|
Name |
Accession |
Description |
Interval |
E-value |
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2114-2271 |
1.82e-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: 118.67 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 2114 GSYFPGDAYAIYKRNFNVGKFMDVDLELRTSEVNGILMSVAD-PINGFpaFSLEISNGNVVLSIDVGDGyPIRVQSTlps 2192
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSqNGGDF--LALELEDGRLVLRYDLGSG-SLVLSSK--- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 2193 nYTLCDNRWHNVSALYEDHQIVLRVDHYPPNTLLVQSNDVLRRvaTKAPLYIGGLPDTAPSGTLLLRENFKGCIRNVVI 2271
Cdd:cd00110 75 -TPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
416-556 |
1.88e-30 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 118.14 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 416 YFQLPPQFLGDRTTSYGGLLNYTLVTVGAFQnipEASLRQFPMVQLHTHDeLVLDYYEDRIVY--DKEVNRYSARLHESL 493
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPG---GGSLNSEPDVILEGNG-LRLSYSSPDQPPpdPGQEQTYSVRLHEEN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167879687 494 WKnHYDGQHITRAILMVALQNVRHIFVRGTITTDFRQVVLTNVTLDAGifVAGAENNRAYGIE 556
Cdd:pfam00052 77 WR-DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSA--VPGGSGPPASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1942-2089 |
8.75e-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: 110.97 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1942 HSIVTVAARNLWQRNFNIQFDFRTFYPNGVLFAAlGSKDKaKHFITLALRDGTLALTIR-GRKRDQLLLPVKLNDGQWHH 2020
Cdd:cd00110 7 SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYA-GSQNG-GDFLALELEDGRLVLRYDlGSGSLVLSSKTPLNDGQWHS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 2021 VSLNSVKKKATLSVHVGNSLSSAQIRLPKKLNAANNLFVGGIPDEALLPKELQPKPeeFKGCLRKFSVN 2089
Cdd:cd00110 85 VSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPG--FVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1708-1870 |
2.22e-27 |
|
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: 109.82 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1708 AGFYGNGWVEFP-SHSLRKRANFGFVFRTLEPNCSLLVSGfpSSLSSDFdskdlrgnYSVFLYEGKLNLWVDSGAGRVEL 1786
Cdd:cd00110 2 VSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAG--SQNGGDF--------LALELEDGRLVLRYDLGSGSLVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1787 ESNNTLNDGEYHVISVIKRGRTVELRIDDELQGSKGLPKAQALVNLPGEaggLFLGGVPDDpAFDSLSKTFSGLKGVIAN 1866
Cdd:cd00110 72 SSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGP---LYLGGLPED-LKSPGLPVSPGFVGCIRD 147
|
....
gi 167879687 1867 VVFN 1870
Cdd:cd00110 148 LKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1519-1681 |
5.07e-23 |
|
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: 97.49 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1519 RHFNGDGYAVLQKSSSHRSNkqFSLTLSFKTLDENALIFLALDETNNRSISLTLYQGRLVFRVDYGGdSKLEINTTNRYN 1598
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTR--LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGS-GSLVLSSKTPLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1599 TGQWVVVEAARSFSKGStengiLKVDNQE--EHRGAPTKPINsgmlpNLGVNYYLGGVPPGFKSGTTKAPgadHAFLGCL 1676
Cdd:cd00110 79 DGQWHSVSVERNGRSVT-----LSVDGERvvESGSPGGSALL-----NLDGPLYLGGLPEDLKSPGLPVS---PGFVGCI 145
|
....*
gi 167879687 1677 KGVHI 1681
Cdd:cd00110 146 RDLKV 150
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
130-175 |
1.49e-18 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 80.82 E-value: 1.49e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167879687 130 CTCDPSGSVHQECDAFSGQCYCKPGVEGPSCDRCQPGYYGFSSQGC 175
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
225-273 |
7.22e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.16 E-value: 7.22e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 225 CECDIAGSIGQSCNAQTGQCNCKEGFTGRQCNECAAGYYGYPNCQRCGC 273
