|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
32-278 |
3.41e-87 |
|
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: 285.02 E-value: 3.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 32 FPVIFNLATEADITSNATCGETGPETYCKLVEHVKQLMmknyQCGICDANGdlPYQRHPIQNAIDGSN----RWWQSPSL 107
Cdd:smart00136 8 YPPFVNLAFGREVTATSTCGEPGPERYCKLVGHTEQGK----KCDYCDARN--PRRSHPAENLTDGNNpnnpTWWQSEPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 108 ANGWQYdwVTITLDLGQAFQIAYVIVKAAnSPRPANWILERSVDGITFTPWQYFAlsdGECWNAFGVPPTVGRPRYRrDD 187
Cdd:smart00136 82 SNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITKGN-ED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 188 EVICTSFYSRLDPIENGEIHTSLVNGRPGAVNGP-SDLLLEFTTARFLRLRLQKIRTLNADLMTIRTSnpdkidkaVTRR 266
Cdd:smart00136 155 EVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDnSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPE--------VTRR 226
|
250
....*....|..
gi 919026507 267 YFYSIKDISIGG 278
Cdd:smart00136 227 YYYAISDIAVGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
569-719 |
3.69e-33 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 126.23 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 569 YWHAPAPyagskanFLGNKLASYGGNLTYSMYYVVQRLEDVNTAYTadlDVIMEGNELLIGYGGR---YYREGLENTMQV 645
Cdd:pfam00052 1 YWSAPEQ-------FLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEP---DVILEGNGLRLSYSSPdqpPPDPGQEQTYSV 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919026507 646 FLTERDWYHVDpdtglpkQQIVTRQEFMTVLANIERLLIRASYHIHQTQIQFLDMAMDVAVENSTSPSImSSVE 719
Cdd:pfam00052 71 RLHEENWRDSD-------GAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPA-SWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1338-1482 |
2.75e-32 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 123.53 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1338 YWSAPRKFLGDKTLSYYGKLKFVIYFEDQDslntlpipivDHSEYRRFPLVRITGN-FRVVLDYFAPLTP--GVENEFEI 1414
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLP----------GGGSLNSEPDVILEGNgLRLSYSSPDQPPPdpGQEQTYSV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919026507 1415 FLREDQWTDplQPSKPVTREMLMVGLQNLQSIKIRASGNSNLKYAEIRGLSLQHATNASAGEAALGVE 1482
Cdd:pfam00052 71 RLHEENWRD--SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3047-3200 |
5.94e-30 |
|
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: 117.52 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 3047 GVYFSGYAYGIYDSNFVVGSNFLLTFDFRTTKPEGVILTISHPYRRPSMALELFDGQLQFTVNNEDGLifsmTEYENPFR 3126
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGS----LVLSSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 3127 LCNNKWHTVRAELVKNTIMLTVDG--VEQLSETGGSEFLATDHPLFIGGYPYYAEPQGAAqANEKFQGCIRNMKIN 3200
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGerVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP-VSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2627-2777 |
7.80e-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: 114.44 E-value: 7.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2627 VAGFHGDGYIQLTGDSLPGREADISFSFRSLQDIALLLLGLGGQADPhFYSVSLIDGKLQAKFDAGDGEVTITSDDTFND 2706
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGD-FLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919026507 2707 GMLHGVSIIRNRRKLDMFVDDLPVGTERLSKGSK--VEISSLYLGGVPADLDiASASATSQPLQGCIRDLVLN 2777
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGERVVESGSPGGSAllNLDGPLYLGGLPEDLK-SPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2443-2599 |
1.33e-28 |
|
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: 113.67 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2443 FDGTGYAEVPPIQRYDSTGYLAlFEFRTFWEDALLFFSGNKANGEYIAVELVNGKVVFSVNFGGGnNISIESREKYNTNQ 2522
Cdd:cd00110 4 FSGSSYVRLPTLPAPRTRLSIS-FSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG-SLVLSSKTPLNDGQ 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 2523 WMTVKAETQGNAGQLEVttsegrEELKRAQATASGEDSLDISNASVYFGGIPSTSKFDSFPlsVRTPFLGCMKGIQV 2599
Cdd:cd00110 82 WHSVSVERNGRSVTLSV------DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP--VSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2882-3022 |
2.89e-26 |
|
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: 107.12 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2882 LVDRDEISSNFDIMLEFRTYYPNGLLVYLSNEDQSEYVAIQMAGGTVMTSYadqktgvpvNLTEGATVL-----VDDGKW 2956
Cdd:cd00110 12 LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRY---------DLGSGSLVLssktpLNDGQW 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919026507 2957 HKIRLMKSANNIIFKVDEGP---DIVGRIANKIDVLAPMYVGGLPRGYNMRMGLVPDSLKGCVRGFRLN 3022
Cdd:cd00110 83 HSVSVERNGRSVTLSVDGERvveSGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2260-2411 |
4.30e-18 |
|
Laminin G domain;
:
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 83.16 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2260 TISFNFKTnnTEKDMLLFYVQGEEKPEFMAVEIVERKLRFVWNSGGGVAmanhslQIESEETSIqPDEKWYSVIARRTAN 2339
Cdd:smart00282 1 SISFSFRT--TSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPA------RLTSDPTPL-NDGQWHRVAVERNGR 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919026507 2340 VGTLAVqkikfagnDDPALASSSSSAQFTKLDLNDRakLYVAGAP-QGTVERDPALKGgmFVGCIADVTLDGR 2411
Cdd:smart00282 72 SVTLSV--------DGGNRVSGESPGGLTILNLDGP--LYLGGLPeDLKLPPLPVTPG--FRGCIRNLKVNGK 132
|
|
| Laminin_I super family |
cl26988 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1701-1941 |
2.07e-15 |
|
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.
The actual alignment was detected with superfamily member pfam06008:
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 78.99 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1701 VRGVNTSTMvviPWERFFAM----ENKTQVLRGKLDAIR------KVKVGDMEVI---VKELQANATKLYTQTSSMANDA 1767
Cdd:pfam06008 1 LLSLNSLTG---ALPAPYKInynlENLTKQLQEYLSPENahkiqiEILEKELSSLaqeTEELQKKATQTLAKAQQVNAES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1768 MGYSMVASNLSKTADGMEKEIREIITSARDLLDNLpdvHQLSGNvNLTSVMMKAQDIMKMIRERDFKPNIENADNELELA 1847
Cdd:pfam06008 78 ERTLGHAKELAEAIKNLIDNIKEINEKVATLGEND---FALPSS-DLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1848 KALKSSISDLQSKLTN-----VTDAAISIQELADRLNDLISLAEQSAKDSRAALELNQKNDElikklqNMTqALQTRALA 1922
Cdd:pfam06008 154 QDLLSRIQTWFQSPQEenkalANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQA------NLR-EFQRKKEE 226
|
250
....*....|....*....
gi 919026507 1923 VSSMLNMSSEMLKEANMTL 1941
Cdd:pfam06008 227 VSEQKNQLEETLKTARDSL 245
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1075-1120 |
7.60e-15 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 70.80 E-value: 7.60e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1075 CDCDVTGSTSLQCGMTSGQCPCKPGVTGQKCDQCRPGYYGFSSNGC 1120
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_II super family |
cl05515 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2129-2252 |
5.30e-14 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
The actual alignment was detected with superfamily member pfam06009:
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 71.36 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2129 ANDNATGALEkamnTVTSVDSIQEGLDNDLKpkldvvkvntKELQDLETMTGTMMEINNNLD----GIRDVNRSIHTTLG 2204
Cdd:pfam06009 1 SKELAREANE----TAKEVLEQLAPLSQNLE----------NTSEKLSGINRSLEETNELVNdankALDDAGRSVKKLEE 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919026507 2205 ALNRL-------------NMSLSQSLEELRESIQKAREQANNIKVSLAAGGSCHREYRTEE 2252
Cdd:pfam06009 67 LAPDLldklkplkqlevnSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPI 127
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1025-1073 |
1.52e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.99 E-value: 1.52e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 1025 ACNCHLKGSNDSQCDLVTGTCTCQPNVIGDKCDQCEINYYDLDS-GNGCQ 1073
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1170-1218 |
3.69e-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: 63.14 E-value: 3.69e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 1170 CNCNMTGSLDTQCDTVDGQCECRPEYDGMKCDMCRFGHFGFPNCRPCHC 1218
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
978-1023 |
3.31e-11 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.31e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 978 CSCNLTGSVSNLCDQVSGQCPCKNGVGGQYCGSCLPDHWEYSEEGC 1023
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1634-1672 |
1.20e-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: 1.20e-10
10 20 30
....*....|....*....|....*....|....*....
gi 919026507 1634 PCDCSEDGSLDNLCDRESGQCICHPGVLGRACDQCQPRY 1672
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1525-1574 |
3.63e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.63e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 919026507 1525 PCECHGHSDM---CNKETGVCLnCAHNTAGDHCNTCAEGYYGNATSGREdaCQ 1574
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
931-968 |
8.67e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 8.67e-10
10 20 30
....*....|....*....|....*....|....*...
gi 919026507 931 CDCNQYGSTGTSCDQRSGQCSCRPYYEGRACDSCVAGY 968
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1863-2198 |
1.18e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
:
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.38 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1863 NVTDAAISIQELADRLNDLIS-LAEQSAKDSRAALELNQKNDELiKKLQNMTQALQTRALAVSSMLNMSSEMLKEANmtl 1941
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREeLEQAREELEQLEEELEQARSEL-EQLEEELEELNEQLQAAQAELAQAQEELESLQ--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1942 pnSSAEFLRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAEKLRMQADNLDNMFQGARATSEdAVKAAQVYEG 2021
Cdd:COG4372 108 --EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ-ALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2022 IVVAVDDALKEAQSAHDLAsEAMNKTTTADGSTLQEKAKKSANTSLDFVNEANRLVNSSKDLKDLLGSIDKDIDQANKRM 2101
Cdd:COG4372 185 LDELLKEANRNAEKEEELA-EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2102 DEVDSAKERLTEGMDRLPAGIHEKLIEANDnatGALEKAMNTVTSVDSIQEGLDNDLKPKLDVVKVNTKELQDLETMTGT 2181
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAAL---ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330 340
....*....|....*....|
gi 919026507 2182 ---MMEINNNLDGIRDVNRS 2198
Cdd:COG4372 341 dllQLLLVGLLDNDVLELLS 360
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1216-1271 |
1.22e-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: 56.21 E-value: 1.22e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 1216 CHCNENGTVMSDCNakghcqcQEDGQCPCRGNVEGLKCKHCKEGSFSLQSNNPEGC 1271
Cdd:pfam00053 1 CDCNPHGSLSDTCD-------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
457-504 |
6.26e-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: 54.28 E-value: 6.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 919026507 457 PCPCSRAGSRNvDTC---QGDCICKPNVVGENCDQCKPGFFNmEASNPAGC 504
Cdd:cd00055 1 PCDCNGHGSLS-GQCdpgTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
768-815 |
1.86e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.86e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 919026507 768 CNCNNHA---DTCEASSGLCtSCRDNTVGPHCENCEFGYYGNATrGTPNDC 815
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
404-460 |
5.98e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 5.98e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 919026507 404 CQCSQLGS-TGTCVQdnsrrgeglMPGDCICRVGFGGRNCDRCASGYKNFPSCIPCPC 460
Cdd:pfam00053 1 CDCNPHGSlSDTCDP---------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1122-1168 |
6.38e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 6.38e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 919026507 1122 ECPVCPVAGQVCDAVTGECVCPTNTEGDRCERCVPDTWGHD-QLLGCK 1168
Cdd:cd00055 3 DCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
878-921 |
1.00e-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: 47.73 E-value: 1.00e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 919026507 878 PCACSGNINPNavGNCDRTTGQCLkCLFNTEGWNCAQCKPDYYG 921
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
280-327 |
2.38e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.88 E-value: 2.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 280 CKCYGHASSCPR-SPDTGKlmCVCEDNTCGKNCEKCCPKFNQQPYKPGT 327
Cdd:cd00055 2 CDCNGHGSLSGQcDPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1605-1632 |
9.28e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 9.28e-04
10 20
....*....|....*....|....*...
gi 919026507 1605 CPRGYEGDHCERCSDYFYGDPTKLGGEC 1632
Cdd:pfam00053 22 CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
848-876 |
1.27e-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: 39.26 E-value: 1.27e-03
10 20
....*....|....*....|....*....
gi 919026507 848 SCPDGYIGNHCEMCDDGYFGNPLVPGNYC 876
Cdd:pfam00053 21 LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
368-401 |
1.87e-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: 1.87e-03
10 20 30
....*....|....*....|....*....|....
gi 919026507 368 GGVCMnCRDHTTGVNCEQCEAGYYRTTDDPREPC 401
Cdd:pfam00053 17 TGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
32-278 |
3.41e-87 |
|
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: 285.02 E-value: 3.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 32 FPVIFNLATEADITSNATCGETGPETYCKLVEHVKQLMmknyQCGICDANGdlPYQRHPIQNAIDGSN----RWWQSPSL 107
Cdd:smart00136 8 YPPFVNLAFGREVTATSTCGEPGPERYCKLVGHTEQGK----KCDYCDARN--PRRSHPAENLTDGNNpnnpTWWQSEPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 108 ANGWQYdwVTITLDLGQAFQIAYVIVKAAnSPRPANWILERSVDGITFTPWQYFAlsdGECWNAFGVPPTVGRPRYRrDD 187
Cdd:smart00136 82 SNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITKGN-ED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 188 EVICTSFYSRLDPIENGEIHTSLVNGRPGAVNGP-SDLLLEFTTARFLRLRLQKIRTLNADLMTIRTSnpdkidkaVTRR 266
Cdd:smart00136 155 EVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDnSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPE--------VTRR 226
|
250
....*....|..
gi 919026507 267 YFYSIKDISIGG 278
Cdd:smart00136 227 YYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
32-278 |
1.29e-83 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 274.46 E-value: 1.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 32 FPVIFNLATEADITSNATCGETGPETYCKLVEHvkqlmMKNYQCGICDANgdLPYQRHPIQNAIDGSNR----WWQSPSL 107
Cdd:pfam00055 2 YPAFGNLAFGREVSATSTCGLNGPERYCILSGL-----EGGKKCFICDSR--DPHNSHPPSNLTDSNNGtnetWWQSETG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 108 ANgwQYDWVTITLDLGQAFQIAYVIVKAAnSPRPANWILERSVD-GITFTPWQYFAlsdGECWNAFGVPPtvGRPRYRRD 186
Cdd:pfam00055 75 VI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPS--GPSRGIKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 187 DEVICTSFYSRLDPIENGEIHTSLVNGRPGAVN-GPSDLLLEFTTARFLRLRLQKIRTLNADLMTirtsnpdkiDKAVTR 265
Cdd:pfam00055 147 DEVICTSEYSDISPLTGGEVIFSTLEGRPSANIfDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVLR 217
|
250
....*....|...
gi 919026507 266 RYFYSIKDISIGG 278
Cdd:pfam00055 218 KYYYAISDISVGG 230
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
569-719 |
3.69e-33 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 126.23 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 569 YWHAPAPyagskanFLGNKLASYGGNLTYSMYYVVQRLEDVNTAYTadlDVIMEGNELLIGYGGR---YYREGLENTMQV 645
Cdd:pfam00052 1 YWSAPEQ-------FLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEP---DVILEGNGLRLSYSSPdqpPPDPGQEQTYSV 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919026507 646 FLTERDWYHVDpdtglpkQQIVTRQEFMTVLANIERLLIRASYHIHQTQIQFLDMAMDVAVENSTSPSImSSVE 719
Cdd:pfam00052 71 RLHEENWRDSD-------GAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPA-SWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1338-1482 |
2.75e-32 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 123.53 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1338 YWSAPRKFLGDKTLSYYGKLKFVIYFEDQDslntlpipivDHSEYRRFPLVRITGN-FRVVLDYFAPLTP--GVENEFEI 1414
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLP----------GGGSLNSEPDVILEGNgLRLSYSSPDQPPPdpGQEQTYSV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919026507 1415 FLREDQWTDplQPSKPVTREMLMVGLQNLQSIKIRASGNSNLKYAEIRGLSLQHATNASAGEAALGVE 1482
Cdd:pfam00052 71 RLHEENWRD--SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3047-3200 |
5.94e-30 |
|
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: 117.52 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 3047 GVYFSGYAYGIYDSNFVVGSNFLLTFDFRTTKPEGVILTISHPYRRPSMALELFDGQLQFTVNNEDGLifsmTEYENPFR 3126
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGS----LVLSSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 3127 LCNNKWHTVRAELVKNTIMLTVDG--VEQLSETGGSEFLATDHPLFIGGYPYYAEPQGAAqANEKFQGCIRNMKIN 3200
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGerVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP-VSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2627-2777 |
7.80e-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: 114.44 E-value: 7.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2627 VAGFHGDGYIQLTGDSLPGREADISFSFRSLQDIALLLLGLGGQADPhFYSVSLIDGKLQAKFDAGDGEVTITSDDTFND 2706
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGD-FLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919026507 2707 GMLHGVSIIRNRRKLDMFVDDLPVGTERLSKGSK--VEISSLYLGGVPADLDiASASATSQPLQGCIRDLVLN 2777
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGERVVESGSPGGSAllNLDGPLYLGGLPEDLK-SPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2443-2599 |
1.33e-28 |
|
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: 113.67 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2443 FDGTGYAEVPPIQRYDSTGYLAlFEFRTFWEDALLFFSGNKANGEYIAVELVNGKVVFSVNFGGGnNISIESREKYNTNQ 2522
Cdd:cd00110 4 FSGSSYVRLPTLPAPRTRLSIS-FSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG-SLVLSSKTPLNDGQ 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 2523 WMTVKAETQGNAGQLEVttsegrEELKRAQATASGEDSLDISNASVYFGGIPSTSKFDSFPlsVRTPFLGCMKGIQV 2599
Cdd:cd00110 82 WHSVSVERNGRSVTLSV------DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP--VSPGFVGCIRDLKV 150
|
|
| LamB |
smart00281 |
Laminin B domain; |
564-707 |
2.21e-27 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 109.27 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 564 LNPVYYWHAPAPyagskanFLGNKLASYGGNLTYSMYYVVQRledvNTAYTADLDVIMEGNELLIGYGGR-YYREGLENT 642
Cdd:smart00281 1 DNEPVYWVAPEQ-------FLGDKVTSYGGKLRYTLSFDGRR----GGTHVSAPDVILEGNGLRISHPAEgPPLPDELTT 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 643 MQVFLTERDWYHVDpdtGLPkqqiVTRQEFMTVLANIERLLIRASYHIHQTQIQFLDMAMDVAVE 707
Cdd:smart00281 70 VEVRFREENWQYYG---GRP----VTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
smart00282 |
Laminin G domain; |
3070-3201 |
1.80e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.04 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 3070 LTFDFRTTKPEGVILTISHPYRRPSMALELFDGQLQFTVNNEDGLIfsmTEYENPFRLCNNKWHTVRAELVKNTIMLTVD 3149
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPA---RLTSDPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 919026507 3150 GVEQLSET--GGSEFLATDHPLFIGGYPYYAEPQGAAQaNEKFQGCIRNMKING 3201
Cdd:smart00282 79 GGNRVSGEspGGLTILNLDGPLYLGGLPEDLKLPPLPV-TPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2882-3022 |
2.89e-26 |
|
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: 107.12 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2882 LVDRDEISSNFDIMLEFRTYYPNGLLVYLSNEDQSEYVAIQMAGGTVMTSYadqktgvpvNLTEGATVL-----VDDGKW 2956
Cdd:cd00110 12 LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRY---------DLGSGSLVLssktpLNDGQW 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919026507 2957 HKIRLMKSANNIIFKVDEGP---DIVGRIANKIDVLAPMYVGGLPRGYNMRMGLVPDSLKGCVRGFRLN 3022
Cdd:cd00110 83 HSVSVERNGRSVTLSVDGERvveSGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2893-3024 |
8.78e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 102.03 E-value: 8.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2893 DIMLEFRTYYPNGLLVYLSNEDQSEYVAIQMAGGTVMTSYadqKTGVPVNLTEGATVLVDDGKWHKIRLMKSANNIIFKV 2972
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRY---DLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 2973 DEGPDIVGRI---ANKIDVLAPMYVGGLPRGYNMRMGLVPDSLKGCVRGFRLNSQ 3024
Cdd:smart00282 78 DGGNRVSGESpggLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3074-3205 |
1.18e-24 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 101.62 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 3074 FRTTKPEGVILTISHPYRRPSMALELFDGQLQFTVNNEDGLIFSMTeyenPFRLCNNKWHTVRAELVKNTIMLTVDGVEQ 3153
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRS----GDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 3154 L---SETGGSEFLATDHPLFIGGYPYYAEPQGAAQANEKFQGCIRNMKINGAEVD 3205
Cdd:pfam00054 77 PtgeSPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2466-2599 |
3.55e-24 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 100.49 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2466 FEFRTFWEDALLFFSGNKANGEYIAVELVNGKVVFSVNFGGGNNISIESREKYNTNQWMTVKAETQGNAGQLEVTtsegr 2545
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 919026507 2546 EELKRAQATASGEDSLDIsNASVYFGGIPSTSKfdSFPLSVRTPFLGCMKGIQV 2599
Cdd:smart00282 79 GGNRVSGESPGGLTILNL-DGPLYLGGLPEDLK--LPPLPVTPGFRGCIRNLKV 129
|
|
| LamB |
smart00281 |
Laminin B domain; |
1334-1469 |
1.10e-23 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 98.87 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1334 ERPLYWSAPRKFLGDKTLSYYGKLKFVIYFEDQDSlntlpipivDHSEYRrfPLVRITGN-FRVVLDYFAPLTPGVENEF 1412
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG---------GTHVSA--PDVILEGNgLRISHPAEGPPLPDELTTV 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 1413 EIFLREDQWTDPlqPSKPVTREMLMVGLQNLQSIKIRASGNSNLKYAEIRGLSLQHA 1469
Cdd:smart00281 71 EVRFREENWQYY--GGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVA 125
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2468-2599 |
5.41e-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: 96.72 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2468 FRTFWEDALLFFSGNKaNGEYIAVELVNGKVVFSVNFGGGNNISIESREKYNTNQWMTVKAETQGNAGQLEVttsegrEE 2547
Cdd:pfam02210 1 FRTRQPNGLLLYAGGG-GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV------DG 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 2548 LKRAQATASGEDSLDISNASVYFGGIPSTSKFDSFPlsVRTPFLGCMKGIQV 2599
Cdd:pfam02210 74 QTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALP--VRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2649-2779 |
1.03e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 93.17 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2649 DISFSFRSLQDIALLLLGLGGQADPHFySVSLIDGKLQAKFDAGDGEVTITSDDT-FNDGMLHGVSIIRNRRKLDMFVDD 2727
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYL-ALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 919026507 2728 -LPVGTERLSKGSKVEI-SSLYLGGVPADLDiASASATSQPLQGCIRDLVLNGK 2779
Cdd:smart00282 80 gNRVSGESPGGLTILNLdGPLYLGGLPEDLK-LPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2898-3024 |
7.39e-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: 90.56 E-value: 7.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2898 FRTYYPNGLLVYLSNeDQSEYVAIQMAGGTVMTSYaDQKTGVPVNLTEGATVlvDDGKWHKIRLMKSANNIIFKVDEGPD 2977
Cdd:pfam02210 1 FRTRQPNGLLLYAGG-GGSDFLALELVNGRLVLRY-DLGSGPESLLSSGKNL--NDGQWHSVRVERNGNTLTLSVDGQTV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 919026507 2978 IVGRIANKIDVL---APMYVGGLPRGYNMRMGLVPDSLKGCVRGFRLNSQ 3024
Cdd:pfam02210 77 VSSLPPGESLLLnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2672-2779 |
6.93e-19 |
|
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: 85.16 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2672 DPHFYSVSLIDGKLQAKFDAGDGEVTITS-DDTFNDGMLHGVSIIRNRRKLDMFVDDLPVGTERLSKGSKV--EISSLYL 2748
Cdd:pfam02210 17 GSDFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPPGESLLlnLNGPLYL 96
|
90 100 110
....*....|....*....|....*....|.
