHRAEQHASE---LQSRAGALDRDLENVR 1896
Cdd:COG4913 412 AALRDLRRELRELEAEiasLERRKSNIPARLLALR 446
|
|
| F-BAR_Rgd1 |
cd07652 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ... |
1610-1782 |
2.59e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153336 [Multi-domain] Cd Length: 234 Bit Score: 42.33 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1610 KENAK--KIRAEIQLEGIaeqtENLQKeltrvLARHQKvnaEMERTSNGTQAlaTFIEQLHANIkEITEKVATLNQTArk 1687
Cdd:cd07652 22 KEFATflKKRAAIEEEHA----RGLKK-----LARTTL---DTYKRPDHKQG--SFSNAYHSSL-EFHEKLADNGLRF-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1688 dfqppVSALQSMHQNISSLL-------------GLIKERNFTEMQQ---NATLELKAAKDLLSRIqkRFQKPQEKLKALK 1751
Cdd:cd07652 85 -----AKALNEMSDELSSLAktveksrksiketGKRAEKKVQDAEAaaeKAKARYDSLADDLERV--KTGDPGKKLKFGL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 148706391 1752 EANSLLSNHSE----KLQAAEELLKeagSKTQESN 1782
Cdd:cd07652 158 KGNKSAAQHEDellrKVQAADQDYA---SKVNAAQ 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1762-1977 |
3.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1762 EKLQA-AEELLKEAGSKTqesnlllllvKANLKEFQEKKLRVQEEQNVTSELiakgrewvdaagthtAAAQDTLTQLEHH 1840
Cdd:COG4717 49 ERLEKeADELFKPQGRKP----------ELNLKELKELEEELKEAEEKEEEY---------------AELQEELEELEEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1841 RDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQSRAGALDRDLENVRNvslnatsaahVHSNIQTLTEEAE 1920
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE----------LEEELEELEAELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148706391 1921 MLAADAHKTANKTDLISE----SLASRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKN 1977
Cdd:COG4717 174 ELQEELEELLEQLSLATEeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
731-755 |
4.93e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 4.93e-03
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1605-1804 |
5.28e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1605 QRYLIKENAKKIRAEIqlEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQT 1684
Cdd:COG1340 30 KRDELNEELKELAEKR--DELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1685 arkdfQPPVSALQSMhqnISSLLglikernftEMQQNATLELKAAKDLLSRIQKRfqkpQEKLKALKEANSLLSNHSEKL 1764
Cdd:COG1340 108 -----GGSIDKLRKE---IERLE---------WRQQTEVLSPEEEKELVEKIKEL----EKELEKAKKALEKNEKLKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148706391 1765 QAAEELLKEAGSKTQEsnlllllVKANLKEFQEKKLRVQE 1804
Cdd:COG1340 167 AELKELRKEAEEIHKK-------IKELAEEAQELHEEMIE 199
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1621-1774 |
6.65e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1621 QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQ---TAR--KDFQppvsA 1695
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgNVRnnKEYE----A 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148706391 1696 LQsmHQnISSLLGLIKERNFTEMQQNATLElkAAKDLLSRIQKRFQKPQEKLKALKEAnslLSNHSEKLQAAEELLKEA 1774
Cdd:COG1579 94 LQ--KE-IESLKRRISDLEDEILELMERIE--ELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAE 164
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
731-763 |
8.09e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 36.95 E-value: 8.09e-03
10 20 30
....*....|....*....|....*....|...
gi 148706391 731 HCECPQGYTGTSCEACLPGYYRVDGILFGgiCQ 763
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| PTZ00214 |
PTZ00214 |
high cysteine membrane protein Group 4; Provisional |
780-1121 |
9.30e-03 |
|
high cysteine membrane protein Group 4; Provisional
Pssm-ID: 173479 [Multi-domain] Cd Length: 800 Bit Score: 41.83 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 780 CSVCTHNTTGDHCEQCLPGFYG----TPSRGTPGDCQ---------------PCACPLSIDSNNFSPTCHLTDGEEVVCD 840
Cdd:PTZ00214 364 CATCGYNSGAVTCTRCSAGYLGvdgkSCSESCSGDTRgvctkvaegsestevSCRCVCKPTFYNSSGTCTPCTDSCAVCK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 841 QCAPgysgSWCERCADGYYGNPTVPGGTCVPCncsgnvdpleAGHCdSVTGECLKCLWNTDGA-HCERCADG----FYGD 915
Cdd:PTZ00214 444 DGTP----TGCQQCSPGKILEFSIVSSESADC----------VDQC-SVGSECAECGITIDGSrYCTRCKDAstypFNGV 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 916 AVTAKNCRA-CDCHENG---SLSGVCHLETGLCDCKPHVTGQ---------QCDQCLSGYYGLDTG--LGCVPCNCSveg 980
Cdd:PTZ00214 509 CIPNTQRDAyCTSTANGactTCSGAAFLMNGGCYTTEHYPGSticdkqsngKCTTTKKGYGISPDGklLECDPTCLA--- 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 981 svsdnCTEEGQCHCGPGVSGKQCDR--------------CSHGFYAFQDgGCTPC------DCAHTqNNCDPASGECLCP 1040
Cdd:PTZ00214 586 -----CTAPGPGRCTRCPSDKLLKRasgaatgscvdpgaCVDGYYADGD-ACLPCatpgckTCGHA-SFCTECAGELFVS 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1041 phTQGLKC-EECE-EAYWGLDPEQGCQCPCKKGFggqschqcslgyrsFPDCVPCGCdlrgTLPDTCDLEQGLCSCSEDS 1118
Cdd:PTZ00214 659 --LDGQSClEECTgDKVVGEVSGGVRRCWCERGF--------------LPALDRSGC----VLPTECPPDMPSCAACDES 718
|
...
gi 148706391 1119 GTC 1121
Cdd:PTZ00214 719 GRC 721
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1621-1836 |
9.55e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.36 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1621 QLEGIAEQTEN------LQKELTRVLARHQKVNAEMERtsngTQALATFIEQLHANIKEITEKVATLNQTARKDFQP--- 1691
Cdd:pfam12795 1 KLDELEKAKLDeaakkkLLQDLQQALSLLDKIDASKQR----AAAYQKALDDAPAELRELRQELAALQAKAEAAPKEila 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148706391 1692 --PVSALQSMHQNISSLLGLIKERNFTEMQQNATLE--LKAAKDLLSRIQKRFQKPQEKLKALKEANSLLSNHSEKLQAA 1767
Cdd:pfam12795 77 slSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQtrPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148706391 1768 EELLKEAGSKTQE-----SNLLLLLVKANLKEFQEKKLRVQEEQNVTSELI-AKGREWVDAAgthtAAAQDTLTQ 1836
Cdd:pfam12795 157 ELAALKAQIDMLEqellsNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLnEKRLQEAEQA----VAQTEQLAE 227
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