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
81-127 |
2.13e-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: 66.22 E-value: 2.13e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 81 CNCHVQGSLNRICNQQRGLCVCKPFVEGRQCNRCVAGYWNL--ESGVGC 127
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
702-736 |
2.78e-11 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 2.78e-11
10 20 30
....*....|....*....|....*....|....*
gi 167879687 702 CDCNREGSLSDECETKSGQCQCKPGIMGKRCDRCE 736
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCA 35
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
600-646 |
4.62e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 4.62e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167879687 600 PCDCNGR---SEECHPETGHCLnCRNNTGGDSCQNCAEGFFGNP-NYGSCE 646
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-323 |
1.24e-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: 1.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167879687 271 CGCDERGSIprpdgSFDCDEH-GQCLCKSMVFGRQCDQCKSATFGLAAINPDGC 323
Cdd:pfam00053 1 CDCNPHGSL-----SDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1326-1469 |
5.90e-08 |
|
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: 53.96 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1326 SYAPVSYGPSTTNKIMLSVALSGDKPNSPLVFIQGEER-RFIAVEMVKRRIRLVWNLGDEVVVITHPTEIKprdpkyDDA 1404
Cdd:cd00110 8 SYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGgDFLALELEDGRLVLRYDLGSGSLVLSSKTPLN------DGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167879687 1405 WYFIEANRTFNLCNLNVRRmthsgvlvhSNPVTGASNPEQSKLTMGpsSRIWVGGVPDELRVPQL 1469
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDG---------ERVVESGSPGGSALLNLD--GPLYLGGLPEDLKSPGL 135
|
|
| COG1340 super family |
cl34231 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
820-1165 |
1.32e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
The actual alignment was detected with superfamily member COG1340:
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.69 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 820 DSMKRNSTRLNKRLNKISNRADDFRD--NAVIKTLDRSIALRDDiggLRNDVRSTIEVLNNYgtgdhhiklpiaVKEADE 897
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEkrDELNEELKELAEKRDE---LNAQVKELREEAQEL------------REKRDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 898 LLADIKfKYGQSKpnpevlecslrqhdhwNNVSEVVKRQADRLDDLKFEFATLRGRMDDFDRLnrevfnnatltesftsm 977
Cdd:COG1340 69 LNEKVK-ELKEER----------------DELNEKLNELREELDELRKELAELNKAGGSIDKL----------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 978 nRRKLAELERKFQQAD-------EMVDEMQVfLDEDI--LADSAVKYEQIIDNYKQLEQNRENLKWLNDALEDTIKEFDR 1048
Cdd:COG1340 115 -RKEIERLEWRQQTEVlspeeekELVEKIKE-LEKELekAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1049 RFEElMQDVVPKAiargHQLKEEADEYQRKFKHTEDgAANALKAslAYDNIIKAIVSAQELADIAtdSAKAANIKVHplg 1128
Cdd:COG1340 193 LHEE-MIELYKEA----DELRKEADELHKEIVEAQE-KADELHE--EIIELQKELRELRKELKKL--RKKQRALKRE--- 259
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 167879687 1129 gisvAERSEhslnvssnIEKKANKELEKAR-----ELEEILI 1165
Cdd:COG1340 260 ----KEKEE--------LEEKAEEIFEKLKkgeklTTEELKL 289
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
661-699 |
2.57e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.50 E-value: 2.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167879687 661 CHVKGSEVS--------CICKPGYAGKLCERCVKGYYGFPELEDGRC 699
Cdd:pfam00053 3 CNPHGSLSDtcdpetgqCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
178-223 |
4.35e-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: 42.73 E-value: 4.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167879687 178 CEQCASPSYVCDPDTGRCMCPPNSHGHECRSCVANTWGNVFQR-GCQ 223