gi 919026507 2749 GGVPADLDIaSASATSQPLQGCIRDLVLNGK 2779
Cdd:pfam02210 97 GGLPPLLLL-PALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
2260-2411 |
4.30e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 83.16 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2260 TISFNFKTnnTEKDMLLFYVQGEEKPEFMAVEIVERKLRFVWNSGGGVAmanhslQIESEETSIqPDEKWYSVIARRTAN 2339
Cdd:smart00282 1 SISFSFRT--TSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPA------RLTSDPTPL-NDGQWHRVAVERNGR 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919026507 2340 VGTLAVqkikfagnDDPALASSSSSAQFTKLDLNDRakLYVAGAP-QGTVERDPALKGgmFVGCIADVTLDGR 2411
Cdd:smart00282 72 SVTLSV--------DGGNRVSGESPGGLTILNLDGP--LYLGGLPeDLKLPPLPVTPG--FRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2255-2409 |
2.54e-16 |
|
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: 78.61 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2255 PSTTNTISFNFKTnnTEKDMLLFYVQGEEKPEFMAVEIVERKLRFVWNSGGGVAMANHSLQIEseetsiqpDEKWYSVIA 2334
Cdd:cd00110 18 PRTRLSISFSFRT--TSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLN--------DGQWHSVSV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 2335 RRTANVGTLAVqkikfagnDDPALASSSSSAQFTKLDLNDRakLYVAGAP-QGTVERDPALKGgmFVGCIADVTLD 2409
Cdd:cd00110 88 ERNGRSVTLSV--------DGERVVESGSPGGSALLNLDGP--LYLGGLPeDLKSPGLPVSPG--FVGCIRDLKVN 151
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1701-1941 |
2.07e-15 |
|
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: 78.99 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1701 VRGVNTSTMvviPWERFFAM----ENKTQVLRGKLDAIR------KVKVGDMEVI---VKELQANATKLYTQTSSMANDA 1767
Cdd:pfam06008 1 LLSLNSLTG---ALPAPYKInynlENLTKQLQEYLSPENahkiqiEILEKELSSLaqeTEELQKKATQTLAKAQQVNAES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1768 MGYSMVASNLSKTADGMEKEIREIITSARDLLDNLpdvHQLSGNvNLTSVMMKAQDIMKMIRERDFKPNIENADNELELA 1847
Cdd:pfam06008 78 ERTLGHAKELAEAIKNLIDNIKEINEKVATLGEND---FALPSS-DLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1848 KALKSSISDLQSKLTN-----VTDAAISIQELADRLNDLISLAEQSAKDSRAALELNQKNDElikklqNMTqALQTRALA 1922
Cdd:pfam06008 154 QDLLSRIQTWFQSPQEenkalANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQA------NLR-EFQRKKEE 226
|
250
....*....|....*....
gi 919026507 1923 VSSMLNMSSEMLKEANMTL 1941
Cdd:pfam06008 227 VSEQKNQLEETLKTARDSL 245
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1075-1120 |
7.60e-15 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 70.80 E-value: 7.60e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1075 CDCDVTGSTSLQCGMTSGQCPCKPGVTGQKCDQCRPGYYGFSSNGC 1120
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1074-1119 |
2.55e-14 |
|
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: 69.31 E-value: 2.55e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1074 SCDCDVTGSTSLQCGMTSGQCPCKPGVTGQKCDQCRPGYYGFSSNG 1119
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1075-1123 |
2.80e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 69.30 E-value: 2.80e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 1075 CDCDVTGSTSLQCGMTSGQCPCKPGVTGQKCDQCRPGYYGFSSNGCTEC 1123
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2129-2252 |
5.30e-14 |
|
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: 71.36 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2129 ANDNATGALEkamnTVTSVDSIQEGLDNDLKpkldvvkvntKELQDLETMTGTMMEINNNLD----GIRDVNRSIHTTLG 2204
Cdd:pfam06009 1 SKELAREANE----TAKEVLEQLAPLSQNLE----------NTSEKLSGINRSLEETNELVNdankALDDAGRSVKKLEE 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919026507 2205 ALNRL-------------NMSLSQSLEELRESIQKAREQANNIKVSLAAGGSCHREYRTEE 2252
Cdd:pfam06009 67 LAPDLldklkplkqlevnSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPI 127
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1025-1073 |
1.52e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.99 E-value: 1.52e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 1025 ACNCHLKGSNDSQCDLVTGTCTCQPNVIGDKCDQCEINYYDLDS-GNGCQ 1073
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1026-1072 |
2.98e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.18 E-value: 2.98e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 919026507 1026 CNCHLKGSNDSQCDLVTGTCTCQPNVIGDKCDQCEINYYDlDSGNGC 1072
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1747-2234 |
3.79e-13 |
|
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: 75.83 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1747 KELQANATKLYTQTSsmandamgysmvasNLSKTADGMEKEIRE---IITSARDLLDNLPDVH-----QLSGNVN-LTSV 1817
Cdd:TIGR04523 214 KSLESQISELKKQNN--------------QLKDNIEKKQQEINEkttEISNTQTQLNQLKDEQnkikkQLSEKQKeLEQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1818 MMKAQDIMKMIRErdFKPNIENADNELE--LAKALKSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQSAKDSRAA 1895
Cdd:TIGR04523 280 NKKIKELEKQLNQ--LKSEISDLNNQKEqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1896 -----LELNQKNDElIKKLQNMTQALQTralavssmlnmSSEMLKeanmtlpnSSAEFLRDLLEQLKKDTENltiaaglL 1970
Cdd:TIGR04523 358 nsekqRELEEKQNE-IEKLKKENQSYKQ-----------EIKNLE--------SQINDLESKIQNQEKLNQQ-------K 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1971 RQNLPNLEPKVRQAEELAEKLRmqADNLDNMFQGARATSEDAVKaaqvyEGIVVAVDDALKEAQSAHDLASEAMNKTTta 2050
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLK--ETIIKNNSEIKDLTNQDSVK-----ELIIKNLDNTRESLETQLKVLSRSINKIK-- 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2051 dgSTLQEKAK--KSANTSLDFVNEANR-LVNSSKDLKDLLGSIDKDIDQANKRM----DEVDSAKERLTEGMDRLPAGIH 2123
Cdd:TIGR04523 482 --QNLEQKQKelKSKEKELKKLNEEKKeLEEKVKDLTKKISSLKEKIEKLESEKkekeSKISDLEDELNKDDFELKKENL 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2124 EKLIEANDNatgALEKAMNTVTSVDSIQEGLDNDLKPKLDVVKVNTKElqdLETMTGTMMEINNNLDGIRDVNRSIHTTL 2203
Cdd:TIGR04523 560 EKEIDEKNK---EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---IEEKEKKISSLEKELEKAKKENEKLSSII 633
|
490 500 510
....*....|....*....|....*....|.
gi 919026507 2204 GALNRLNMSLSQSLEELRESIQKAREQANNI 2234
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1026-1072 |
8.44e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.07 E-value: 8.44e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 1026 CNCHLKGSNDSQCDLVTGTCTCQPNVIGDKCDQCEINYYDL--DSGNGC 1072
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1170-1218 |
3.69e-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: 63.14 E-value: 3.69e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 1170 CNCNMTGSLDTQCDTVDGQCECRPEYDGMKCDMCRFGHFGFPNCRPCHC 1218
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1170-1211 |
2.33e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.83 E-value: 2.33e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 919026507 1170 CNCNMTGSLDTQCDTVDGQCECRPEYDGMKCDMCRFGHFGFP 1211
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
978-1023 |
3.31e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.31e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 978 CSCNLTGSVSNLCDQVSGQCPCKNGVGGQYCGSCLPDHWEYSEEGC 1023
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1779-2236 |
4.72e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1779 KTADGMEKEIREIITSARDLLDnlpDVHQLSGNVNLTSVMMKAQDIMKMIRERDFKPNIENADNELELAKALKSSISDLQ 1858
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEK---RLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1859 SKLTnvtdAAIS-----IQELADRLNDLIS-----------LAEQSAKD--SRAALELNQKNDELiKKLQNMTQALQTRA 1920
Cdd:PRK03918 408 SKIT----ARIGelkkeIKELKKAIEELKKakgkcpvcgreLTEEHRKEllEEYTAELKRIEKEL-KEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1921 LAVSSMLNMSSEMLKEANMtlpnssAEFLRDLLEQLKKdtenltiaagllrQNLPNLEPKVRQAEELAEKLrmqadnldN 2000
Cdd:PRK03918 483 RELEKVLKKESELIKLKEL------AEQLKELEEKLKK-------------YNLEELEKKAEEYEKLKEKL--------I 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2001 MFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSA----HDLASEAMNKTTTADGSTLQEKAKksantsldFVNEANRL 2076
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEELEERLKELEP--------FYNEYLEL 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2077 VNSSKDLKDLLGSIDK---DIDQANKRMDEVDSAKERLTEGMDRLP--------AGIHEKLIEANDNATGALEKAMNTVT 2145
Cdd:PRK03918 608 KDAEKELEREEKELKKleeELDKAFEELAETEKRLEELRKELEELEkkyseeeyEELREEYLELSRELAGLRAELEELEK 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2146 SVDSIQEGLDnDLKPKLDVVKVNTKELQDLETMTGTMMEINNNldgIRDVNRSIhtTLGALNRLNMSLSQSLEELRE--- 2222
Cdd:PRK03918 688 RREEIKKTLE-KLKEELEEREKAKKELEKLEKALERVEELREK---VKKYKALL--KERALSKVGEIASEIFEELTEgky 761
|
490
....*....|....
gi 919026507 2223 SIQKAREQANNIKV 2236
Cdd:PRK03918 762 SGVRVKAEENKVKL 775
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2265-2411 |
6.30e-11 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 62.44 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2265 FKTnnTEKDMLLFYVqGEEKPEFMAVEIVERKLRFVWNSGGGVAmanhslQIESEETSIQpDEKWYSVIARRTANVGTLA 2344
Cdd:pfam02210 1 FRT--RQPNGLLLYA-GGGGSDFLALELVNGRLVLRYDLGSGPE------SLLSSGKNLN-DGQWHSVRVERNGNTLTLS 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 2345 VqkikfagnDDPALASSSSSAQFTKLDLNDRakLYVAGAPQGTVERDPALKGGmFVGCIADVTLDGR 2411
Cdd:pfam02210 71 V--------DGQTVVSSLPPGESLLLNLNGP--LYLGGLPPLLLLPALPVRAG-FVGCIRDVRVNGE 126
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1634-1672 |
1.20e-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: 1.20e-10
10 20 30
....*....|....*....|....*....|....*....
gi 919026507 1634 PCDCSEDGSLDNLCDRESGQCICHPGVLGRACDQCQPRY 1672
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1170-1213 |
1.79e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 1.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1170 CNCNMTGSLDTQCDTVDGQCECRPEYDGMKCDMCRFGHFG--FPNC 1213
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1525-1574 |
3.63e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.63e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 919026507 1525 PCECHGHSDM---CNKETGVCLnCAHNTAGDHCNTCAEGYYGNATSGREdaCQ 1574
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1635-1672 |
6.46e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 6.46e-10
10 20 30
....*....|....*....|....*....|....*...
gi 919026507 1635 CDCSEDGSLDNLCDRESGQCICHPGVLGRACDQCQPRY 1672
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
977-1024 |
6.99e-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: 6.99e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 977 RCSCNLTGSVSNLCDQVSGQCPCKNGVGGQYCGSCLPDHWEYSE--EGCK 1024
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
931-968 |
8.67e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 8.67e-10
10 20 30
....*....|....*....|....*....|....*...
gi 919026507 931 CDCNQYGSTGTSCDQRSGQCSCRPYYEGRACDSCVAGY 968
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
931-980 |
8.97e-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: 56.59 E-value: 8.97e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 931 CDCNQYGSTGTSCDQRSGQCSCRPYYEGRACDSCVAGYGNiIAGCPRCSC 980
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1863-2198 |
1.18e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.38 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1863 NVTDAAISIQELADRLNDLIS-LAEQSAKDSRAALELNQKNDELiKKLQNMTQALQTRALAVSSMLNMSSEMLKEANmtl 1941
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREeLEQAREELEQLEEELEQARSEL-EQLEEELEELNEQLQAAQAELAQAQEELESLQ--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1942 pnSSAEFLRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAEKLRMQADNLDNMFQGARATSEdAVKAAQVYEG 2021
Cdd:COG4372 108 --EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ-ALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2022 IVVAVDDALKEAQSAHDLAsEAMNKTTTADGSTLQEKAKKSANTSLDFVNEANRLVNSSKDLKDLLGSIDKDIDQANKRM 2101
Cdd:COG4372 185 LDELLKEANRNAEKEEELA-EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2102 DEVDSAKERLTEGMDRLPAGIHEKLIEANDnatGALEKAMNTVTSVDSIQEGLDNDLKPKLDVVKVNTKELQDLETMTGT 2181
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAAL---ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330 340
....*....|....*....|
gi 919026507 2182 ---MMEINNNLDGIRDVNRS 2198
Cdd:COG4372 341 dllQLLLVGLLDNDVLELLS 360
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1216-1271 |
1.22e-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: 56.21 E-value: 1.22e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 1216 CHCNENGTVMSDCNakghcqcQEDGQCPCRGNVEGLKCKHCKEGSFSLQSNNPEGC 1271
Cdd:pfam00053 1 CDCNPHGSLSDTCD-------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1526-1578 |
1.30e-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: 55.82 E-value: 1.30e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 1526 CECHGH---SDMCNKETGVCLnCAHNTAGDHCNTCAEGYYGNATsgredaCQPCGC 1578
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS------DPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1635-1672 |
2.06e-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: 55.44 E-value: 2.06e-09
10 20 30
....*....|....*....|....*....|....*...
gi 919026507 1635 CDCSEDGSLDNLCDRESGQCICHPGVLGRACDQCQPRY 1672
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
978-1026 |
2.39e-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: 2.39e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 978 CSCNLTGSVSNLCDQVSGQCPCKNGVGGQYCGSCLPDHWEYSEEGCKAC 1026
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
931-975 |
5.56e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.24 E-value: 5.56e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 931 CDCNQYGSTGTSCDQRSGQCSCRPYYEGRACDSCVAGY-GNIIAGC 975
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYyGDGPPGC 46
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1837-2082 |
5.95e-09 |
|
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: 59.73 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1837 IENADNELElakALKSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQSAKDSRAALElnqkndELIKKLQNMTQAL 1916
Cdd:pfam06008 42 IEILEKELS---SLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIK------EINEKVATLGEND 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1917 QtrALAVSSMlnmsSEMLKEANMTLPNSSAeflRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAEKLRMQAD 1996
Cdd:pfam06008 113 F--ALPSSDL----SRMLAEAQRMLGEIRS---RDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1997 NLDNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSAHDLASEAMNKTTtadgstlqekakKSANTSLDFVNEANRL 2076
Cdd:pfam06008 184 EYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLE------------ETLKTARDSLDAANLL 251
|
....*.