Cdd:cd00055 4 CNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1117-1322 |
2.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
:
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1117 AKAANIKVHPLGGISVAERSEhslNVSSNIE--KKANKELEKAR-ELEEiligKEKKVESLQYQLRLAgvdNNKVMEEQG 1193
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSE---QLRKALFelDKLQEELEQLReELEQ----AREELEQLEEELEQA---RSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1194 QINrgEAMKKLQGTLDQANIVSNQMKFVREEAvglnsdvyklklklaklepewdtkfgmaeENVSQSLGNILNAKKELNG 1273
Cdd:COG4372 81 ELE--ELNEQLQAAQAELAQAQEELESLQEEA-----------------------------EELQEELEELQKERQDLEQ 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167879687 1274 VEKLARTQSEKFQAWNASFSAQLQELKDKIARAKHAAEGIRVSLESQDE 1322
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2114-2271 |
1.82e-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: 118.67 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 2114 GSYFPGDAYAIYKRNFNVGKFMDVDLELRTSEVNGILMSVAD-PINGFpaFSLEISNGNVVLSIDVGDGyPIRVQSTlps 2192
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSqNGGDF--LALELEDGRLVLRYDLGSG-SLVLSSK--- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 2193 nYTLCDNRWHNVSALYEDHQIVLRVDHYPPNTLLVQSNDVLRRvaTKAPLYIGGLPDTAPSGTLLLRENFKGCIRNVVI 2271
Cdd:cd00110 75 -TPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
416-556 |
1.88e-30 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 118.14 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 416 YFQLPPQFLGDRTTSYGGLLNYTLVTVGAFQnipEASLRQFPMVQLHTHDeLVLDYYEDRIVY--DKEVNRYSARLHESL 493
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPG---GGSLNSEPDVILEGNG-LRLSYSSPDQPPpdPGQEQTYSVRLHEEN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167879687 494 WKnHYDGQHITRAILMVALQNVRHIFVRGTITTDFRQVVLTNVTLDAGifVAGAENNRAYGIE 556
Cdd:pfam00052 77 WR-DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSA--VPGGSGPPASWVE 136
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2141-2271 |
5.00e-28 |
|
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: 110.59 E-value: 5.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 2141 LRTSEVNGILMSVADPINGFpaFSLEISNGNVVLSIDVGDGypirVQSTLPSNYTLCDNRWHNVSALYEDHQIVLRVDHY 2220
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDF--LALELVNGRLVLRYDLGSG----PESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 167879687 2221 PPNTLLVQSNDVLRRvaTKAPLYIGGLPDTAPSGTLLLRENFKGCIRNVVI 2271
Cdd:pfam02210 75 TVVSSLPPGESLLLN--LNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1942-2089 |
8.75e-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: 110.97 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1942 HSIVTVAARNLWQRNFNIQFDFRTFYPNGVLFAAlGSKDKaKHFITLALRDGTLALTIR-GRKRDQLLLPVKLNDGQWHH 2020
Cdd:cd00110 7 SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYA-GSQNG-GDFLALELEDGRLVLRYDlGSGSLVLSSKTPLNDGQWHS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 2021 VSLNSVKKKATLSVHVGNSLSSAQIRLPKKLNAANNLFVGGIPDEALLPKELQPKPeeFKGCLRKFSVN 2089
Cdd:cd00110 85 VSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPG--FVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1708-1870 |
2.22e-27 |
|
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: 109.82 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1708 AGFYGNGWVEFP-SHSLRKRANFGFVFRTLEPNCSLLVSGfpSSLSSDFdskdlrgnYSVFLYEGKLNLWVDSGAGRVEL 1786
Cdd:cd00110 2 VSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAG--SQNGGDF--------LALELEDGRLVLRYDLGSGSLVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1787 ESNNTLNDGEYHVISVIKRGRTVELRIDDELQGSKGLPKAQALVNLPGEaggLFLGGVPDDpAFDSLSKTFSGLKGVIAN 1866
Cdd:cd00110 72 SSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGP---LYLGGLPED-LKSPGLPVSPGFVGCIRD 147
|
....
gi 167879687 1867 VVFN 1870
Cdd:cd00110 148 LKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2136-2274 |
1.78e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 106.65 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 2136 DVDLELRTSEVNGILMSvADPINGFPAFSLEISNGNVVLSIDVGDGyPIRVQSTlpsNYTLCDNRWHNVSALYEDHQIVL 2215
Cdd:smart00282 1 SISFSFRTTSPNGLLLY-AGSKGGGDYLALELRDGRLVLRYDLGSG-PARLTSD---PTPLNDGQWHRVAVERNGRSVTL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 2216 RVDHYPPntLLVQSNDVLRRVATKAPLYIGGLPDTAPSGTLLLRENFKGCIRNVVIRNE 2274
Cdd:smart00282 76 SVDGGNR--VSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
1958-2091 |
2.56e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 103.19 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1958 NIQFDFRTFYPNGVLFAAlGSKDKaKHFITLALRDGTLALTIRGRKRDQLLL--PVKLNDGQWHHVSLNSVKKKATLSVH 2035
Cdd:smart00282 1 SISFSFRTTSPNGLLLYA-GSKGG-GDYLALELRDGRLVLRYDLGSGPARLTsdPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 167879687 2036 VGNSLSSAQIRLPKKLNAANNLFVGGIPDEALLPKELQPKPeeFKGCLRKFSVNNN 2091
Cdd:smart00282 79 GGNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPG--FRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1519-1681 |
5.07e-23 |
|
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: 97.49 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1519 RHFNGDGYAVLQKSSSHRSNkqFSLTLSFKTLDENALIFLALDETNNRSISLTLYQGRLVFRVDYGGdSKLEINTTNRYN 1598
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTR--LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGS-GSLVLSSKTPLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1599 TGQWVVVEAARSFSKGStengiLKVDNQE--EHRGAPTKPINsgmlpNLGVNYYLGGVPPGFKSGTTKAPgadHAFLGCL 1676
Cdd:cd00110 79 DGQWHSVSVERNGRSVT-----LSVDGERvvESGSPGGSALL-----NLDGPLYLGGLPEDLKSPGLPVS---PGFVGCI 145
|
....*
gi 167879687 1677 KGVHI 1681
Cdd:cd00110 146 RDLKV 150
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1963-2091 |
5.83e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 93.25 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1963 FRTFYPNGVLFAALGSKdkaKHFITLALRDGTLALTIRGRKRDQLLL--PVKLNDGQWHHVSLNSVKKKATLSVHVGNSL 2040
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG---SDFLALELVNGRLVLRYDLGSGPESLLssGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 167879687 2041 SSAQIRLPKKLNAANNLFVGGIPDEALLPKELQPKPeeFKGCLRKFSVNNN 2091
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAG--FVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
1728-1872 |
9.96e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 90.09 E-value: 9.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1728 NFGFVFRTLEPNCSLLVSGfpSSLSSDFdskdlrgnYSVFLYEGKLNLWVDSGAGRVELES-NNTLNDGEYHVISVIKRG 1806
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAG--SKGGGDY--------LALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNG 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167879687 1807 RTVELRIDDELQGSKGLPKAQALVNLPgeaGGLFLGGVPDDPAFDSLsKTFSGLKGVIANVVFNNR 1872
Cdd:smart00282 71 RSVTLSVDGGNRVSGESPGGLTILNLD---GPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1733-1872 |
2.69e-20 |
|
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: 88.63 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1733 FRTLEPNCSLLVSGfpsSLSSDFdskdlrgnYSVFLYEGKLNLWVDSGAGRVEL-ESNNTLNDGEYHVISVIKRGRTVEL 1811
Cdd:pfam02210 1 FRTRQPNGLLLYAG---GGGSDF--------LALELVNGRLVLRYDLGSGPESLlSSGKNLNDGQWHSVRVERNGNTLTL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167879687 1812 RIDDELQGSKGLPKAQALVNLPGEaggLFLGGVPDDPAFDSLSkTFSGLKGVIANVVFNNR 1872
Cdd:pfam02210 70 SVDGQTVVSSLPPGESLLLNLNGP---LYLGGLPPLLLLPALP-VRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
1542-1684 |