gi 919026507 2077 VNSSKD 2082
Cdd:pfam06008 252 LQEIDD 257
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
457-504 |
6.26e-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: 54.28 E-value: 6.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 919026507 457 PCPCSRAGSRNvDTC---QGDCICKPNVVGENCDQCKPGFFNmEASNPAGC 504
Cdd:cd00055 1 PCDCNGHGSLS-GQCdpgTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1838-2124 |
7.28e-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: 62.00 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1838 ENADNELELAKALKSSISDLQSKLTNVTDAA-ISIQELADRLNDL-ISLAEQSAKDSRAALELNQKNDELIKKLQNMtQA 1915
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLeAEVEQLEERIAQLsKELTELEAEIEELEERLEEAEEELAEAEAEI-EE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1916 LQTRALAVSSMLNMSSEMLKEANMTLPNSSAEF--LRDLLEQLKKDTENLTIAAGLLRQ-------NLPNLEPKVRQAEE 1986
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAanLRERLESLERRIAATERRLEDLEEqieelseDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1987 LAEKLRMQADNLDNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSAHDLASEAMNK------TTTADGSTLQEKAK 2060
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQlelrleGLEVRIDNLQERLS 946
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919026507 2061 KSANTSLDFV-NEANRLVNSSKDLKDLLGSIDKDID--------------QANKRMDEVDSAKERLTEGMDRLPAGIHE 2124
Cdd:TIGR02168 947 EEYSLTLEEAeALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
458-504 |
9.49e-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: 53.51 E-value: 9.49e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 458 CPCSRAGSRNvDTC---QGDCICKPNVVGENCDQCKPGFFNMEASNPAGC 504
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. |
768-815 |
1.86e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.86e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 919026507 768 CNCNNHA---DTCEASSGLCtSCRDNTVGPHCENCEFGYYGNATrGTPNDC 815
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
458-504 |
3.00e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.00e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 458 CPCSRAGSRNvDTC---QGDCICKPNVVGENCDQCKPGFFNmeaSNPAGC 504
Cdd:smart00180 1 CDCDPGGSAS-GTCdpdTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
768-816 |
5.40e-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: 51.59 E-value: 5.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 768 CNCNNHAD---TCEASSGLCTsCRDNTVGPHCENCEFGYYGNATRgtPNDCR 816
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1215-1272 |
6.01e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 6.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 919026507 1215 PCHCNENGTVMSDCNakghcqcQEDGQCPCRGNVEGLKCKHCKEGSFSLQSnNPEGCT 1272
Cdd:cd00055 1 PCDCNGHGSLSGQCD-------PGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1526-1568 |
1.09e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.09e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1526 CECHG---HSDMCNKETGVCLnCAHNTAGDHCNTCAEGYYGNATSG 1568
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
404-460 |
5.98e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 5.98e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 919026507 404 CQCSQLGS-TGTCVQdnsrrgeglMPGDCICRVGFGGRNCDRCASGYKNFPSCIPCPC 460
Cdd:pfam00053 1 CDCNPHGSlSDTCDP---------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1850-2230 |
5.99e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1850 LKSSISDLQSKLT-----------NVTDAAISIQELADRLNDLISLAEQSAKDSRAaleLNQKNDELIKKLQNMTQALQT 1918
Cdd:PRK02224 256 LEAEIEDLRETIAeterereelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEA---VEARREELEDRDEELRDRLEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1919 RALAVSSMlnmssemlkeanmtlpNSSAEFLRDLLEQLKKDTENLTIAAGllrqnlpNLEPKVRQAEELAEKLRMQADNL 1998
Cdd:PRK02224 333 CRVAAQAH----------------NEEAESLREDADDLEERAEELREEAA-------ELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1999 DNMFQGARATSEDAvkaaqvyegivvavDDALKEAQSAHDLASEAMN------KTTTADGSTLQEKakksantsldfVNE 2072
Cdd:PRK02224 390 EEEIEELRERFGDA--------------PVDLGNAEDFLEELREERDelrereAELEATLRTARER-----------VEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2073 ANRLVNSSK------DLKD--LLGSIDKDIDQANKRMDEVDSAKERLTEGMDRLPAGihEKLIEANDNATGALEKAMNTV 2144
Cdd:PRK02224 445 AEALLEAGKcpecgqPVEGspHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA--EDLVEAEDRIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2145 TSVDSIQEGLDNDlKPKLDVVKVNTKELQD-----LETMTGTMMEINNNLDGIRDVNR---SIHTTLGALNRLNMSLSQs 2216
Cdd:PRK02224 523 ELIAERRETIEEK-RERAEELRERAAELEAeaeekREAAAEAEEEAEEAREEVAELNSklaELKERIESLERIRTLLAA- 600
|
410
....*....|....
gi 919026507 2217 LEELRESIQKAREQ 2230
Cdd:PRK02224 601 IADAEDEIERLREK 614
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1122-1168 |
6.38e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 6.38e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 919026507 1122 ECPVCPVAGQVCDAVTGECVCPTNTEGDRCERCVPDTWGHD-QLLGCK 1168
Cdd:cd00055 3 DCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
878-921 |
1.00e-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: 47.73 E-value: 1.00e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 919026507 878 PCACSGNINPNavGNCDRTTGQCLkCLFNTEGWNCAQCKPDYYG 921
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1216-1271 |
1.38e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.38e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 1216 CHCNENGTVMSDCNakghcqcQEDGQCPCRGNVEGLKCKHCKEGSFslqSNNPEGC 1271
Cdd:smart00180 1 CDCDPGGSASGTCD-------PDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1714-2122 |
1.65e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1714 WERFFAMENKTQVLRGKLDAIRKvKVGDMEVIVKELQANATKLYTQTSSMANDAMGYSMVASNLSKTADGMEKEIREIIT 1793
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRK-ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1794 SARDLLDNL----PDVHQLSGN-VNLTSVMMKAQDIMKMIRERdfkpnIENADNELelaKALKSSISDLQSKLTNVTDAA 1868
Cdd:TIGR02168 762 EIEELEERLeeaeEELAEAEAEiEELEAQIEQLKEELKALREA-----LDELRAEL---TLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1869 ISIQELADRLNDLISLAEQSAKDSRAALE-----LNQKNDELIKKLQNMTQALQTRALAVSSMLNMSSEmlkeanmtlpn 1943
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEeleelIEELESELEALLNERASLEEALALLRSELEELSEE----------- 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1944 ssaefLRDLLEQLKKdtenltiaaglLRQNLPNLEPKVRQAEELAEKLRMQADNLDNMFqgaratSEDAVKAAQVYEGIV 2023
Cdd:TIGR02168 903 -----LRELESKRSE-----------LRRELEELREKLAQLELRLEGLEVRIDNLQERL------SEEYSLTLEEAEALE 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2024 VAVDDALKEAQSAHDLASEAMNKTTTADGSTLQEkaKKSANTSLDFVNEANRLVNSSKdlKDLLGSIDK-D--------- 2093
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELGPVNLAAIEE--YEELKERYDFLTAQKEDLTEAK--ETLEEAIEEiDrearerfkd 1036
|
410 420 430
....*....|....*....|....*....|....*..
gi 919026507 2094 -IDQANKRMDEV-------DSAKERLTEGMDRLPAGI 2122
Cdd:TIGR02168 1037 tFDQVNENFQRVfpklfggGEAELRLTDPEDLLEAGI 1073
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1799-1963 |
3.12e-06 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 50.87 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1799 LDNLPDvhQLSGNVNLTSVMMkaQDIMKMIRErdfkPNIENADNELELAKALKSSISDLQSKLTNVTDAAISIQELADRL 1878
Cdd:cd21116 57 LLSLPN--DIIGYNNTFQSYY--PDLIELADN----LIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1879 ND----LISLAEQSAKDSRAALELNQKNDELIKKLQNMTQALQTRALAVSSMLNMSSEMLKEANMTLPNSSAEFLRDLLE 1954
Cdd:cd21116 129 DDdsrnLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAFLQADLK 208
|
....*....
gi 919026507 1955 QLKKDTENL 1963
Cdd:cd21116 209 AAKADWNQL 217
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
403-454 |
3.28e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 3.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 919026507 403 PCQCSQLGS-TGTCVQDNsrrgeglmpGDCICRVGFGGRNCDRCASGYKNFPS 454
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
768-815 |
4.44e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 4.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 919026507 768 CNCN---NHADTCEASSGLCTsCRDNTVGPHCENCEFGYYGNatrgTPNDC 815
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD----GPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1122-1167 |
5.91e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 5.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1122 ECPVCPVAGQVCDAVTGECVCPTNTEGDRCERCVPDTWGhDQLLGC 1167
Cdd:smart00180 2 DCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1122-1160 |
9.15e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.04 E-value: 9.15e-06
10 20 30
....*....|....*....|....*....|....*....
gi 919026507 1122 ECPVCPVAGQVCDAVTGECVCPTNTEGDRCERCVPDTWG 1160
Cdd:pfam00053 2 DCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
879-928 |
1.27e-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: 44.65 E-value: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 879 CACSGNINPNavGNCDRTTGQCLkCLFNTEGWNCAQCKPDYYG--MVYGKGC 928
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGlpSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
404-455 |
1.88e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 404 CQCSQLGS-TGTCVQDNsrrgeglmpGDCICRVGFGGRNCDRCASGY--KNFPSC 455
Cdd:smart00180 1 CDCDPGGSaSGTCDPDT---------GQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
280-327 |
2.38e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.88 E-value: 2.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 280 CKCYGHASSCPR-SPDTGKlmCVCEDNTCGKNCEKCCPKFNQQPYKPGT 327
Cdd:cd00055 2 CDCNGHGSLSGQcDPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PHA03413 |
PHA03413 |
putative internal core protein; Provisional |
1687-2135 |
4.84e-05 |
|
putative internal core protein; Provisional
Pssm-ID: 177641 Cd Length: 1304 Bit Score: 49.31 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1687 TRDLMVAVDEMEVMVRGVNTSTMVVIPWERFFAmenktqvlrgkldaiRKVKVGDMEVIVKELQANATKLYTQTSSMAND 1766
Cdd:PHA03413 227 AKAVRAAANAAEVESRALGSATEHVFTAETGLA---------------AKAQTGGVLSDAPEIVPDVVKPEVAAEPMFDP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1767 AMGYSMVASNLSKTADGMEKEIREIITSARDlldnlpDVHQLSGNvNLTSVMMKAQDIMKMIRERDfkpniENADNELEL 1846
Cdd:PHA03413 292 DAPTNETAEDAKVPGTGEGEESFPILDKPLD------ERIQASRN-GRASVNIKAQDLVQFLKNMD-----HLSAGAKAI 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1847 AKALKSSISDLQSKLTNVT----DAAISIQELADRlnDLISLAEQSAKD----SRAALELNQKN-DELIKKLQNMTQALQ 1917
Cdd:PHA03413 360 LDALGDAINDIDFKLMAASanrsRYTFAQQDLAKR--EEIKLRAPAKADgstfKTVGDALNAMDaDTSRVAVHELIHAAT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1918 TRALAVSSMLNMSSEMlkeanmtlpnssAEFLRDLLE---QLKKDTE---NLTIAAGLLRQNLPNLEPKVRQAEELAE-- 1989
Cdd:PHA03413 438 AKAIFQASKGDSAPEI------------ADAIKDLDAlhaSIAADREfapKMRYAASNNHEFLAELADKPEMVEDLAKlp 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1990 -------KLRMQADNLDNM--FQGARATSEDAVKAaqvYEGIV-VAVDDALKEAQS-----AHDLASEAMNKTTTAD-GS 2053
Cdd:PHA03413 506 gvpagknALQALAEKILKAlgFKAKGSALDDALDA---FEDAAkWQAKDNADKANAffsdaFADLADDANRGANAAErAK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2054 TLQEKAKKSANTSLDFVNEANRlvnSSKDLKDLLGSidkDIDQANKRMDEVDSAKERLTEGMDRLPAGIHEKLIEANDNA 2133
Cdd:PHA03413 583 ALEDGAKKKLKQMFALWDNIAQ---GNEDLAKLLVS---DASAMGERAPSVVDHKRNLTLEMDARAAAVEDAILAALKDK 656
|
..
gi 919026507 2134 TG 2135
Cdd:PHA03413 657 HG 658
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1749-2118 |
1.33e-04 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 47.71 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1749 LQANATKLYTQTSSMANDAMGYSMVASNLSKTADGMEKEIREIITSARDLLDNLPDVHQLSGNVNLTSVMMKAQDIMKMI 1828
Cdd:COG0840 2 LILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1829 RERDFKPNIENADNELELAKALKSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQSAKDSRAALELNQKNDELIKK 1908
Cdd:COG0840 82 LALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1909 LQNMTQALQTRALAVSSMLNMSSEMLKEANMTLPNSSAEFL-RDLLEQLKKDTENL-TIAAGLLRQNLPnlepkVRQAEE 1986
Cdd:COG0840 162 ALAALLEAAALALAAAALALALLAAALLALVALAIILALLLsRSITRPLRELLEVLeRIAEGDLTVRID-----VDSKDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1987 ---LAEKLRMQADNLDNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSAHDLASEAMNKTTtadgSTLQEKAKkSA 2063
Cdd:COG0840 237 igqLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELS----ATVQEVAE-NA 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 2064 NTSLDFVNEANRLVNSSKDLkdllgsidkdIDQANKRMDEVDSAKERLTEGMDRL 2118
Cdd:COG0840 312 QQAAELAEEASELAEEGGEV----------VEEAVEGIEEIRESVEETAETIEEL 356
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1998-2194 |
1.74e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.59 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1998 LDNMFQGARATSEDAVKAAQvyEGIVVAVDDALKEAQSAHDLASEAMNKTTTADGSTLQEKAK-KSANTSLD--FVNEAN 2074
Cdd:cd22656 97 LELIDDLADATDDEELEEAK--KTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAlETLEKALKdlLTDEGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2075 RLVNssKDLKDLlgsiDKDIDQANKrmDEVDSAKERLtegmdrlpagihEKLIEANDNATGALEKAMNTVTSVDSIQEGL 2154
Cdd:cd22656 175 AIAR--KEIKDL----QKELEKLNE--EYAAKLKAKI------------DELKALIADDEAKLAAALRLIADLTAADTDL 234
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 919026507 2155 DNdLKPKLDVVkvntkeLQDLETMTGTMMEINNNLDGIRD 2194
Cdd:cd22656 235 DN-LLALIGPA------IPALEKLQGAWQAIATDLDSLKD 267
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
879-928 |
3.55e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 3.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 879 CACS--GNINPNavgnCDRTTGQCLkCLFNTEGWNCAQCKPDYYGmVYGKGC 928
Cdd:smart00180 1 CDCDpgGSASGT----CDPDTGQCE-CKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1812-1915 |
4.61e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 42.96 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1812 VNLTSVMMK---AQDIMKMIrERDFKPNienaDNELE-LAKALKSSISDLQSKLTNVTDAAIsiQELADRLNDLISLAEQ 1887
Cdd:smart00935 4 VDVQKILQEspaGKAAQKQL-EKEFKKR----QAELEkLEKELQKLKEKLQKDAATLSEAAR--EKKEKELQKKVQEFQR 76
|
90 100
....*....|....*....|....*...
gi 919026507 1888 SAKDSRAalELNQKNDELIKKLQNMTQA 1915
Cdd:smart00935 77 KQQKLQQ--DLQKRQQEELQKILDKINK 102
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1605-1632 |
9.28e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 9.28e-04
10 20
....*....|....*....|....*...
gi 919026507 1605 CPRGYEGDHCERCSDYFYGDPTKLGGEC 1632
Cdd:pfam00053 22 CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
848-876 |
1.27e-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: 39.26 E-value: 1.27e-03
10 20
....*....|....*....|....*....
gi 919026507 848 SCPDGYIGNHCEMCDDGYFGNPLVPGNYC 876
Cdd:pfam00053 21 LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
368-401 |
1.87e-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: 1.87e-03
10 20 30
....*....|....*....|....*....|....
gi 919026507 368 GGVCMnCRDHTTGVNCEQCEAGYYRTTDDPREPC 401
Cdd:pfam00053 17 TGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1576-1625 |
2.30e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 2.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 1576 CGCPrlePQNNFSPTCVtnatADGYVCNaCPRGYEGDHCERCSDYFYGDP 1625
Cdd:smart00180 1 CDCD---PGGSASGTCD----PDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1575-1630 |
2.87e-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: 38.10 E-value: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 1575 PCGCPrlePQNNFSPTCVtnatADGYVCNaCPRGYEGDHCERCSDYFYGDPTKLGG 1630
Cdd:cd00055 1 PCDCN---GHGSLSGQCD----PGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| YaaN |
COG3853 |
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms]; |
2108-2229 |
3.92e-03 |
|
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms];
Pssm-ID: 443062 Cd Length: 389 Bit Score: 42.57 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2108 KERLTEGMDRLPAGIH--EKLIEANDNATGALEKAMNTVTSVDSIQEgLdNDLKPKLDVVKvntKELQDLET-MTGTM-- 2182
Cdd:COG3853 178 YEKNWEYFKELNQYIAagELKLEELEAKIPALAAEAEASGDPEDAQA-L-NDLEQVLFRLE---QRVHDLLLqRAVSIqg 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 2183 -----MEINNNLDGIRDVNRSIHTTLGALnRLNMSLSQSLEELRESIQKARE 2229
Cdd:COG3853 253 apqirLVQKNNQELIEKIQSAITTTIPLW-KNQVAVALALARQKLALDAQKA 303
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
367-402 |
4.60e-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: 37.72 E-value: 4.60e-03
10 20 30
....*....|....*....|....*....|....*.
gi 919026507 367 GGGVCMnCRDHTTGVNCEQCEAGYYRTTDDPREpCQ 402
Cdd:cd00055 17 GTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
32-278 |
3.41e-87 |
|
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: 285.02 E-value: 3.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 32 FPVIFNLATEADITSNATCGETGPETYCKLVEHVKQLMmknyQCGICDANGdlPYQRHPIQNAIDGSN----RWWQSPSL 107
Cdd:smart00136 8 YPPFVNLAFGREVTATSTCGEPGPERYCKLVGHTEQGK----KCDYCDARN--PRRSHPAENLTDGNNpnnpTWWQSEPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 108 ANGWQYdwVTITLDLGQAFQIAYVIVKAAnSPRPANWILERSVDGITFTPWQYFAlsdGECWNAFGVPPTVGRPRYRrDD 187
Cdd:smart00136 82 SNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITKGN-ED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 188 EVICTSFYSRLDPIENGEIHTSLVNGRPGAVNGP-SDLLLEFTTARFLRLRLQKIRTLNADLMTIRTSnpdkidkaVTRR 266
Cdd:smart00136 155 EVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDnSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPE--------VTRR 226
|
250
....*....|..
gi 919026507 267 YFYSIKDISIGG 278
Cdd:smart00136 227 YYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
32-278 |
1.29e-83 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 274.46 E-value: 1.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 32 FPVIFNLATEADITSNATCGETGPETYCKLVEHvkqlmMKNYQCGICDANgdLPYQRHPIQNAIDGSNR----WWQSPSL 107
Cdd:pfam00055 2 YPAFGNLAFGREVSATSTCGLNGPERYCILSGL-----EGGKKCFICDSR--DPHNSHPPSNLTDSNNGtnetWWQSETG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 108 ANgwQYDWVTITLDLGQAFQIAYVIVKAAnSPRPANWILERSVD-GITFTPWQYFAlsdGECWNAFGVPPtvGRPRYRRD 186
Cdd:pfam00055 75 VI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPS--GPSRGIKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 187 DEVICTSFYSRLDPIENGEIHTSLVNGRPGAVN-GPSDLLLEFTTARFLRLRLQKIRTLNADLMTirtsnpdkiDKAVTR 265
Cdd:pfam00055 147 DEVICTSEYSDISPLTGGEVIFSTLEGRPSANIfDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVLR 217
|
250
....*....|...