3.13e-20 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 88.55 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1542 SLTLSFKTLDENALIFLALDETNNRSISLTLYQGRLVFRVDYGGDSKLEINTTNRYNTGQWVVVEAARSFSKGStengiL 1621
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVT-----L 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167879687 1622 KVDNQEEHRGapTKPINSGMLpNLGVNYYLGGVPPGFKSGTTKAPgadHAFLGCLKGVHITGV 1684
Cdd:smart00282 76 SVDGGNRVSG--ESPGGLTIL-NLDGPLYLGGLPEDLKLPPLPVT---PGFRGCIRNLKVNGK 132
|
|
| LamB |
smart00281 |
Laminin B domain; |
414-539 |
2.90e-19 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 85.78 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 414 PLYFQLPPQFLGDRTTSYGGLLNYTLVTVGAFQNIPEaslrQFPMVQLH-THDELVLDYYEDRIVYDKEVNRYsaRLHES 492
Cdd:smart00281 4 PVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHV----SAPDVILEgNGLRISHPAEGPPLPDELTTVEV--RFREE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 167879687 493 LWKnHYDGQHITRAILMVALQNVRHIFVRGTITTDFRQVVLTNVTLD 539
Cdd:smart00281 78 NWQ-YYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLE 123
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
130-175 |
1.49e-18 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 80.82 E-value: 1.49e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167879687 130 CTCDPSGSVHQECDAFSGQCYCKPGVEGPSCDRCQPGYYGFSSQGC 175
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1547-1684 |
6.77e-18 |
|
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: 81.70 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1547 FKTLDENALIFLALDETNNrSISLTLYQGRLVFRVDYGGDSKLEINTTNRYNTGQWVVVEAARSFSkgsteNGILKVDNQ 1626
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD-FLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGN-----TLTLSVDGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 167879687 1627 EEHRGAPTKPINsgmLPNLGVNYYLGGVPPgfkSGTTKAPGADHAFLGCLKGVHITGV 1684
Cdd:pfam02210 75 TVVSSLPPGESL---LLNLNGPLYLGGLPP---LLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
130-176 |
3.11e-17 |
|
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: 77.39 E-value: 3.11e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 130 CTCDPSGSVHQECDAFSGQCYCKPGVEGPSCDRCQPGYYGFSSQ--GCK 176
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
130-178 |
3.69e-17 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 77.01 E-value: 3.69e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 130 CTCDPSGSVHQECDAFSGQCYCKPGVEGPSCDRCQPGYYGFSSQGCKRC 178
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
225-273 |
7.22e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.16 E-value: 7.22e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 225 CECDIAGSIGQSCNAQTGQCNCKEGFTGRQCNECAAGYYGYPNCQRCGC 273
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
225-266 |
4.37e-15 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 71.23 E-value: 4.37e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 167879687 225 CECDIAGSIGQSCNAQTGQCNCKEGFTGRQCNECAAGYYGYP 266
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
225-266 |
1.46e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 69.65 E-value: 1.46e-14
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 167879687 225 CECDIAGSIGQSCNAQTGQCNCKEGFTGRQCNECAAGYYGYP 266
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
81-127 |
2.13e-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: 66.22 E-value: 2.13e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 81 CNCHVQGSLNRICNQQRGLCVCKPFVEGRQCNRCVAGYWNL--ESGVGC 127
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
80-127 |
9.10e-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: 64.68 E-value: 9.10e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 80 ACNCHVQGSLNRICNQQRGLCVCKPFVEGRQCNRCVAGYWNL-ESGVGC 127