gi 919026507 266 RYFYSIKDISIGG 278
Cdd:pfam00055 218 KYYYAISDISVGG 230
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
569-719 |
3.69e-33 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 126.23 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 569 YWHAPAPyagskanFLGNKLASYGGNLTYSMYYVVQRLEDVNTAYTadlDVIMEGNELLIGYGGR---YYREGLENTMQV 645
Cdd:pfam00052 1 YWSAPEQ-------FLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEP---DVILEGNGLRLSYSSPdqpPPDPGQEQTYSV 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919026507 646 FLTERDWYHVDpdtglpkQQIVTRQEFMTVLANIERLLIRASYHIHQTQIQFLDMAMDVAVENSTSPSImSSVE 719
Cdd:pfam00052 71 RLHEENWRDSD-------GAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPA-SWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1338-1482 |
2.75e-32 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 123.53 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1338 YWSAPRKFLGDKTLSYYGKLKFVIYFEDQDslntlpipivDHSEYRRFPLVRITGN-FRVVLDYFAPLTP--GVENEFEI 1414
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLP----------GGGSLNSEPDVILEGNgLRLSYSSPDQPPPdpGQEQTYSV 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919026507 1415 FLREDQWTDplQPSKPVTREMLMVGLQNLQSIKIRASGNSNLKYAEIRGLSLQHATNASAGEAALGVE 1482
Cdd:pfam00052 71 RLHEENWRD--SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3047-3200 |
5.94e-30 |
|
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: 117.52 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 3047 GVYFSGYAYGIYDSNFVVGSNFLLTFDFRTTKPEGVILTISHPYRRPSMALELFDGQLQFTVNNEDGLifsmTEYENPFR 3126
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGS----LVLSSKTP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 3127 LCNNKWHTVRAELVKNTIMLTVDG--VEQLSETGGSEFLATDHPLFIGGYPYYAEPQGAAqANEKFQGCIRNMKIN 3200
Cdd:cd00110 77 LNDGQWHSVSVERNGRSVTLSVDGerVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP-VSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2627-2777 |
7.80e-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: 114.44 E-value: 7.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2627 VAGFHGDGYIQLTGDSLPGREADISFSFRSLQDIALLLLGLGGQADPhFYSVSLIDGKLQAKFDAGDGEVTITSDDTFND 2706
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGD-FLALELEDGRLVLRYDLGSGSLVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919026507 2707 GMLHGVSIIRNRRKLDMFVDDLPVGTERLSKGSK--VEISSLYLGGVPADLDiASASATSQPLQGCIRDLVLN 2777
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGERVVESGSPGGSAllNLDGPLYLGGLPEDLK-SPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2443-2599 |
1.33e-28 |
|
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: 113.67 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2443 FDGTGYAEVPPIQRYDSTGYLAlFEFRTFWEDALLFFSGNKANGEYIAVELVNGKVVFSVNFGGGnNISIESREKYNTNQ 2522
Cdd:cd00110 4 FSGSSYVRLPTLPAPRTRLSIS-FSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG-SLVLSSKTPLNDGQ 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 2523 WMTVKAETQGNAGQLEVttsegrEELKRAQATASGEDSLDISNASVYFGGIPSTSKFDSFPlsVRTPFLGCMKGIQV 2599
Cdd:cd00110 82 WHSVSVERNGRSVTLSV------DGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLP--VSPGFVGCIRDLKV 150
|
|
| LamB |
smart00281 |
Laminin B domain; |
564-707 |
2.21e-27 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 109.27 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 564 LNPVYYWHAPAPyagskanFLGNKLASYGGNLTYSMYYVVQRledvNTAYTADLDVIMEGNELLIGYGGR-YYREGLENT 642
Cdd:smart00281 1 DNEPVYWVAPEQ-------FLGDKVTSYGGKLRYTLSFDGRR----GGTHVSAPDVILEGNGLRISHPAEgPPLPDELTT 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 643 MQVFLTERDWYHVDpdtGLPkqqiVTRQEFMTVLANIERLLIRASYHIHQTQIQFLDMAMDVAVE 707
Cdd:smart00281 70 VEVRFREENWQYYG---GRP----VTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| LamG |
smart00282 |
Laminin G domain; |
3070-3201 |
1.80e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 107.04 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 3070 LTFDFRTTKPEGVILTISHPYRRPSMALELFDGQLQFTVNNEDGLIfsmTEYENPFRLCNNKWHTVRAELVKNTIMLTVD 3149
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPA---RLTSDPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 919026507 3150 GVEQLSET--GGSEFLATDHPLFIGGYPYYAEPQGAAQaNEKFQGCIRNMKING 3201
Cdd:smart00282 79 GGNRVSGEspGGLTILNLDGPLYLGGLPEDLKLPPLPV-TPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2882-3022 |
2.89e-26 |
|
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: 107.12 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2882 LVDRDEISSNFDIMLEFRTYYPNGLLVYLSNEDQSEYVAIQMAGGTVMTSYadqktgvpvNLTEGATVL-----VDDGKW 2956
Cdd:cd00110 12 LPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRY---------DLGSGSLVLssktpLNDGQW 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919026507 2957 HKIRLMKSANNIIFKVDEGP---DIVGRIANKIDVLAPMYVGGLPRGYNMRMGLVPDSLKGCVRGFRLN 3022
Cdd:cd00110 83 HSVSVERNGRSVTLSVDGERvveSGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2893-3024 |
8.78e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 102.03 E-value: 8.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2893 DIMLEFRTYYPNGLLVYLSNEDQSEYVAIQMAGGTVMTSYadqKTGVPVNLTEGATVLVDDGKWHKIRLMKSANNIIFKV 2972
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRY---DLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 2973 DEGPDIVGRI---ANKIDVLAPMYVGGLPRGYNMRMGLVPDSLKGCVRGFRLNSQ 3024
Cdd:smart00282 78 DGGNRVSGESpggLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3074-3205 |
1.18e-24 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 101.62 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 3074 FRTTKPEGVILTISHPYRRPSMALELFDGQLQFTVNNEDGLIFSMTeyenPFRLCNNKWHTVRAELVKNTIMLTVDGVEQ 3153
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRS----GDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 3154 L---SETGGSEFLATDHPLFIGGYPYYAEPQGAAQANEKFQGCIRNMKINGAEVD 3205
Cdd:pfam00054 77 PtgeSPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2466-2599 |
3.55e-24 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 100.49 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2466 FEFRTFWEDALLFFSGNKANGEYIAVELVNGKVVFSVNFGGGNNISIESREKYNTNQWMTVKAETQGNAGQLEVTtsegr 2545
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 919026507 2546 EELKRAQATASGEDSLDIsNASVYFGGIPSTSKfdSFPLSVRTPFLGCMKGIQV 2599
Cdd:smart00282 79 GGNRVSGESPGGLTILNL-DGPLYLGGLPEDLK--LPPLPVTPGFRGCIRNLKV 129
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3074-3201 |
3.98e-24 |
|
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: 100.19 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 3074 FRTTKPEGVILtISHPYRRPSMALELFDGQLQFTVNNEDGlifSMTEYENPFRLCNNKWHTVRAELVKNTIMLTVDGVEQ 3153
Cdd:pfam02210 1 FRTRQPNGLLL-YAGGGGSDFLALELVNGRLVLRYDLGSG---PESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 919026507 3154 LSE--TGGSEFLATDHPLFIGGYPyYAEPQGAAQANEKFQGCIRNMKING 3201
Cdd:pfam02210 77 VSSlpPGESLLLNLNGPLYLGGLP-PLLLLPALPVRAGFVGCIRDVRVNG 125
|
|
| LamB |
smart00281 |
Laminin B domain; |
1334-1469 |
1.10e-23 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 98.87 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1334 ERPLYWSAPRKFLGDKTLSYYGKLKFVIYFEDQDSlntlpipivDHSEYRrfPLVRITGN-FRVVLDYFAPLTPGVENEF 1412
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG---------GTHVSA--PDVILEGNgLRISHPAEGPPLPDELTTV 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 1413 EIFLREDQWTDPlqPSKPVTREMLMVGLQNLQSIKIRASGNSNLKYAEIRGLSLQHA 1469
Cdd:smart00281 71 EVRFREENWQYY--GGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVA 125
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2468-2599 |
5.41e-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: 96.72 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2468 FRTFWEDALLFFSGNKaNGEYIAVELVNGKVVFSVNFGGGNNISIESREKYNTNQWMTVKAETQGNAGQLEVttsegrEE 2547
Cdd:pfam02210 1 FRTRQPNGLLLYAGGG-GSDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV------DG 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 2548 LKRAQATASGEDSLDISNASVYFGGIPSTSKFDSFPlsVRTPFLGCMKGIQV 2599
Cdd:pfam02210 74 QTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALP--VRAGFVGCIRDVRV 123
|
|
| LamG |
smart00282 |
Laminin G domain; |
2649-2779 |
1.03e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 93.17 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2649 DISFSFRSLQDIALLLLGLGGQADPHFySVSLIDGKLQAKFDAGDGEVTITSDDT-FNDGMLHGVSIIRNRRKLDMFVDD 2727
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYL-ALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 919026507 2728 -LPVGTERLSKGSKVEI-SSLYLGGVPADLDiASASATSQPLQGCIRDLVLNGK 2779
Cdd:smart00282 80 gNRVSGESPGGLTILNLdGPLYLGGLPEDLK-LPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2898-3024 |
7.39e-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: 90.56 E-value: 7.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2898 FRTYYPNGLLVYLSNeDQSEYVAIQMAGGTVMTSYaDQKTGVPVNLTEGATVlvDDGKWHKIRLMKSANNIIFKVDEGPD 2977
Cdd:pfam02210 1 FRTRQPNGLLLYAGG-GGSDFLALELVNGRLVLRY-DLGSGPESLLSSGKNL--NDGQWHSVRVERNGNTLTLSVDGQTV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 919026507 2978 IVGRIANKIDVL---APMYVGGLPRGYNMRMGLVPDSLKGCVRGFRLNSQ 3024
Cdd:pfam02210 77 VSSLPPGESLLLnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2672-2779 |
6.93e-19 |
|
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: 85.16 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2672 DPHFYSVSLIDGKLQAKFDAGDGEVTITS-DDTFNDGMLHGVSIIRNRRKLDMFVDDLPVGTERLSKGSKV--EISSLYL 2748
Cdd:pfam02210 17 GSDFLALELVNGRLVLRYDLGSGPESLLSsGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPPGESLLlnLNGPLYL 96
|
90 100 110
....*....|....*....|....*....|.
gi 919026507 2749 GGVPADLDIaSASATSQPLQGCIRDLVLNGK 2779
Cdd:pfam02210 97 GGLPPLLLL-PALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2670-2784 |
3.53e-18 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 83.14 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2670 QADPHFYSVSLIDGKLQAKFDAGDGEVTITSDDTFNDGMLHGVSIIRNRRKLDMFVDDLPVGTERLSKGSKVEIS---SL 2746
Cdd:pfam00054 16 QTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGESPLGATTDLDvdgPL 95
|
90 100 110
....*....|....*....|....*....|....*...
gi 919026507 2747 YLGGVPADLDIASASATSQPLQGCIRDLVLNGKlvQLD 2784
Cdd:pfam00054 96 YVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGK--PLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2260-2411 |
4.30e-18 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 83.16 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2260 TISFNFKTnnTEKDMLLFYVQGEEKPEFMAVEIVERKLRFVWNSGGGVAmanhslQIESEETSIqPDEKWYSVIARRTAN 2339
Cdd:smart00282 1 SISFSFRT--TSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPA------RLTSDPTPL-NDGQWHRVAVERNGR 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919026507 2340 VGTLAVqkikfagnDDPALASSSSSAQFTKLDLNDRakLYVAGAP-QGTVERDPALKGgmFVGCIADVTLDGR 2411
Cdd:smart00282 72 SVTLSV--------DGGNRVSGESPGGLTILNLDGP--LYLGGLPeDLKLPPLPVTPG--FRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2898-3027 |
2.15e-16 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 78.13 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2898 FRTYYPNGLLVYLSNEDQSEYVAIQMAGGTVMTSYADQKTGVpvnlTEGATVLVDDGKWHKIRLMKSANNIIFKVDEGPD 2977
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAA----VVRSGDKLNDGKWHSVELERNGRSGTLSVDGEAR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 2978 IVGRI----ANKIDVLAPMYVGGLPRGYNMRMGLV-PDSLKGCVRGFRLNSQKVD 3027
Cdd:pfam00054 77 PTGESplgaTTDLDVDGPLYVGGLPSLGVKKRRLAiSPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2255-2409 |
2.54e-16 |
|
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: 78.61 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2255 PSTTNTISFNFKTnnTEKDMLLFYVQGEEKPEFMAVEIVERKLRFVWNSGGGVAMANHSLQIEseetsiqpDEKWYSVIA 2334
Cdd:cd00110 18 PRTRLSISFSFRT--TSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLN--------DGQWHSVSV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 2335 RRTANVGTLAVqkikfagnDDPALASSSSSAQFTKLDLNDRakLYVAGAP-QGTVERDPALKGgmFVGCIADVTLD 2409
Cdd:cd00110 88 ERNGRSVTLSV--------DGERVVESGSPGGSALLNLDGP--LYLGGLPeDLKSPGLPVSPG--FVGCIRDLKVN 151
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1701-1941 |
2.07e-15 |
|
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: 78.99 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1701 VRGVNTSTMvviPWERFFAM----ENKTQVLRGKLDAIR------KVKVGDMEVI---VKELQANATKLYTQTSSMANDA 1767
Cdd:pfam06008 1 LLSLNSLTG---ALPAPYKInynlENLTKQLQEYLSPENahkiqiEILEKELSSLaqeTEELQKKATQTLAKAQQVNAES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1768 MGYSMVASNLSKTADGMEKEIREIITSARDLLDNLpdvHQLSGNvNLTSVMMKAQDIMKMIRERDFKPNIENADNELELA 1847
Cdd:pfam06008 78 ERTLGHAKELAEAIKNLIDNIKEINEKVATLGEND---FALPSS-DLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1848 KALKSSISDLQSKLTN-----VTDAAISIQELADRLNDLISLAEQSAKDSRAALELNQKNDElikklqNMTqALQTRALA 1922
Cdd:pfam06008 154 QDLLSRIQTWFQSPQEenkalANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQA------NLR-EFQRKKEE 226
|
250
....*....|....*....
gi 919026507 1923 VSSMLNMSSEMLKEANMTL 1941
Cdd:pfam06008 227 VSEQKNQLEETLKTARDSL 245
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2468-2595 |
4.02e-15 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 74.28 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2468 FRTFWEDALLFFSGNKANGEYIAVELVNGKVVFSVNFGGGnNISIESREKYNTNQWMTVKAETQGNAGQLEVttsEGREE 2547
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSG-AAVVRSGDKLNDGKWHSVELERNGRSGTLSV---DGEAR 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 919026507 2548 LKRAQATaSGEDSLDISNAsVYFGGIPSTSKFDSfPLSVRTPFLGCMK 2595
Cdd:pfam00054 77 PTGESPL-GATTDLDVDGP-LYVGGLPSLGVKKR-RLAISPSFDGCIR 121
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1075-1120 |
7.60e-15 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 70.80 E-value: 7.60e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1075 CDCDVTGSTSLQCGMTSGQCPCKPGVTGQKCDQCRPGYYGFSSNGC 1120
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1074-1119 |
2.55e-14 |
|
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: 69.31 E-value: 2.55e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1074 SCDCDVTGSTSLQCGMTSGQCPCKPGVTGQKCDQCRPGYYGFSSNG 1119
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1075-1123 |
2.80e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 69.30 E-value: 2.80e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 1075 CDCDVTGSTSLQCGMTSGQCPCKPGVTGQKCDQCRPGYYGFSSNGCTEC 1123
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2129-2252 |
5.30e-14 |
|
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: 71.36 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2129 ANDNATGALEkamnTVTSVDSIQEGLDNDLKpkldvvkvntKELQDLETMTGTMMEINNNLD----GIRDVNRSIHTTLG 2204
Cdd:pfam06009 1 SKELAREANE----TAKEVLEQLAPLSQNLE----------NTSEKLSGINRSLEETNELVNdankALDDAGRSVKKLEE 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919026507 2205 ALNRL-------------NMSLSQSLEELRESIQKAREQANNIKVSLAAGGSCHREYRTEE 2252
Cdd:pfam06009 67 LAPDLldklkplkqlevnSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPI 127
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1025-1073 |
1.52e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.99 E-value: 1.52e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 1025 ACNCHLKGSNDSQCDLVTGTCTCQPNVIGDKCDQCEINYYDLDS-GNGCQ 1073
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1026-1072 |
2.98e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 66.18 E-value: 2.98e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 919026507 1026 CNCHLKGSNDSQCDLVTGTCTCQPNVIGDKCDQCEINYYDlDSGNGC 1072
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1747-2234 |
3.79e-13 |
|
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: 75.83 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1747 KELQANATKLYTQTSsmandamgysmvasNLSKTADGMEKEIRE---IITSARDLLDNLPDVH-----QLSGNVN-LTSV 1817
Cdd:TIGR04523 214 KSLESQISELKKQNN--------------QLKDNIEKKQQEINEkttEISNTQTQLNQLKDEQnkikkQLSEKQKeLEQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1818 MMKAQDIMKMIRErdFKPNIENADNELE--LAKALKSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQSAKDSRAA 1895
Cdd:TIGR04523 280 NKKIKELEKQLNQ--LKSEISDLNNQKEqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1896 -----LELNQKNDElIKKLQNMTQALQTralavssmlnmSSEMLKeanmtlpnSSAEFLRDLLEQLKKDTENltiaaglL 1970
Cdd:TIGR04523 358 nsekqRELEEKQNE-IEKLKKENQSYKQ-----------EIKNLE--------SQINDLESKIQNQEKLNQQ-------K 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1971 RQNLPNLEPKVRQAEELAEKLRmqADNLDNMFQGARATSEDAVKaaqvyEGIVVAVDDALKEAQSAHDLASEAMNKTTta 2050
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLK--ETIIKNNSEIKDLTNQDSVK-----ELIIKNLDNTRESLETQLKVLSRSINKIK-- 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2051 dgSTLQEKAK--KSANTSLDFVNEANR-LVNSSKDLKDLLGSIDKDIDQANKRM----DEVDSAKERLTEGMDRLPAGIH 2123
Cdd:TIGR04523 482 --QNLEQKQKelKSKEKELKKLNEEKKeLEEKVKDLTKKISSLKEKIEKLESEKkekeSKISDLEDELNKDDFELKKENL 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2124 EKLIEANDNatgALEKAMNTVTSVDSIQEGLDNDLKPKLDVVKVNTKElqdLETMTGTMMEINNNLDGIRDVNRSIHTTL 2203
Cdd:TIGR04523 560 EKEIDEKNK---EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---IEEKEKKISSLEKELEKAKKENEKLSSII 633
|
490 500 510
....*....|....*....|....*....|.
gi 919026507 2204 GALNRLNMSLSQSLEELRESIQKAREQANNI 2234
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1026-1072 |
8.44e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.07 E-value: 8.44e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 1026 CNCHLKGSNDSQCDLVTGTCTCQPNVIGDKCDQCEINYYDL--DSGNGC 1072
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1170-1218 |
3.69e-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: 63.14 E-value: 3.69e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 1170 CNCNMTGSLDTQCDTVDGQCECRPEYDGMKCDMCRFGHFGFPNCRPCHC 1218
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1170-1211 |
2.33e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.83 E-value: 2.33e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 919026507 1170 CNCNMTGSLDTQCDTVDGQCECRPEYDGMKCDMCRFGHFGFP 1211
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
978-1023 |
3.31e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.31e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 978 CSCNLTGSVSNLCDQVSGQCPCKNGVGGQYCGSCLPDHWEYSEEGC 1023
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1779-2236 |
4.72e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1779 KTADGMEKEIREIITSARDLLDnlpDVHQLSGNVNLTSVMMKAQDIMKMIRERDFKPNIENADNELELAKALKSSISDLQ 1858
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEK---RLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1859 SKLTnvtdAAIS-----IQELADRLNDLIS-----------LAEQSAKD--SRAALELNQKNDELiKKLQNMTQALQTRA 1920
Cdd:PRK03918 408 SKIT----ARIGelkkeIKELKKAIEELKKakgkcpvcgreLTEEHRKEllEEYTAELKRIEKEL-KEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1921 LAVSSMLNMSSEMLKEANMtlpnssAEFLRDLLEQLKKdtenltiaagllrQNLPNLEPKVRQAEELAEKLrmqadnldN 2000
Cdd:PRK03918 483 RELEKVLKKESELIKLKEL------AEQLKELEEKLKK-------------YNLEELEKKAEEYEKLKEKL--------I 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2001 MFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSA----HDLASEAMNKTTTADGSTLQEKAKksantsldFVNEANRL 2076
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEELEERLKELEP--------FYNEYLEL 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2077 VNSSKDLKDLLGSIDK---DIDQANKRMDEVDSAKERLTEGMDRLP--------AGIHEKLIEANDNATGALEKAMNTVT 2145
Cdd:PRK03918 608 KDAEKELEREEKELKKleeELDKAFEELAETEKRLEELRKELEELEkkyseeeyEELREEYLELSRELAGLRAELEELEK 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2146 SVDSIQEGLDnDLKPKLDVVKVNTKELQDLETMTGTMMEINNNldgIRDVNRSIhtTLGALNRLNMSLSQSLEELRE--- 2222
Cdd:PRK03918 688 RREEIKKTLE-KLKEELEEREKAKKELEKLEKALERVEELREK---VKKYKALL--KERALSKVGEIASEIFEELTEgky 761
|
490
....*....|....
gi 919026507 2223 SIQKAREQANNIKV 2236
Cdd:PRK03918 762 SGVRVKAEENKVKL 775
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2265-2411 |
6.30e-11 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 62.44 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2265 FKTnnTEKDMLLFYVqGEEKPEFMAVEIVERKLRFVWNSGGGVAmanhslQIESEETSIQpDEKWYSVIARRTANVGTLA 2344
Cdd:pfam02210 1 FRT--RQPNGLLLYA-GGGGSDFLALELVNGRLVLRYDLGSGPE------SLLSSGKNLN-DGQWHSVRVERNGNTLTLS 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 2345 VqkikfagnDDPALASSSSSAQFTKLDLNDRakLYVAGAPQGTVERDPALKGGmFVGCIADVTLDGR 2411
Cdd:pfam02210 71 V--------DGQTVVSSLPPGESLLLNLNGP--LYLGGLPPLLLLPALPVRAG-FVGCIRDVRVNGE 126
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1634-1672 |
1.20e-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: 1.20e-10
10 20 30
....*....|....*....|....*....|....*....
gi 919026507 1634 PCDCSEDGSLDNLCDRESGQCICHPGVLGRACDQCQPRY 1672
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1170-1213 |
1.79e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 1.79e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1170 CNCNMTGSLDTQCDTVDGQCECRPEYDGMKCDMCRFGHFG--FPNC 1213
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1525-1574 |
3.63e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.63e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 919026507 1525 PCECHGHSDM---CNKETGVCLnCAHNTAGDHCNTCAEGYYGNATSGREdaCQ 1574
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1635-1672 |
6.46e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 6.46e-10
10 20 30
....*....|....*....|....*....|....*...
gi 919026507 1635 CDCSEDGSLDNLCDRESGQCICHPGVLGRACDQCQPRY 1672
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
977-1024 |
6.99e-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: 6.99e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 977 RCSCNLTGSVSNLCDQVSGQCPCKNGVGGQYCGSCLPDHWEYSE--EGCK 1024
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
931-968 |
8.67e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 8.67e-10
10 20 30
....*....|....*....|....*....|....*...
gi 919026507 931 CDCNQYGSTGTSCDQRSGQCSCRPYYEGRACDSCVAGY 968
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
931-980 |
8.97e-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: 56.59 E-value: 8.97e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 931 CDCNQYGSTGTSCDQRSGQCSCRPYYEGRACDSCVAGYGNiIAGCPRCSC 980
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG-LPSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1863-2198 |
1.18e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.38 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1863 NVTDAAISIQELADRLNDLIS-LAEQSAKDSRAALELNQKNDELiKKLQNMTQALQTRALAVSSMLNMSSEMLKEANmtl 1941
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREeLEQAREELEQLEEELEQARSEL-EQLEEELEELNEQLQAAQAELAQAQEELESLQ--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1942 pnSSAEFLRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAEKLRMQADNLDNMFQGARATSEdAVKAAQVYEG 2021
Cdd:COG4372 108 --EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ-ALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2022 IVVAVDDALKEAQSAHDLAsEAMNKTTTADGSTLQEKAKKSANTSLDFVNEANRLVNSSKDLKDLLGSIDKDIDQANKRM 2101
Cdd:COG4372 185 LDELLKEANRNAEKEEELA-EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2102 DEVDSAKERLTEGMDRLPAGIHEKLIEANDnatGALEKAMNTVTSVDSIQEGLDNDLKPKLDVVKVNTKELQDLETMTGT 2181
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAAL---ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330 340
....*....|....*....|
gi 919026507 2182 ---MMEINNNLDGIRDVNRS 2198
Cdd:COG4372 341 dllQLLLVGLLDNDVLELLS 360
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1216-1271 |
1.22e-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: 56.21 E-value: 1.22e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 1216 CHCNENGTVMSDCNakghcqcQEDGQCPCRGNVEGLKCKHCKEGSFSLQSNNPEGC 1271
Cdd:pfam00053 1 CDCNPHGSLSDTCD-------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1526-1578 |
1.30e-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: 55.82 E-value: 1.30e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 1526 CECHGH---SDMCNKETGVCLnCAHNTAGDHCNTCAEGYYGNATsgredaCQPCGC 1578
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS------DPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1635-1672 |
2.06e-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: 55.44 E-value: 2.06e-09
10 20 30
....*....|....*....|....*....|....*...
gi 919026507 1635 CDCSEDGSLDNLCDRESGQCICHPGVLGRACDQCQPRY 1672
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
978-1026 |
2.39e-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: 2.39e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 978 CSCNLTGSVSNLCDQVSGQCPCKNGVGGQYCGSCLPDHWEYSEEGCKAC 1026
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
931-975 |
5.56e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.24 E-value: 5.56e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 931 CDCNQYGSTGTSCDQRSGQCSCRPYYEGRACDSCVAGY-GNIIAGC 975
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYyGDGPPGC 46
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1837-2082 |
5.95e-09 |
|
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: 59.73 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1837 IENADNELElakALKSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQSAKDSRAALElnqkndELIKKLQNMTQAL 1916
Cdd:pfam06008 42 IEILEKELS---SLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIK------EINEKVATLGEND 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1917 QtrALAVSSMlnmsSEMLKEANMTLPNSSAeflRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAEKLRMQAD 1996
Cdd:pfam06008 113 F--ALPSSDL----SRMLAEAQRMLGEIRS---RDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1997 NLDNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSAHDLASEAMNKTTtadgstlqekakKSANTSLDFVNEANRL 2076
Cdd:pfam06008 184 EYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLE------------ETLKTARDSLDAANLL 251
|
....*.
gi 919026507 2077 VNSSKD 2082
Cdd:pfam06008 252 LQEIDD 257
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
457-504 |
6.26e-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: 54.28 E-value: 6.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 919026507 457 PCPCSRAGSRNvDTC---QGDCICKPNVVGENCDQCKPGFFNmEASNPAGC 504
Cdd:cd00055 1 PCDCNGHGSLS-GQCdpgTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1835-2073 |
6.26e-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: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1835 PNIENADNELelaKALKSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQSAKDSRAAL-ELNQKNDELIKKLQNMT 1913
Cdd:COG3883 16 PQIQAKQKEL---SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1914 QALQtRALAVSSMLNM--SSEMLKEA--NMTLPNSSAEFLRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAE 1989
Cdd:COG3883 93 RALY-RSGGSVSYLDVllGSESFSDFldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1990 KLRMQADNLDNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSAHDLASEAMNKTTTADGSTLQEKAKKSANTSLDF 2069
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
....
gi 919026507 2070 VNEA 2073
Cdd:COG3883 252 AGAA 255
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2265-2411 |
6.65e-09 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 56.56 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2265 FKTNNTEKdmLLFYVQGEEKPEFMAVEIVERKLRFVWNSGGGVAMANHSLQIEseetsiqpDEKWYSVIARRTANVGTLA 2344
Cdd:pfam00054 1 FRTTEPSG--LLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLN--------DGKWHSVELERNGRSGTLS 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 2345 VqkikfAGNDDPALASSSSSAQftklDLNDRAKLYVAGAPQGTVERDPALKGGMFVGCIADVTLDGR 2411
Cdd:pfam00054 71 V-----DGEARPTGESPLGATT----DLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGK 128
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1838-2124 |
7.28e-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: 62.00 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1838 ENADNELELAKALKSSISDLQSKLTNVTDAA-ISIQELADRLNDL-ISLAEQSAKDSRAALELNQKNDELIKKLQNMtQA 1915
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLeAEVEQLEERIAQLsKELTELEAEIEELEERLEEAEEELAEAEAEI-EE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1916 LQTRALAVSSMLNMSSEMLKEANMTLPNSSAEF--LRDLLEQLKKDTENLTIAAGLLRQ-------NLPNLEPKVRQAEE 1986
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAanLRERLESLERRIAATERRLEDLEEqieelseDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1987 LAEKLRMQADNLDNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSAHDLASEAMNK------TTTADGSTLQEKAK 2060
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQlelrleGLEVRIDNLQERLS 946
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919026507 2061 KSANTSLDFV-NEANRLVNSSKDLKDLLGSIDKDID--------------QANKRMDEVDSAKERLTEGMDRLPAGIHE 2124
Cdd:TIGR02168 947 EEYSLTLEEAeALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
458-504 |
9.49e-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: 53.51 E-value: 9.49e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 458 CPCSRAGSRNvDTC---QGDCICKPNVVGENCDQCKPGFFNMEASNPAGC 504
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. |
768-815 |
1.86e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.86e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 919026507 768 CNCNNHA---DTCEASSGLCtSCRDNTVGPHCENCEFGYYGNATrGTPNDC 815
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
458-504 |
3.00e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.00e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 458 CPCSRAGSRNvDTC---QGDCICKPNVVGENCDQCKPGFFNmeaSNPAGC 504
Cdd:smart00180 1 CDCDPGGSAS-GTCdpdTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1689-2240 |
3.09e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 60.07 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1689 DLMVAVDEMEVMVRGVNTSTMVVipweRFFAMENKTQVLrgkLDAIRKVKVGDMEVIVKELQANATKLYTQTSSMANDAM 1768
Cdd:TIGR01612 700 DLKSKIDKEYDKIQNMETATVEL----HLSNIENKKNEL---LDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKIN 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1769 GYSMVASNLSKtadgMEKEIREIITSARDL--LDNLPDvHQLSGNVN-----LTSVMMKAQDIMKMIRERDFKP------ 1835
Cdd:TIGR01612 773 DYAKEKDELNK----YKSKISEIKNHYNDQinIDNIKD-EDAKQNYDkskeyIKTISIKEDEIFKIINEMKFMKddflnk 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1836 -----NIENadNELELAKALKSSISDLQSKLTN-VTDAAISIQElaDRLND---LISLAEQSAKDSRAALELNQKNDELI 1906
Cdd:TIGR01612 848 vdkfiNFEN--NCKEKIDSEHEQFAELTNKIKAeISDDKLNDYE--KKFNDsksLINEINKSIEEEYQNINTLKKVDEYI 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1907 KKLQNMTQALQ---TRALAVSSMLNMSSEMLKEANMTLPNSSAEF---LRDLLEQLKKDTENLTIAA-----GLLRQNLP 1975
Cdd:TIGR01612 924 KICENTKESIEkfhNKQNILKEILNKNIDTIKESNLIEKSYKDKFdntLIDKINELDKAFKDASLNDyeaknNELIKYFN 1003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1976 NLEPKVRQAEElaEKLRMQADNLDNMFQGARATSEDAVKAAQ-----VYEGIVVAVDDALKE-AQSAHDLASEAMNK--T 2047
Cdd:TIGR01612 1004 DLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPnieiaIHTSIYNIIDEIEKEiGKNIELLNKEILEEaeI 1081
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2048 TTADGSTLQEKAKKSaNTSlDFVNEAN-RLVNSSKDLKDLLGSIDKDIDQANKRMDEVDSAKERLtegMDRLPAGIH--E 2124
Cdd:TIGR01612 1082 NITNFNEIKEKLKHY-NFD-DFGKEENiKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENY---IDEIKAQINdlE 1156
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2125 KLIE---ANDNATGALEKAMNTVTSVDSiqegldndlkpkldvvKVNTKElqdletmtgtmmEINNNLDGIRDVNRSiHT 2201
Cdd:TIGR01612 1157 DVADkaiSNDDPEEIEKKIENIVTKIDK----------------KKNIYD------------EIKKLLNEIAEIEKD-KT 1207
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 919026507 2202 TLGALNRLNMSLSQSLEEL-RESIQKAREQANNIKVSLAA 2240
Cdd:TIGR01612 1208 SLEEVKGINLSYGKNLGKLfLEKIDEEKKKSEHMIKAMEA 1247
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
768-816 |
5.40e-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: 51.59 E-value: 5.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 768 CNCNNHAD---TCEASSGLCTsCRDNTVGPHCENCEFGYYGNATRgtPNDCR 816
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1215-1272 |
6.01e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 6.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 919026507 1215 PCHCNENGTVMSDCNakghcqcQEDGQCPCRGNVEGLKCKHCKEGSFSLQSnNPEGCT 1272
Cdd:cd00055 1 PCDCNGHGSLSGQCD-------PGTGQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1848-2126 |
7.93e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.84 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1848 KALKSSISDLQSKLTNVTDAaisIQELADRLNDLISLAEqSAKDSRAAL------------ELNQKNDELIKKLQNMTQ- 1914
Cdd:COG1340 4 DELSSSLEELEEKIEELREE---IEELKEKRDELNEELK-ELAEKRDELnaqvkelreeaqELREKRDELNEKVKELKEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1915 --ALQTRALAVSSMLNMSSEMLKEANmtLPNSSAEFLRDLLEQL--KKDTENLTiaagllrqnlPNLEPK-VRQAEELAE 1989
Cdd:COG1340 80 rdELNEKLNELREELDELRKELAELN--KAGGSIDKLRKEIERLewRQQTEVLS----------PEEEKElVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1990 KL--RMQADNLDNMFQGARATSEDAVKAAqvyEGIVVAVDDALKEAQSAHDLASEAMNKtttADgsTLQEKAKKSANTSL 2067
Cdd:COG1340 148 ELekAKKALEKNEKLKELRAELKELRKEA---EEIHKKIKELAEEAQELHEEMIELYKE---AD--ELRKEADELHKEIV 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 2068 DFVNEANRL----VNSSKDLKDLLGSIDKDIDQAN--KRMDEVDSAKERLTEGMDRLPAGihEKL 2126
Cdd:COG1340 220 EAQEKADELheeiIELQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKKG--EKL 282
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1526-1568 |
1.09e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.09e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1526 CECHG---HSDMCNKETGVCLnCAHNTAGDHCNTCAEGYYGNATSG 1568
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1819-2251 |
4.33e-07 |
|
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: 56.21 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1819 MKAQDIMKMIRErDFKPNIENADNELELAKALKSSISDLQSKLTNVTDAAISIQELADRL-NDLISLAEQSAKdsraaLE 1897
Cdd:TIGR00606 185 IKALETLRQVRQ-TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYeNELDPLKNRLKE-----IE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1898 LNQKNdelIKKLQNMTQALQTRALavsSMLNMSSEmLKEANMTLPNSSAEFLRDLLE--------------QLKKDTENL 1963
Cdd:TIGR00606 259 HNLSK---IMKLDNEIKALKSRKK---QMEKDNSE-LELKMEKVFQGTDEQLNDLYHnhqrtvrekerelvDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1964 TIAAGLLRQNLPNLEPKVRQAEELAEKLRMQADNLDNMFQGARATSE------DAVKAAQVYEGIVVAVDDALKEAQSAH 2037
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgferGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2038 DLASEAMNKTTTADGSTLQEKAKKSA------NTSLDFVNEANRLVNSSKDLKDLLGSIDK--DIDQA-NKRMDEVDSAK 2108
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGlgrtieLKKEILEKKQEELKFVIKELQQLEGSSDRilELDQElRKAERELSKAE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2109 ER-LTE--------------GMDRLPAGIHEKLIEANDNATGALEKAMNTVTSVDSIQEGLDNDLKPKLDVVKV-----N 2168
Cdd:TIGR00606 492 KNsLTEtlkkevkslqnekaDLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpN 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2169 TKELQDleTMTGTMMEINNNLDGIRDVNRSIHTTLGALNRLNMSLSQ-----------------------SLEELRESIQ 2225
Cdd:TIGR00606 572 KKQLED--WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESkeeqlssyedklfdvcgsqdeesDLERLKEEIE 649
|
490 500
....*....|....*....|....*.
gi 919026507 2226 KAREQanniKVSLAAGGSCHREYRTE 2251
Cdd:TIGR00606 650 KSSKQ----RAMLAGATAVYSQFITQ 671
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
404-460 |
5.98e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 5.98e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 919026507 404 CQCSQLGS-TGTCVQdnsrrgeglMPGDCICRVGFGGRNCDRCASGYKNFPSCIPCPC 460
Cdd:pfam00053 1 CDCNPHGSlSDTCDP---------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1850-2230 |
5.99e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1850 LKSSISDLQSKLT-----------NVTDAAISIQELADRLNDLISLAEQSAKDSRAaleLNQKNDELIKKLQNMTQALQT 1918
Cdd:PRK02224 256 LEAEIEDLRETIAeterereelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEA---VEARREELEDRDEELRDRLEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1919 RALAVSSMlnmssemlkeanmtlpNSSAEFLRDLLEQLKKDTENLTIAAGllrqnlpNLEPKVRQAEELAEKLRMQADNL 1998
Cdd:PRK02224 333 CRVAAQAH----------------NEEAESLREDADDLEERAEELREEAA-------ELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1999 DNMFQGARATSEDAvkaaqvyegivvavDDALKEAQSAHDLASEAMN------KTTTADGSTLQEKakksantsldfVNE 2072
Cdd:PRK02224 390 EEEIEELRERFGDA--------------PVDLGNAEDFLEELREERDelrereAELEATLRTARER-----------VEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2073 ANRLVNSSK------DLKD--LLGSIDKDIDQANKRMDEVDSAKERLTEGMDRLPAGihEKLIEANDNATGALEKAMNTV 2144
Cdd:PRK02224 445 AEALLEAGKcpecgqPVEGspHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA--EDLVEAEDRIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2145 TSVDSIQEGLDNDlKPKLDVVKVNTKELQD-----LETMTGTMMEINNNLDGIRDVNR---SIHTTLGALNRLNMSLSQs 2216
Cdd:PRK02224 523 ELIAERRETIEEK-RERAEELRERAAELEAeaeekREAAAEAEEEAEEAREEVAELNSklaELKERIESLERIRTLLAA- 600
|
410
....*....|....