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
81-127 |
6.94e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 6.94e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167879687 81 CNCHVQGSLNRICNQQRGLCVCKPFVEGRQCNRCVAGYWNlESGVGC 127
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
702-736 |
2.78e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 2.78e-11
10 20 30
....*....|....*....|....*....|....*
gi 167879687 702 CDCNREGSLSDECETKSGQCQCKPGIMGKRCDRCE 736
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCA 35
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
600-646 |
4.62e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 4.62e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167879687 600 PCDCNGR---SEECHPETGHCLnCRNNTGGDSCQNCAEGFFGNP-NYGSCE 646
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
702-736 |
9.16e-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: 58.90 E-value: 9.16e-11
10 20 30
....*....|....*....|....*....|....*
gi 167879687 702 CDCNREGSLSDECETKSGQCQCKPGIMGKRCDRCE 736
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCA 36
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
702-736 |
2.55e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 57.75 E-value: 2.55e-10
10 20 30
....*....|....*....|....*....|....*
gi 167879687 702 CDCNREGSLSDECETKSGQCQCKPGIMGKRCDRCE 736
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCK 35
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
601-648 |
5.79e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 5.79e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167879687 601 CDCNGR---SEECHPETGHCLnCRNNTGGDSCQNCAEGFFGNPNyGSCEAC 648
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. |
271-323 |
1.24e-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: 1.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167879687 271 CGCDERGSIprpdgSFDCDEH-GQCLCKSMVFGRQCDQCKSATFGLAAINPDGC 323
Cdd:pfam00053 1 CDCNPHGSL-----SDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
601-645 |
1.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.03e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 167879687 601 CDCNGR---SEECHPETGHCLnCRNNTGGDSCQNCAEGFFGNpNYGSC 645
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
271-323 |
2.05e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 2.05e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167879687 271 CGCDERGSIprpdgSFDCD-EHGQCLCKSMVFGRQCDQCKSATFGlaaINPDGC 323
Cdd:smart00180 1 CDCDPGGSA-----SGTCDpDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1326-1469 |
5.90e-08 |
|
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: 53.96 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1326 SYAPVSYGPSTTNKIMLSVALSGDKPNSPLVFIQGEER-RFIAVEMVKRRIRLVWNLGDEVVVITHPTEIKprdpkyDDA 1404
Cdd:cd00110 8 SYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGgDFLALELEDGRLVLRYDLGSGSLVLSSKTPLN------DGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167879687 1405 WYFIEANRTFNLCNLNVRRmthsgvlvhSNPVTGASNPEQSKLTMGpsSRIWVGGVPDELRVPQL 1469
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDG---------ERVVESGSPGGSALLNLD--GPLYLGGLPEDLKSPGL 135
|
|
| LamG |
smart00282 |
Laminin G domain; |
1342-1469 |
1.12e-07 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 52.73 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1342 LSVALSGDKPNSPLVFIQGEER-RFIAVEMVKRRIRLVWNLGDEVVVITHPteikprDPKYDD-AWYFIEANRTFNLCNL 1419
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSD------PTPLNDgQWHRVAVERNGRSVTL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 167879687 1420 NVRrmthsgvlvHSNPVTGASNPEQSKLTMGpsSRIWVGGVPDELRVPQL 1469