gi 919026507 2217 LEELRESIQKAREQ 2230
Cdd:PRK02224 601 IADAEDEIERLREK 614
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1122-1168 |
6.38e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 6.38e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 919026507 1122 ECPVCPVAGQVCDAVTGECVCPTNTEGDRCERCVPDTWGHD-QLLGCK 1168
Cdd:cd00055 3 DCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
878-921 |
1.00e-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: 47.73 E-value: 1.00e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 919026507 878 PCACSGNINPNavGNCDRTTGQCLkCLFNTEGWNCAQCKPDYYG 921
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1720-2227 |
1.01e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.83 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1720 MENKTQVLRGKLDAIRKVkvgdMEVIvkELQANATKLYTQTSSMANDAMGYSMVASNLSKTADGMEKE---IREIITSAR 1796
Cdd:pfam10174 146 IETQKQTLGARDESIKKL----LEML--QSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKEnihLREELHRRN 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1797 DLLDNLPDVHQLSgnvnlTSVMMKAQDIMKMIRE-RDFKPNIE----NA-----DNELEL---------AKALKSSISDL 1857
Cdd:pfam10174 220 QLQPDPAKTKALQ-----TVIEMKDTKISSLERNiRDLEDEVQmlktNGllhteDREEEIkqmevykshSKFMKNKIDQL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1858 QSKLTNVTDAAISIQELADRLNDLISLAEQ---------SAKDSRAA----------LELNQKNDELIKK---LQNMTQA 1915
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNSDCKQhievlkeslTAKEQRAAilqtevdalrLRLEEKESFLNKKtkqLQDLTEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1916 LQTRALAVSSMLNMS-----------------SEMLKEANMTLPNssaefLRDLLEQLKKDTENLTIAagllrqnLPNLE 1978
Cdd:pfam10174 375 KSTLAGEIRDLKDMLdvkerkinvlqkkienlQEQLRDKDKQLAG-----LKERVKSLQTDSSNTDTA-------LTTLE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1979 PKVRQAEELAEKLRMQADNLDNMFqgaRATSEDAVKAAQVYEGIVVAVDDALKEAQSAhdlASEAMNKTTTADGSTLQek 2058
Cdd:pfam10174 443 EALSEKERIIERLKEQREREDRER---LEELESLKKENKDLKEKVSALQPELTEKESS---LIDLKEHASSLASSGLK-- 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2059 aKKSANTSLDF-----VNEANRLVNSSK-------------DLKDLLGSIDKDI----DQANKRMDEVDSA----KERLT 2112
Cdd:pfam10174 515 -KDSKLKSLEIaveqkKEECSKLENQLKkahnaeeavrtnpEINDRIRLLEQEVarykEESGKAQAEVERLlgilREVEN 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2113 EGMDRlpagihEKLIEA----------NDNATGALEKAMNTVTSVDSIQEgLDNDLKPKlDVVKVNTKELQdLETMTGTM 2182
Cdd:pfam10174 594 EKNDK------DKKIAElesltlrqmkEQNKKVANIKHGQQEMKKKGAQL-LEEARRRE-DNLADNSQQLQ-LEELMGAL 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 919026507 2183 MEINNNLDGIR----DVNRSIHTTLGALNRLNMSLSQSLEELRESIQKA 2227
Cdd:pfam10174 665 EKTRQELDATKarlsSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEA 713
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1216-1271 |
1.38e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.38e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 1216 CHCNENGTVMSDCNakghcqcQEDGQCPCRGNVEGLKCKHCKEGSFslqSNNPEGC 1271
Cdd:smart00180 1 CDCDPGGSASGTCD-------PDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1714-2122 |
1.65e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1714 WERFFAMENKTQVLRGKLDAIRKvKVGDMEVIVKELQANATKLYTQTSSMANDAMGYSMVASNLSKTADGMEKEIREIIT 1793
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRK-ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1794 SARDLLDNL----PDVHQLSGN-VNLTSVMMKAQDIMKMIRERdfkpnIENADNELelaKALKSSISDLQSKLTNVTDAA 1868
Cdd:TIGR02168 762 EIEELEERLeeaeEELAEAEAEiEELEAQIEQLKEELKALREA-----LDELRAEL---TLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1869 ISIQELADRLNDLISLAEQSAKDSRAALE-----LNQKNDELIKKLQNMTQALQTRALAVSSMLNMSSEmlkeanmtlpn 1943
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEeleelIEELESELEALLNERASLEEALALLRSELEELSEE----------- 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1944 ssaefLRDLLEQLKKdtenltiaaglLRQNLPNLEPKVRQAEELAEKLRMQADNLDNMFqgaratSEDAVKAAQVYEGIV 2023
Cdd:TIGR02168 903 -----LRELESKRSE-----------LRRELEELREKLAQLELRLEGLEVRIDNLQERL------SEEYSLTLEEAEALE 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2024 VAVDDALKEAQSAHDLASEAMNKTTTADGSTLQEkaKKSANTSLDFVNEANRLVNSSKdlKDLLGSIDK-D--------- 2093
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKELGPVNLAAIEE--YEELKERYDFLTAQKEDLTEAK--ETLEEAIEEiDrearerfkd 1036
|
410 420 430
....*....|....*....|....*....|....*..
gi 919026507 2094 -IDQANKRMDEV-------DSAKERLTEGMDRLPAGI 2122
Cdd:TIGR02168 1037 tFDQVNENFQRVfpklfggGEAELRLTDPEDLLEAGI 1073
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1745-2240 |
2.00e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1745 IVKELQANATKLytqtSSMANDAMGYSMVASNLSKTADGME----------KEIREIITSARDLLDNL-PDVHQLSGNVN 1813
Cdd:PRK01156 174 VIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEkshsitlkeiERLSIEYNNAMDDYNNLkSALNELSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1814 ----LTSVMMKAQDIMKMIRERDFK-PNIENADNELELAKA------------LKSSISDLQSKLTNVTDAAISIQELAD 1876
Cdd:PRK01156 250 mknrYESEIKTAESDLSMELEKNNYyKELEERHMKIINDPVyknrnyindyfkYKNDIENKKQILSNIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1877 RLNDLISLAEQSAKDSRAALELNQKNDEL----------IKKLQNMTQALQTRALAVSSMLNMSSEMLK--EANMTLPNS 1944
Cdd:PRK01156 330 KLSVLQKDYNDYIKKKSRYDDLNNQILELegyemdynsyLKSIESLKKKIEEYSKNIERMSAFISEILKiqEIDPDAIKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1945 SAEFLRDLLEQLKKDTENLTIAAGLLRQNLPNLEpkvRQAEELAEKLRMQADNLDNMFQGARATSED-AVKAAQVYEGI- 2022
Cdd:PRK01156 410 ELNEINVKLQDISSKVSSLNQRIRALRENLDELS---RNMEMLNGQSVCPVCGTTLGEEKSNHIINHyNEKKSRLEEKIr 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2023 -----VVAVDDALKEAQSAHD-LASEAMNKTTTADG--STLQ---EKAKKSANTSLDFVNEANRLVN--SSKDLKDL--- 2086
Cdd:PRK01156 487 eieieVKDIDEKIVDLKKRKEyLESEEINKSINEYNkiESARadlEDIKIKINELKDKHDKYEEIKNryKSLKLEDLdsk 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2087 -------LGSIDK-DIDQANKRMDEVDSAKERLTEGMDRLPAGI------HEKLIEANDNATGALEKAMNTVTS----VD 2148
Cdd:PRK01156 567 rtswlnaLAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFpddksyIDKSIREIENEANNLNNKYNEIQEnkilIE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2149 SIQEGLDNdlkPKLDVVKVNTKElQDLETMTGTMMEINNNLDGIRDVNRSIHTTLGALNRLNMSLSQSLEELRESIQKAR 2228
Cdd:PRK01156 647 KLRGKIDN---YKKQIAEIDSII-PDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN 722
|
570
....*....|..
gi 919026507 2229 EQANNIKVSLAA 2240
Cdd:PRK01156 723 ETLESMKKIKKA 734
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1778-2039 |
3.09e-06 |
|
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: 51.15 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1778 SKTADGMEKEIREIITSARDLLDNLpdvhqlsgnvnltsvmmKAQDImkmiRERDFKPNIENADNELelaKALKSSISDL 1857
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKI-----------------DASKQ----RAAAYQKALDDAPAEL---RELRQELAAL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1858 QSKLTNVT---DAAISIQELADRLNDlislaeQSAKDSRAALELNQKNDELIK------KLQNMTQALQTRALAVSSMLN 1928
Cdd:pfam12795 64 QAKAEAAPkeiLASLSLEELEQRLLQ------TSAQLQELQNQLAQLNSQLIElqtrpeRAQQQLSEARQRLQQIRNRLN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1929 ---MSSEMLKEANMTLPNSSAEFLRDLLEQLKKDTENLTIaagllRQNLPNLepkvrQAEELAEK---LRMQADNLDNMF 2002
Cdd:pfam12795 138 gpaPPGEPLSEAQRWALQAELAALKAQIDMLEQELLSNNN-----RQDLLKA-----RRDLLTLRiqrLEQQLQALQELL 207
|
250 260 270
....*....|....*....|....*....|....*...
gi 919026507 2003 QGAR-ATSEDAVKAAqvyegivvavDDALKEAQSAHDL 2039
Cdd:pfam12795 208 NEKRlQEAEQAVAQT----------EQLAEEAAGDHPL 235
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1799-1963 |
3.12e-06 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 50.87 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1799 LDNLPDvhQLSGNVNLTSVMMkaQDIMKMIRErdfkPNIENADNELELAKALKSSISDLQSKLTNVTDAAISIQELADRL 1878
Cdd:cd21116 57 LLSLPN--DIIGYNNTFQSYY--PDLIELADN----LIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1879 ND----LISLAEQSAKDSRAALELNQKNDELIKKLQNMTQALQTRALAVSSMLNMSSEMLKEANMTLPNSSAEFLRDLLE 1954
Cdd:cd21116 129 DDdsrnLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDLEDAESSIDAAFLQADLK 208
|
....*....
gi 919026507 1955 QLKKDTENL 1963
Cdd:cd21116 209 AAKADWNQL 217
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
403-454 |
3.28e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 3.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 919026507 403 PCQCSQLGS-TGTCVQDNsrrgeglmpGDCICRVGFGGRNCDRCASGYKNFPS 454
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGT---------GQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
768-815 |
4.44e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 4.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 919026507 768 CNCN---NHADTCEASSGLCTsCRDNTVGPHCENCEFGYYGNatrgTPNDC 815
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD----GPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1122-1167 |
5.91e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 5.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 919026507 1122 ECPVCPVAGQVCDAVTGECVCPTNTEGDRCERCVPDTWGhDQLLGC 1167
Cdd:smart00180 2 DCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1122-1160 |
9.15e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.04 E-value: 9.15e-06
10 20 30
....*....|....*....|....*....|....*....
gi 919026507 1122 ECPVCPVAGQVCDAVTGECVCPTNTEGDRCERCVPDTWG 1160
Cdd:pfam00053 2 DCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
879-928 |
1.27e-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: 44.65 E-value: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 879 CACSGNINPNavGNCDRTTGQCLkCLFNTEGWNCAQCKPDYYG--MVYGKGC 928
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGlpSDPPQGC 49
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1730-2017 |
1.67e-05 |
|
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: 48.84 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1730 KLDAIRKVKVGDmevivkELQANATKLYTQTSSMANDAMGYSMVASNLSKTADGMEKEIREIitsaRDLLDNLpdvhqls 1809
Cdd:pfam12795 1 KLDELEKAKLDE------AAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELREL----RQELAAL------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1810 gnvnltsvmmkAQDIMKMIRERDFKPNIEnadnELE--LAKALkSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQ 1887
Cdd:pfam12795 64 -----------QAKAEAAPKEILASLSLE----ELEqrLLQTS-AQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1888 SAKDSRAALELNQKNDELIkklqnmTQALQTRALAVSSMLNMSSEMLKEANMTLPNssaefLRDLLeQLKKDTENLTIAA 1967
Cdd:pfam12795 128 RLQQIRNRLNGPAPPGEPL------SEAQRWALQAELAALKAQIDMLEQELLSNNN-----RQDLL-KARRDLLTLRIQR 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 919026507 1968 glLRQNLPNLEpkvrqaEELAEKLRMQADnldnmfQGARATSEDAVKAAQ 2017
Cdd:pfam12795 196 --LEQQLQALQ------ELLNEKRLQEAE------QAVAQTEQLAEEAAG 231
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
404-455 |
1.88e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 404 CQCSQLGS-TGTCVQDNsrrgeglmpGDCICRVGFGGRNCDRCASGY--KNFPSC 455
Cdd:smart00180 1 CDCDPGGSaSGTCDPDT---------GQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1871-2111 |
1.88e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1871 IQELADRLNDlislAEQSAKDSRAALELNQKNDELIKKLQNM------TQALQTRALAVSSMLnmssEMLKEANMTLpns 1944
Cdd:COG4913 619 LAELEEELAE----AEERLEALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAEL----ERLDASSDDL--- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1945 saEFLRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAEKLRMQADNLDNMFQGARATSEDAVKAA----QVYE 2020
Cdd:COG4913 688 --AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgdAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2021 GIVVAVDDALKEAQSAHDLASEAMNK-----------------TTTADGSTLQEKAKKSANTSL-DFVNEANRLVNSSK- 2081
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERamrafnrewpaetadldADLESLPEYLALLDRLEEDGLpEYEERFKELLNENSi 845
|
250 260 270
....*....|....*....|....*....|.
gi 919026507 2082 -DLKDLLGSIDKDIDQANKRMDEVDSAKERL 2111
Cdd:COG4913 846 eFVADLLSKLRRAIREIKERIDPLNDSLKRI 876
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1741-2237 |
1.94e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.99 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1741 DMEVIVKELQANATKlytqTSSMANDAMGYSMVASNLSKTadgMEKEIREIITSARDLLDNLPDvHQLSGNVNL-----T 1815
Cdd:PTZ00440 1295 DSEKILKEILNSTKK----AEEFSNDAKKELEKTDNLIKQ---VEAKIEQAKEHKNKIYGSLED-KQIDDEIKKieqikE 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1816 SVMMKAQDIMKMIRerDFKPNIENADNELELAKALKSSISDLQSKltNVTDAAISIQELADRLNDLISLAEQSAKD-SRA 1894
Cdd:PTZ00440 1367 EISNKRKEINKYLS--NIKSNKEKCDLHVRNASRGKDKIDFLNKH--EAIEPSNSKEVNIIKITDNINKCKQYSNEaMET 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1895 ALELNQKNDELIKKLQNMTQALQTralavSSMLNM---SSEMLKEAN-----MTLPNS--------SAEFLRDLLEQ--L 1956
Cdd:PTZ00440 1443 ENKADENNDSIIKYEKEITNILNN-----SSILGKktkLEKKKKEATnimddINGEHSiiktkltkSSEKLNQLNEQpnI 1517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1957 KKDTENL-----TIAAGLLRQNLPNLEpkvrqaEELAEKLRMqADNLDNMFQGARATSEDAVKAAQVyegivvavdDALK 2031
Cdd:PTZ00440 1518 KREGDVLnndksTIAYETIQYNLGRVK------HNLLNILNI-KDEIETILNKAQDLMRDISKISKI---------VENK 1581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2032 EAQSAHDLASEAMN--KTTTADGSTLQEKAKKsANTSLDFVNEANRLVNSSKDLKDLlGSIDKDIDQANKRMDEVDSAKE 2109
Cdd:PTZ00440 1582 NLENLNDKEADYVKylDNILKEKQLMEAEYKK-LNEIYSDVDNIEKELKKHKKNYEI-GLLEKVIEINKNIKLYMDSTKE 1659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2110 RLTEGMD---RLPAGIHEKLIEANDNATGALEKaMNTV-----TSVDSIQEGLDNDLKPKLDVVKVNT--KELQDLE-TM 2178
Cdd:PTZ00440 1660 SLNSLVNnfsSLFNNFYLNKYNINENLEKYKKK-LNEIynefmESYNIIQEKMKEVSNDDVDYNEAKTlrEEAQKEEvNL 1738
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919026507 2179 TGTMMEINNNLDGIRDV--NRSIHTTLGALNRLNMSLSQSLEELRESIQKAREQANNIKVS 2237
Cdd:PTZ00440 1739 NNKEEEAKKYLNDIKKQesFRFILYMKEKLDELSKMCKQQYNIVDEGYNYIKKKIEYIKTL 1799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1919-2239 |
2.00e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1919 RALAVSSMLNMSSEMLKeanmtlpnssaefLRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAEKLRMQADNL 1998
Cdd:TIGR02168 665 SAKTNSSILERRREIEE-------------LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1999 DNMFQGARATSEdavKAAQVYEGIVVAVDDALKEAQSAHDLASEAMnktttadgSTLQEKAKKSAntsldfvnEANRLVN 2078
Cdd:TIGR02168 732 RKDLARLEAEVE---QLEERIAQLSKELTELEAEIEELEERLEEAE--------EELAEAEAEIE--------ELEAQIE 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2079 sskDLKDLLGSIDKDIDQANKRMDEVDSAKERLTEGMDRLPAGIHEKLIEANDnATGALEKAMNTVTSVDSIQEGLDNDL 2158
Cdd:TIGR02168 793 ---QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED-LEEQIEELSEDIESLAAEIEELEELI 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2159 KPKLDVVKVNTKELQDLETmtgTMMEINNNLDGIRDVNRSIHTTLGALNRLnmslsqsLEELRESIQKAREQANNIKVSL 2238
Cdd:TIGR02168 869 EELESELEALLNERASLEE---ALALLRSELEELSEELRELESKRSELRRE-------LEELREKLAQLELRLEGLEVRI 938
|
.
gi 919026507 2239 A 2239
Cdd:TIGR02168 939 D 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1837-2149 |
2.02e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1837 IENADNELElakALKSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQSAKDSRAAL-ELNQKndelIKKLQNMTQA 1915
Cdd:TIGR02168 234 LEELREELE---ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyALANE----ISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1916 LQTRALAVSSMLNMSSEMLKEANMTLPNSSAEF--LRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAEKLR- 1992
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELaeLEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRs 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1993 ------MQADNLDNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQ----SAHDLASEAMNKTTTADGSTLQ---EKA 2059
Cdd:TIGR02168 387 kvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelQAELEELEEELEELQEELERLEealEEL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2060 KKSANTSLDFVNEANRLVNSSKDLKDLLGSIDKDIDQANKRMDEVDSAKERLTEGMDRLPAGIH-----EKLIEAndnat 2134
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvdegyEAAIEA----- 541
|
330
....*....|....*
gi 919026507 2135 gALEKAMNTVTSVDS 2149
Cdd:TIGR02168 542 -ALGGRLQAVVVENL 555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1943-2240 |
2.04e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1943 NSSAEFLRDLLE---------QLKKDTEN-----------LTIAAGLLRQNLPNLEPKVRQAEELAEkLRMQADNLD--- 1999
Cdd:TIGR02168 151 EAKPEERRAIFEeaagiskykERRKETERklertrenldrLEDILNELERQLKSLERQAEKAERYKE-LKAELRELElal 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2000 -----NMFQGARATSEDAVKAAQV----YEGIVVAVDDALKEAQSAHDLASEAMNKTTTADGSTLQEKAK---------- 2060
Cdd:TIGR02168 230 lvlrlEELREELEELQEELKEAEEeleeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkqilre 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2061 --KSANTSLDFVNEANRLVNSSKD-LKDLLGSIDKDIDQANKRMDEVD---SAKERLTEGMDRLPAGIHEKLIEANDN-- 2132
Cdd:TIGR02168 310 rlANLERQLEELEAQLEELESKLDeLAEELAELEEKLEELKEELESLEaelEELEAELEELESRLEELEEQLETLRSKva 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2133 -ATGALEKAMNTVTSVDSIQEGLDNDLKPKLDVVKVNTKELQDLEtmtgtMMEINNNLDGIrdvNRSIHTTLGALNRLNM 2211
Cdd:TIGR02168 390 qLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEEL---EEELEELQEELERLEE 461
|
330 340 350
....*....|....*....|....*....|..
gi 919026507 2212 ---SLSQSLEELRESIQKAREQANNIKVSLAA 2240
Cdd:TIGR02168 462 aleELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1829-2255 |
2.33e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1829 RERDFKPNIENADNELELAKALKSSISDLQSKLTNVTDAAISIQELADRLNDL---ISLAEQSAKDSRAAL--------- 1896
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELeaeLEELREELEKLEKLLqllplyqel 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1897 -ELNQKNDELIKKLQNMTQALQTRALAVSSMLNMSSEM------LKEANMTLPNSSAEFLRDLLEQLKKdtenltiaagl 1969
Cdd:COG4717 135 eALEAELAELPERLEELEERLEELRELEEELEELEAELaelqeeLEELLEQLSLATEEELQDLAEELEE----------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1970 LRQNLPNLEPKVRQAEELAEKLRMQADNLDNmfQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSAHDLASEAMNKTT- 2048
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2049 ----TADGSTLQEKAKKSANTSLDFVNEANRLVN-SSKDLKDLLGSID--------------KDIDQANKRMDEVDSAKE 2109
Cdd:COG4717 282 vlglLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGlppdlspeellellDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2110 RLT-----EGMDRLPAGIHEKLIEANDNATGALEKAMNTVTSVDSIQEGLDNDLKPKLDVVKVNTK-----ELQDLET-M 2178
Cdd:COG4717 362 ELQleeleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeleeELEELEEeL 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 2179 TGTMMEINNNLDGIRDVNRSIHtTLGALNRLnMSLSQSLEELRESIQKAREQANNIKVSLAAGGSCHREYRTEELKP 2255
Cdd:COG4717 442 EELEEELEELREELAELEAELE-QLEEDGEL-AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPP 516
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
280-327 |
2.38e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.88 E-value: 2.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 919026507 280 CKCYGHASSCPR-SPDTGKlmCVCEDNTCGKNCEKCCPKFNQQPYKPGT 327
Cdd:cd00055 2 CDCNGHGSLSGQcDPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1741-2256 |
2.98e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.96 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1741 DMEVIVKELQANATKLYTQTSSMANDAM----GYSMVASNLSKTADGMEKEIREIITSARDLLDNLPDVHQLSgnvnlts 1816
Cdd:COG5185 5 SKFLQVKNPLAKEGNANKELIEILLESSksegKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLNYQNDVK------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1817 vmmKAQDIMKMIRERDFKPNIENADNELElakalKSSIsdlqsKLTNVTDAAISIQELADRLNDLI-----SLAEQSAKD 1891
Cdd:COG5185 78 ---KSESSVKARKFLKEKKLDTKILQEYV-----NSLI-----KLPNYEWSADILISLLYLYKSEIvalkdELIKVEKLD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1892 SRAALELNQKNDELIKKLQNM---TQALQTRALAVSSMLNMSSEMLKEANMTLPNSSAEF---LRDLLEQLKKDTENLTI 1965
Cdd:COG5185 145 EIADIEASYGEVETGIIKDIFgklTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVnsiKESETGNLGSESTLLEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1966 AAGLlrQNLPNLEPKVRQAEELAEKLRMQADNL-DNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSAHDLASEAM 2044
Cdd:COG5185 225 AKEI--INIEEALKGFQDPESELEDLAQTSDKLeKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2045 nKTTTADGSTLQEKAKKSANTSLDFVNEANRLVNSSkdLKDLLGSIDKDIDQANKRMDEVDSAKERL--TEGMDRLPAGI 2122
Cdd:COG5185 303 -KSIDIKKATESLEEQLAAAEAEQELEESKRETETG--IQNLTAEIEQGQESLTENLEAIKEEIENIvgEVELSKSSEEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2123 H------EKLIEANDNATGALEKAMN--------TVTSVDSIQEGLDNDLKPKLDVVKVNTKELQDLET-----MTGTMM 2183
Cdd:COG5185 380 DsfkdtiESTKESLDEIPQNQRGYAQeilatledTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISelnkvMREADE 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919026507 2184 EINNNLDGIRD-VNRSIHTTLGALNRLNMSLSQSLEELRESIQKAReqaNNIKVSLAAGGSCHREYrTEELKPS 2256
Cdd:COG5185 460 ESQSRLEEAYDeINRSVRSKKEDLNEELTQIESRVSTLKATLEKLR---AKLERQLEGVRSKLDQV-AESLKDF 529
|
|
| PHA03413 |
PHA03413 |
putative internal core protein; Provisional |
1687-2135 |
4.84e-05 |
|
putative internal core protein; Provisional
Pssm-ID: 177641 Cd Length: 1304 Bit Score: 49.31 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1687 TRDLMVAVDEMEVMVRGVNTSTMVVIPWERFFAmenktqvlrgkldaiRKVKVGDMEVIVKELQANATKLYTQTSSMAND 1766
Cdd:PHA03413 227 AKAVRAAANAAEVESRALGSATEHVFTAETGLA---------------AKAQTGGVLSDAPEIVPDVVKPEVAAEPMFDP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1767 AMGYSMVASNLSKTADGMEKEIREIITSARDlldnlpDVHQLSGNvNLTSVMMKAQDIMKMIRERDfkpniENADNELEL 1846
Cdd:PHA03413 292 DAPTNETAEDAKVPGTGEGEESFPILDKPLD------ERIQASRN-GRASVNIKAQDLVQFLKNMD-----HLSAGAKAI 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1847 AKALKSSISDLQSKLTNVT----DAAISIQELADRlnDLISLAEQSAKD----SRAALELNQKN-DELIKKLQNMTQALQ 1917
Cdd:PHA03413 360 LDALGDAINDIDFKLMAASanrsRYTFAQQDLAKR--EEIKLRAPAKADgstfKTVGDALNAMDaDTSRVAVHELIHAAT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1918 TRALAVSSMLNMSSEMlkeanmtlpnssAEFLRDLLE---QLKKDTE---NLTIAAGLLRQNLPNLEPKVRQAEELAE-- 1989
Cdd:PHA03413 438 AKAIFQASKGDSAPEI------------ADAIKDLDAlhaSIAADREfapKMRYAASNNHEFLAELADKPEMVEDLAKlp 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1990 -------KLRMQADNLDNM--FQGARATSEDAVKAaqvYEGIV-VAVDDALKEAQS-----AHDLASEAMNKTTTAD-GS 2053
Cdd:PHA03413 506 gvpagknALQALAEKILKAlgFKAKGSALDDALDA---FEDAAkWQAKDNADKANAffsdaFADLADDANRGANAAErAK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2054 TLQEKAKKSANTSLDFVNEANRlvnSSKDLKDLLGSidkDIDQANKRMDEVDSAKERLTEGMDRLPAGIHEKLIEANDNA 2133
Cdd:PHA03413 583 ALEDGAKKKLKQMFALWDNIAQ---GNEDLAKLLVS---DASAMGERAPSVVDHKRNLTLEMDARAAAVEDAILAALKDK 656
|
..
gi 919026507 2134 TG 2135
Cdd:PHA03413 657 HG 658
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1712-2131 |
5.33e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.13 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1712 IPWERFFAMENKTQvlRGKLDAIRKVKVG-----DMEVIVKELQANATKLYTQTSSMANDAMGYSMVASNLSKTADGMEK 1786
Cdd:PLN02939 25 LPSRRRLAVSCRAR--RRGFSSQQKKKRGkniapKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1787 EI-REIITSARDLLDNLPDVHQLSgNVNLtsvmmkaQDIMKMIRerdfkpNIENadNELELAKALKSSISDLQSKLTNVT 1865
Cdd:PLN02939 103 QRdEAIAAIDNEQQTNSKDGEQLS-DFQL-------EDLVGMIQ------NAEK--NILLLNQARLQALEDLEKILTEKE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1866 DAAISIQELADRLNDLISLAEQSAKDsRAALELNqknDELIKKLQNMTQALQTRALAVSSMLNMSSEMLKEANMTLPNsS 1945
Cdd:PLN02939 167 ALQGKINILEMRLSETDARIKLAAQE-KIHVEIL---EEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKD-D 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1946 AEFLRDLLEQLKKDTENLTI---AAGLLRQNLPNLEPKVRQAEELAEKLRM--------QADNLDNMFQGARATSEDAVK 2014
Cdd:PLN02939 242 IQFLKAELIEVAETEERVFKlekERSLLDASLRELESKFIVAQEDVSKLSPlqydcwweKVENLQDLLDRATNQVEKAAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2015 AAQVYEGIVVAVD---DALKEAqSAHDLASEAMNktttadgsTLQEKAkKSANTSLDFVN-EANRLV----NSSKDLKDL 2086
Cdd:PLN02939 322 VLDQNQDLRDKVDkleASLKEA-NVSKFSSYKVE--------LLQQKL-KLLEERLQASDhEIHSYIqlyqESIKEFQDT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 919026507 2087 LGSIdkdIDQANKR-MDEvdSAKERLTEGMDRLPAGIH----EKLIEAND 2131
Cdd:PLN02939 392 LSKL---KEESKKRsLEH--PADDMPSEFWSRILLLIDgwllEKKISNND 436
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1720-2001 |
6.06e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1720 MENKTQVLRGKLDA----IRKVKvGDMEVIVKELQANAT---KLYTQTSSMANDAMGYSMVASNLSKTADGMEKEIREII 1792
Cdd:TIGR04523 459 LDNTRESLETQLKVlsrsINKIK-QNLEQKQKELKSKEKelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1793 TSARDLLDNLpdvhqLSGNVNLTSVMMKA------QDIMKMIRERDfkpNIENADNEL-ELAKALKSSISDLQSKLTNVT 1865
Cdd:TIGR04523 538 SKISDLEDEL-----NKDDFELKKENLEKeideknKEIEELKQTQK---SLKKKQEEKqELIDQKEKEKKDLIKEIEEKE 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1866 daaisiqELADRLNDLISLAEqsakdsraalELNQKNDELIKKLQNMTQALQTRALAVSSML----NMSSEMLKEAN--M 1939
Cdd:TIGR04523 610 -------KKISSLEKELEKAK----------KENEKLSSIIKNIKSKKNKLKQEVKQIKETIkeirNKWPEIIKKIKesK 672
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919026507 1940 TLPNSSAEFLRDLLEQL-----KKDTENLTIaagllrQNLPNLEPKVRQAEELAEKLRMQADNLDNM 2001
Cdd:TIGR04523 673 TKIDDIIELMKDWLKELslhykKYITRMIRI------KDLPKLEEKYKEIEKELKKLDEFSKELENI 733
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1832-2075 |
1.02e-04 |
|
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: 48.10 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1832 DFKPNIENADNElelAKALKSSISDLQSKLTN-----------VTDAAISIQELADRLNDL---ISLAEQSAKDSRaale 1897
Cdd:pfam05701 304 EVKANIEKAKDE---VNCLRVAAASLRSELEKekaelaslrqrEGMASIAVSSLEAELNRTkseIALVQAKEKEAR---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1898 lnQKNDELIKKLQNMTQ-ALQTRALAVSS--MLNMSSEMLKEANMTLpnSSAEFlRdlLEQLKKDTEnltiAAgllrqnl 1974
Cdd:pfam05701 377 --EKMVELPKQLQQAAQeAEEAKSLAQAAreELRKAKEEAEQAKAAA--STVES-R--LEAVLKEIE----AA------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1975 pnlepkvRQAEELAeklRMQADNLDNMFQGARATSEDAVKAaqvyeGIVVAVDDALKEAQSAHDlASEAMNKTTTADGST 2054
Cdd:pfam05701 439 -------KASEKLA---LAAIKALQESESSAESTNQEDSPR-----GVTLSLEEYYELSKRAHE-AEELANKRVAEAVSQ 502
|
250 260
....*....|....*....|.
gi 919026507 2055 LQEkAKKSANTSLDFVNEANR 2075
Cdd:pfam05701 503 IEE-AKESELRSLEKLEEVNR 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1870-2235 |
1.21e-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: 48.14 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1870 SIQELADRLNDL-ISLAEQSAKDSRAALELNQKNDELiKKLQNMTQALQTRALAVSSMLNMSSEMLKEanmtlpnssaef 1948
Cdd:TIGR02169 675 ELQRLRERLEGLkRELSSLQSELRRIENRLDELSQEL-SDASRKIGEIEKEIEQLEQEEEKLKERLEE------------ 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1949 LRDLLEQLKKDTENLtiaagllRQNLPNLEPKVRQAEELAEKLRMQADNLDNM-----FQGARATSEDAVKAAQVYEGIV 2023
Cdd:TIGR02169 742 LEEDLSSLEQEIENV-------KSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2024 VAVDDALKEAQSAHDLASEAM-NKTTTADGSTLQEKAKKSANTSL-----DFVNEANRLVNSSKDLKDLLGSIDKDIDQA 2097
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLngkkeELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2098 NKRMDEVDSAKERLTEGMDRLPAGIHE---KLIEANDNATgALEKAmntvtsVDSIQEGLDNDlkPKLDVVKvntKELQD 2174
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSElkaKLEALEEELS-EIEDP------KGEDEEIPEEE--LSLEDVQ---AELQR 962
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919026507 2175 LETMTGTMMEINnnldgirdvNRSIHTTLGALNRLNmSLS---QSLEELRESIQKAREQANNIK 2235
Cdd:TIGR02169 963 VEEEIRALEPVN---------MLAIQEYEEVLKRLD-ELKekrAKLEEERKAILERIEEYEKKK 1016
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1749-2118 |
1.33e-04 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 47.71 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1749 LQANATKLYTQTSSMANDAMGYSMVASNLSKTADGMEKEIREIITSARDLLDNLPDVHQLSGNVNLTSVMMKAQDIMKMI 1828
Cdd:COG0840 2 LILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1829 RERDFKPNIENADNELELAKALKSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQSAKDSRAALELNQKNDELIKK 1908
Cdd:COG0840 82 LALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1909 LQNMTQALQTRALAVSSMLNMSSEMLKEANMTLPNSSAEFL-RDLLEQLKKDTENL-TIAAGLLRQNLPnlepkVRQAEE 1986
Cdd:COG0840 162 ALAALLEAAALALAAAALALALLAAALLALVALAIILALLLsRSITRPLRELLEVLeRIAEGDLTVRID-----VDSKDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1987 ---LAEKLRMQADNLDNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSAHDLASEAMNKTTtadgSTLQEKAKkSA 2063
Cdd:COG0840 237 igqLADAFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELS----ATVQEVAE-NA 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 919026507 2064 NTSLDFVNEANRLVNSSKDLkdllgsidkdIDQANKRMDEVDSAKERLTEGMDRL 2118
Cdd:COG0840 312 QQAAELAEEASELAEEGGEV----------VEEAVEGIEEIRESVEETAETIEEL 356
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1898-2238 |
1.51e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.54 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1898 LNQKNDELIKKLQNMTQALQTRALAvssmlnmsSEMLKEANMTLPNSSAEflrdLLEQLKKDTENLTiaagllRQNLPNL 1977
Cdd:pfam06160 4 LRKKIYKEIDELEERKNELMNLPVQ--------EELSKVKKLNLTGETQE----KFEEWRKKWDDIV------TKSLPDI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1978 EPKVRQAEELAEKLRmqadnldnmFQGARATSEDAVKAAQVYEGIVVAVDDALKEAqsahdLASEAMNKTTTADGSTLQE 2057
Cdd:pfam06160 66 EELLFEAEELNDKYR---------FKKAKKALDEIEELLDDIEEDIKQILEELDEL-----LESEEKNREEVEELKDKYR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2058 KAKKSANtsldfvneANR--LVNSSKDLKDLLGSIDKDIDQANKRM---------DEVDSAKER---LTEGMDRLPagih 2123
Cdd:pfam06160 132 ELRKTLL--------ANRfsYGPAIDELEKQLAEIEEEFSQFEELTesgdylearEVLEKLEEEtdaLEELMEDIP---- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2124 eklieandnatGALEKAMNTV-TSVDSIQEGLDnDLKPK---LDVVKVnTKELQDLET-MTGTMMEINN-NLDGIRDVNR 2197
Cdd:pfam06160 200 -----------PLYEELKTELpDQLEELKEGYR-EMEEEgyaLEHLNV-DKEIQQLEEqLEENLALLENlELDEAEEALE 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 2198 SIHTTLGAL-----------NRLNmslsQSLEELRESIQKAREQANNIKVSL 2238
Cdd:pfam06160 267 EIEERIDQLydllekevdakKYVE----KNLPEIEDYLEHAEEQNKELKEEL 314
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1747-1954 |
1.53e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 44.95 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1747 KELQANATKLYTQTSSMANDAMgysmvaSNLSKTADGMEKEIREIITSARDlldnlpdvhqlsgnvnltSVMMKAQDIMK 1826
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELV------DRLEKETEALRERLQKDLEEVRA------------------KLEPYLEELQA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1827 MIRErdfkpNIENADNEL-----ELAKALKSSISDLQSKLTNVTDaaisiqELADRlndlislAEQSAKDSRAALE---- 1897
Cdd:pfam01442 63 KLGQ-----NVEELRQRLepyteELRKRLNADAEELQEKLAPYGE------ELRER-------LEQNVDALRARLApyae 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919026507 1898 -----LNQKNDELIKKLQNMTQALQTRAlavSSMLNMSSEMLKEAnmtlpnssAEFLRDLLE 1954
Cdd:pfam01442 125 elrqkLAERLEELKESLAPYAEEVQAQL---SQRLQELREKLEPQ--------AEDLREKLD 175
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1998-2194 |
1.74e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.59 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1998 LDNMFQGARATSEDAVKAAQvyEGIVVAVDDALKEAQSAHDLASEAMNKTTTADGSTLQEKAK-KSANTSLD--FVNEAN 2074
Cdd:cd22656 97 LELIDDLADATDDEELEEAK--KTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAlETLEKALKdlLTDEGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2075 RLVNssKDLKDLlgsiDKDIDQANKrmDEVDSAKERLtegmdrlpagihEKLIEANDNATGALEKAMNTVTSVDSIQEGL 2154
Cdd:cd22656 175 AIAR--KEIKDL----QKELEKLNE--EYAAKLKAKI------------DELKALIADDEAKLAAALRLIADLTAADTDL 234
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 919026507 2155 DNdLKPKLDVVkvntkeLQDLETMTGTMMEINNNLDGIRD 2194
Cdd:cd22656 235 DN-LLALIGPA------IPALEKLQGAWQAIATDLDSLKD 267
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1845-2096 |
2.77e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1845 ELAKALKSSISDLQSKLTNVTDAAISIQELADRLNDLISlaeqsakdsraalELNQKNDELIKKLQNMTQALQTRALAVS 1924
Cdd:PHA02562 167 EMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIE-------------EQRKKNGENIARKQNKYDELVEEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1925 SMLNMSSEMLKEANMTLPNSSAEF--LRDLLEQLKKDTENLTIAAGLLRQN--LPNLEPKVRQAEELAEKLRmqaDNLDN 2000
Cdd:PHA02562 234 AEIEELTDELLNLVMDIEDPSAALnkLNTAAAKIKSKIEQFQKVIKMYEKGgvCPTCTQQISEGPDRITKIK---DKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2001 MFQGARATSEDAVKAAQVyegivvaVDDALKEAQSAHDLASEAMNKTTTADGSTLQEKAKKSA--NTSLDFVNEAN---R 2075
Cdd:PHA02562 311 LQHSLEKLDTAIDELEEI-------MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAieELQAEFVDNAEelaK 383
|
250 260
....*....|....*....|.
gi 919026507 2076 LVNSSKDLKDLLGSIDKDIDQ 2096
Cdd:PHA02562 384 LQDELDKIVKTKSELVKEKYH 404
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1836-2178 |
2.84e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1836 NIENADNELELAKA----LKSSISDLQSKLTNVTDAAISIQELADRLNDLISLAEQSAKDSRAALE-LNQKNDEL----- 1905
Cdd:COG4372 39 ELDKLQEELEQLREeleqAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELEsLQEEAEELqeele 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1906 -----IKKLQNMTQALQTRALAVSSMLNMSSEMLKEANMTLpnssaEFLRDLLEQLKKDTENLTIAAglLRQNLPNLepk 1980
Cdd:COG4372 119 elqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL-----ESLQEELAALEQELQALSEAE--AEQALDEL--- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1981 VRQAEELAEKLRMQADNLDNMFQGARATSEDAVKAAQVYEGIVVAVDDALKEAQSahdlaseamnktttadgstLQEKAK 2060
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE-------------------LEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2061 KSANTSLDFVNEANRLVNSskdlkDLLGSIDKDIDQANKRMDEVDSAKERLTEGMDRLPAGIHEKLIEANDNATGALEKA 2140
Cdd:COG4372 250 ELLEEVILKEIEELELAIL-----VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350
....*....|....*....|....*....|....*...
gi 919026507 2141 MNTVTSVDSIQEGLDNDLKPKLDVVKVNTKELQDLETM 2178
Cdd:COG4372 325 AKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
879-928 |
3.55e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.37 E-value: 3.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 879 CACS--GNINPNavgnCDRTTGQCLkCLFNTEGWNCAQCKPDYYGmVYGKGC 928
Cdd:smart00180 1 CDCDpgGSASGT----CDPDTGQCE-CKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1746-2003 |
4.36e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 45.46 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1746 VKELQANATKLYTQTSSMANDAM-----------GYSMVASNLSKTADGMEKEIREIITSARDLLDNLPDVHQlsgnvNL 1814
Cdd:pfam04108 5 AQDLCRWANELLTDARSLLEELVvllakiaflrrGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALE-----RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1815 TSVMmkaqDIMKMIRERDFKPNIENA----------DNELELAKALKSSISDLQSKLTNVTDaaiSIQELADRLNDLISL 1884
Cdd:pfam04108 80 EETL----DKLRNTPVEPALPPGEEKqktlldfideDSVEILRDALKELIDELQAAQESLDS---DLKRFDDDLRDLQKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1885 AEQSAKDSRAALELNQKNDELIKKLQNMTQALQtralavssMLNMSSEMLKEANMTLPNSSAEflrdLLEQLKKDTENLT 1964
Cdd:pfam04108 153 LESLSSPSESISLIPTLLKELESLEEEMASLLE--------SLTNHYDQCVTAVKLTEGGRAE----MLEVLENDARELD 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 919026507 1965 IAAGLLRQNLPNLEPKVRQAEELAEKLRMQADNLDNMFQ 2003
Cdd:pfam04108 221 DVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQ 259
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1812-1915 |
4.61e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 42.96 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1812 VNLTSVMMK---AQDIMKMIrERDFKPNienaDNELE-LAKALKSSISDLQSKLTNVTDAAIsiQELADRLNDLISLAEQ 1887
Cdd:smart00935 4 VDVQKILQEspaGKAAQKQL-EKEFKKR----QAELEkLEKELQKLKEKLQKDAATLSEAAR--EKKEKELQKKVQEFQR 76
|
90 100
....*....|....*....|....*...
gi 919026507 1888 SAKDSRAalELNQKNDELIKKLQNMTQA 1915
Cdd:smart00935 77 KQQKLQQ--DLQKRQQEELQKILDKINK 102
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1886-2225 |
4.80e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1886 EQSAKDSRAALELNQKNDELIKKLQNMTQALQTRALAVSSMLNMSSEMLKEANMTL-----PNSSAEFLRDLLEqlkkdT 1960
Cdd:PRK01156 87 ERRGKGSRREAYIKKDGSIIAEGFDDTTKYIEKNILGISKDVFLNSIFVGQGEMDSlisgdPAQRKKILDEILE-----I 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1961 ENLTIAAGLLRQNLPNLEPKVRQAEELAEKLRMQADNLDNM------FQGARATSEDAVKAAQVYEGIV----VAVDDAL 2030
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqiadDEKSHSITLKEIERLSIEYNNAmddyNNLKSAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2031 KEAQSAHDLASEAMNKTTTADG------------STLQEKAKKSANT----SLDFVNEANRLVNSSKDLKDLLGSIDKDI 2094
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESdlsmeleknnyyKELEERHMKIINDpvykNRNYINDYFKYKNDIENKKQILSNIDAEI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2095 ---DQANKRMDEVDSakerltegmDRLPAGIHEKLIEANDNATGALEK-AMNTVTSVDSIQEgldndLKPKLDVVKVNTK 2170
Cdd:PRK01156 322 nkyHAIIKKLSVLQK---------DYNDYIKKKSRYDDLNNQILELEGyEMDYNSYLKSIES-----LKKKIEEYSKNIE 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2171 ELQDLETMTGTMMEIN-NNLDGIR-DVNRS---IHTTLGALNRLNMSLSQSLEELRESIQ 2225
Cdd:PRK01156 388 RMSAFISEILKIQEIDpDAIKKELnEINVKlqdISSKVSSLNQRIRALRENLDELSRNME 447
|
|
| Tht1 |
pfam04163 |
Tht1-like nuclear fusion protein; |
1748-2017 |
6.18e-04 |
|
Tht1-like nuclear fusion protein;
Pssm-ID: 282073 Cd Length: 595 Bit Score: 45.59 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1748 ELQANATKLYTQTSS---------MANDAMGYSMVASNLSKTADGMEKEIREIITSARDLLDN-LPDVHQLSGNVNLTSV 1817
Cdd:pfam04163 166 ELFLNITELQDQFGDdldmkilhlMFQMEQDFENFLDDLAQMFDKFDGEFNNATESNRIIIENdFKDFNFKVNDEIMGLV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1818 MMKAQDIMKMIRERDFkpnienadneLELAKALKSSISDLQSKLTNVTDaaisiqELADRLNDLISLAEQSAKDSRAALE 1897
Cdd:pfam04163 246 ELENHEQEGMVLEKEI----------IEKIKQLKNEIDDIHHFFADFAD------ELAGYKNDIIEKINDLKDDSENAIA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1898 LNQKNDELIKKLQNMTQALQtralavsSMLNMSSEMLKE---ANMTLPNSSAEFLRDLLEQLKKDTENLTiaagllrqnl 1974
Cdd:pfam04163 310 LSAIGKYTSEFSAFMEKNIK-------DLIEMSEDSLKEsvqRNIDFVNSGFQELEDFSIGLKEELGGLK---------- 372
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 919026507 1975 pnlepkvrqaEELAEKLRMQADNLDNMFQGARATSEDAVKAAQ 2017
Cdd:pfam04163 373 ----------KDLSEQQNLEAEEILQWKSDFLNILHDHLKVLQ 405
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1847-2059 |
7.92e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 43.02 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1847 AKALKSSISDLQSKLTNVTdaaisiQELADRLndlislaeqsAKDSRAALElnqkndELIKKLQNMTQALQTRALAVSSM 1926
Cdd:pfam01442 6 LDELSTYAEELQEQLGPVA------QELVDRL----------EKETEALRE------RLQKDLEEVRAKLEPYLEELQAK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1927 LNMSSEMLKEanmTLpnssAEFLRDLLEQLKKDTENLTiaagllRQnlpnLEPKvrqAEELAEKLRmqaDNLDNMFQGAR 2006
Cdd:pfam01442 64 LGQNVEELRQ---RL----EPYTEELRKRLNADAEELQ------EK----LAPY---GEELRERLE---QNVDALRARLA 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 919026507 2007 ATSEDAV-KAAQVYEGIVVAVDDALKEAQSAHDLASEAMNKTTTADGSTLQEKA 2059
Cdd:pfam01442 121 PYAEELRqKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQAEDLREKL 174
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1605-1632 |
9.28e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 39.64 E-value: 9.28e-04
10 20
....*....|....*....|....*...
gi 919026507 1605 CPRGYEGDHCERCSDYFYGDPTKLGGEC 1632
Cdd:pfam00053 22 CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
848-876 |
1.27e-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: 39.26 E-value: 1.27e-03
10 20
....*....|....*....|....*....
gi 919026507 848 SCPDGYIGNHCEMCDDGYFGNPLVPGNYC 876
Cdd:pfam00053 21 LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1790-2017 |
1.46e-03 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 44.29 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1790 EIITSARDLLDNLPDVHQLSGNVNLTSVMMKAQDIMKMIRErdfkpNIENADNELELAKALKSSISDLQS---KLTNVTD 1866
Cdd:COG4192 59 KLEENSNELVAALPEFAAATNTTERSQLRNQLNTQLADIEE-----LLAELEQLTQDAGDLRAAVADLRNllqQLDSLLT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1867 AAISI----QELADRLNDL-------ISLAEQSAKDSRAALELNQKNDELIKKLQNMTQALQTRALAVSSMLNMSSEMLK 1935
Cdd:COG4192 134 QRIALrrrlQELLEQINWLhqdfnseLTPLLQEASWQQTRLLDSVETTESLRNLQNELQLLLRLLAIENQIVSLLREVAA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1936 -------EANMTLPNSSAEFLRDLLEQLKKDTENLT--------IAAGLLRQNLPNLEPK----VRQAEELAEKLRMQAD 1996
Cdd:COG4192 214 ardqadvDNLFDRLQYLKDELDRNLQALKNYPSTITlrqlidelLAIGSGEGGLPSLRRDelaaQATLEALAEENNSILE 293
|
250 260
....*....|....*....|..
gi 919026507 1997 NLDNMFQG-ARATSEDAVKAAQ 2017
Cdd:COG4192 294 QLRTQISGlVGNSREQLVALNQ 315
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1844-2007 |
1.68e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 44.21 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1844 LELAKA---LKSSISDlqSKLTNVTDAaisIQELADRLND-LISLAEQSAKDS----RAALELNQKNDELIKKLQNMTQA 1915
Cdd:pfam13779 447 LGLRSAlarLELARSD--EALDEVADL---LWELALRIEDgDLSDAERRLRAAqerlSEALERGASDEEIAKLMQELREA 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1916 LQT--RALA--VSSMLNMSSEMLKEANMTLPN-----------------SSAEfLRDLLEQLKKDTENLTIAAGLLRQNL 1974
Cdd:pfam13779 522 LDDymQALAeqAQQNPQDLQQPDDPNAQEMTQqdlqrmldrieelarsgRRAE-AQQMLSQLQQMLENLQAGQPQQQQQQ 600
|
170 180 190
....*....|....*....|....*....|...
gi 919026507 1975 PNlEPKVRQAEELAEKLRMQADNLDNMFQGARA 2007
Cdd:pfam13779 601 GQ-SEMQQAMDELGDLLREQQQLLDETFRQLQQ 632
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
368-401 |
1.87e-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: 1.87e-03
10 20 30
....*....|....*....|....*....|....
gi 919026507 368 GGVCMnCRDHTTGVNCEQCEAGYYRTTDDPREPC 401
Cdd:pfam00053 17 TGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1576-1625 |
2.30e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 2.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919026507 1576 CGCPrlePQNNFSPTCVtnatADGYVCNaCPRGYEGDHCERCSDYFYGDP 1625
Cdd:smart00180 1 CDCD---PGGSASGTCD----PDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1818-1966 |
2.69e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 41.85 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1818 MMKAQDIMKMIRER---DFKPNIENADNELElaKALKSSISDLQSKLTNVTDAAISiqELADRLNDLISLAEQSAKdsRA 1894
Cdd:COG1390 1 MMSLEKIIEEILEEaeaEAEEILEEAEEEAE--KILEEAEEEAEEIKEEILEKAER--EAEREKRRIISSAELEAR--KE 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919026507 1895 ALELNQK-----NDELIKKLQNMTQALQTRALAVSSMLNMSSEML-KEANMTLPNSSAEFLRDLLEQLKKdtENLTIA 1966
Cdd:COG1390 75 LLEAKEElieevFEEALEKLKNLPKDPEYKELLKKLLKEAAEELGsGDLVVYVNEKDKELLEELLKELKK--KGLEVS 150
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1575-1630 |
2.87e-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: 38.10 E-value: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919026507 1575 PCGCPrlePQNNFSPTCVtnatADGYVCNaCPRGYEGDHCERCSDYFYGDPTKLGG 1630
Cdd:cd00055 1 PCDCN---GHGSLSGQCD----PGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1843-2138 |
3.13e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1843 ELELAKA--LKSSISDLQSKLTNVTDAaisIQELADRLNDLIS-LAEQSAKDSRAALELNQKNDElIKKLQNMTQALQTR 1919
Cdd:COG1196 221 ELKELEAelLLLKLRELEAELEELEAE---LEELEAELEELEAeLAELEAELEELRLELEELELE-LEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1920 ALAVSSMLNMSSEMLKEanmtlpnssaefLRDLLEQLKKDTENLTIAAGLLRQNLPNLEPKVRQAEELAEKLRMQADNLD 1999
Cdd:COG1196 297 LARLEQDIARLEERRRE------------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2000 NMFQGARATSEDAVKA-AQVYEGIVVAVDDALKEAQSAHDLAS---------EAMNKTTTADGSTLQEKAKKSANTSLDF 2069
Cdd:COG1196 365 EALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEaeeallerlERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919026507 2070 VNEANRLVNSSKDLKDLLGSIDKDIDQANKRMDEVDSAKERLTEGmdrlpAGIHEKLIEANDNATGALE 2138
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-----AARLLLLLEAEADYEGFLE 508
|
|
| IQG1 |
COG5261 |
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ... |
1823-2104 |
3.62e-03 |
|
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];
Pssm-ID: 227586 [Multi-domain] Cd Length: 1054 Bit Score: 43.34 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1823 DIMKMIRERDFKPNIENADNELELAKALKSSISDLQSKLTNVTDAAISIQELADRLNDLISLaEQSAKDSRaalelnQKN 1902
Cdd:COG5261 610 DSLGLIGGFFFLRFVNEALVSPQTSMLKDSCPSDNVRKLATLSKILQSVFEITSSDKFDVPL-QPFLKEYK------EKV 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1903 DELIKKLQNMTQALQtrALAVSSMLNMSSemLKEANMTLPNSSAEFLRDLLEQLKkDTENLTIAAGLLRQNLPNLEPKVR 1982
Cdd:COG5261 683 HNLLRKLGNVGDFEE--YFEFDQYIDLVK--KSRALEYLVNEIYLTHEIIIEYLD-NLYDPDSLVDLLLQELGELCSFPQ 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1983 QAEELAEKLRMQA------DNLDNMFQGARATSEDAV---KAAQVYEGIVVAVDDalKEAQSAHDLASEAMNKTTTADGS 2053
Cdd:COG5261 758 DQRDTLNCLVTLPlfnrsdDPIRDLKQQLKRTRVYIIyvdAGTNLFEQLLRLLPS--DEPATRNPLDLNPNIRDDPSVSS 835
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 919026507 2054 TLQEKAKKSANTSLDFVNEAN--RLVNSSKDLKDLLGSIDKDIDQANKRMDEV 2104
Cdd:COG5261 836 LKSMSLMKLKIRAIELLDELEtlGFVSRENRYQPLLNEIAKDIINLDALYERR 888
|
|
| YaaN |
COG3853 |
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms]; |
2108-2229 |
3.92e-03 |
|
Uncharacterized conserved protein YaaN involved in tellurite resistance [Defense mechanisms];
Pssm-ID: 443062 Cd Length: 389 Bit Score: 42.57 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 2108 KERLTEGMDRLPAGIH--EKLIEANDNATGALEKAMNTVTSVDSIQEgLdNDLKPKLDVVKvntKELQDLET-MTGTM-- 2182
Cdd:COG3853 178 YEKNWEYFKELNQYIAagELKLEELEAKIPALAAEAEASGDPEDAQA-L-NDLEQVLFRLE---QRVHDLLLqRAVSIqg 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 919026507 2183 -----MEINNNLDGIRDVNRSIHTTLGALnRLNMSLSQSLEELRESIQKARE 2229
Cdd:COG3853 253 apqirLVQKNNQELIEKIQSAITTTIPLW-KNQVAVALALARQKLALDAQKA 303
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
796-1126 |
4.00e-03 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 42.65 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 796 CENCEFGYYGNATRGTPNDCRPCACPLAISTNNFASNCMAAPPGSqeeyfCVSCPDGyigNHCEMCDDGYFGNplvpGNY 875
Cdd:pfam03302 39 CEECNSNNYLTPTSQCIDDCAKIGNYYYTTNANNKKICKECTVAN-----CKTCEDQ---GQCQACNDGFYKS----GDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 876 CQPCacsgniNPNAVGNCDRTTGQCLKCLfntegwncaqckpdyygmvYGKGCKECDCNQYGSTGTSCDQRSGqcscrpy 955
Cdd:pfam03302 107 CSPC------HESCKTCSGGTASDCTECL-------------------TGKALRYGNDGTKGTCGEGCTTGTG------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 956 yEGrACDSCvagyGNIIAGCPRCS-CNLTGSV--SNLCDQVSGQCP--CKNG-VGGQYCGSClPDHWEYSEEGCKACNch 1029
Cdd:pfam03302 155 -AG-ACKTC----GLTIDGTSYCSeCATETEYpqNGVCTSTAARATatCKASsVANGMCSSC-ANGYFRMNGGCYETT-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919026507 1030 lKGSNDSQCDLVTGTCTCQPNVIGDKCDQ-----CEINYYDLDSGNGCQSCDCDVTGSTSLqCGMTSGQCPCKPGVTgQK 1104
Cdd:pfam03302 226 -KFPGKSVCEEANSGGTCQKEAPGYKLNNgdlvtCSPGCKTCTSNTVCTTCMDGYVKTSDS-CTKCDSSCETCTGAT-TT 302
|
330 340
....*....|....*....|..
gi 919026507 1105 CDQCRPGYYGfSSNGCTECPVC 1126
Cdd:pfam03302 303 CKTCATGYYK-SGTGCVSCTSS 323
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
367-402 |
4.60e-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: 37.72 E-value: 4.60e-03
10 20 30
....*....|....*....|....*....|....*.
gi 919026507 367 GGGVCMnCRDHTTGVNCEQCEAGYYRTTDDPREpCQ 402
Cdd:cd00055 17 GTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| |