Cdd:smart00282 76 SVD---------GGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPL 114
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
820-1165 |
1.32e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.69 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 820 DSMKRNSTRLNKRLNKISNRADDFRD--NAVIKTLDRSIALRDDiggLRNDVRSTIEVLNNYgtgdhhiklpiaVKEADE 897
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEkrDELNEELKELAEKRDE---LNAQVKELREEAQEL------------REKRDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 898 LLADIKfKYGQSKpnpevlecslrqhdhwNNVSEVVKRQADRLDDLKFEFATLRGRMDDFDRLnrevfnnatltesftsm 977
Cdd:COG1340 69 LNEKVK-ELKEER----------------DELNEKLNELREELDELRKELAELNKAGGSIDKL----------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 978 nRRKLAELERKFQQAD-------EMVDEMQVfLDEDI--LADSAVKYEQIIDNYKQLEQNRENLKWLNDALEDTIKEFDR 1048
Cdd:COG1340 115 -RKEIERLEWRQQTEVlspeeekELVEKIKE-LEKELekAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1049 RFEElMQDVVPKAiargHQLKEEADEYQRKFKHTEDgAANALKAslAYDNIIKAIVSAQELADIAtdSAKAANIKVHplg 1128
Cdd:COG1340 193 LHEE-MIELYKEA----DELRKEADELHKEIVEAQE-KADELHE--EIIELQKELRELRKELKKL--RKKQRALKRE--- 259
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 167879687 1129 gisvAERSEhslnvssnIEKKANKELEKAR-----ELEEILI 1165
Cdd:COG1340 260 ----KEKEE--------LEEKAEEIFEKLKkgeklTTEELKL 289
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
270-324 |
2.57e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.27 E-value: 2.57e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167879687 270 RCGCDERGSIprpdgSFDCD-EHGQCLCKSMVFGRQCDQCKSATFGLaAINPDGCT 324
Cdd:cd00055 1 PCDCNGHGSL-----SGQCDpGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
928-1078 |
8.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 928 NVSEVVKRQADRLDDLKFEFATLRGRMDDFDRLNREVFNNATLTESFTSMNRRKLAELERKFQQADEMVDEMqvfldeDI 1007
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL------ER 593
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167879687 1008 LADSAVKYEQIIDNYKQLEQNRENLKWLNDALEDTIKEFDRRFEELMQDVVPKAIARGHQLKEEADEYQRK 1078
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQ 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
981-1299 |
2.24e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 981 KLAELERKFQQADEMVDEMQVFLDEDI------LADSAVKYEQIIDNYKQLEQNRENLKwlnDALEDTIKEFDRRfEELM 1054
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVidlqtkLQEMQMERDAMADIRRRESQSQEDLR---NQLQNTVHELEAA-KCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1055 QDVVPKAIARGHQLKeeadeyqrkfkhtedgaanalKASLAYDNIIkaivsaQELADIATDSAKAANIKVHPLGGISvae 1134
Cdd:pfam15921 162 EDMLEDSNTQIEQLR---------------------KMMLSHEGVL------QEIRSILVDFEEASGKKIYEHDSMS--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1135 rSEHSLNVSSNIEKKAnKELE------KAR------ELEEILIGKEKKVESL--QYQLRLAGVDNNKVMEEQGQINRGEA 1200
Cdd:pfam15921 212 -TMHFRSLGSAISKIL-RELDteisylKGRifpvedQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1201 MKKlqgtldQANIVSNQMKFVREEAVGLNSdVYKLklklaklepewdtKFGMAEENVSQSLGNILNAKKEL-NGVEKL-- 1277
Cdd:pfam15921 290 ARS------QANSIQSQLEIIQEQARNQNS-MYMR-------------QLSDLESTVSQLRSELREAKRMYeDKIEELek 349
|
330 340 350
....*....|....*....|....*....|...
gi 167879687 1278 -----------ARTQSEKFQAWNASFSAQLQEL 1299
Cdd:pfam15921 350 qlvlanselteARTERDQFSQESGNLDDQLQKL 382
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
661-699 |
2.57e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.50 E-value: 2.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167879687 661 CHVKGSEVS--------CICKPGYAGKLCERCVKGYYGFPELEDGRC 699
Cdd:pfam00053 3 CNPHGSLSDtcdpetgqCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
647-700 |
2.59e-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: 43.50 E-value: 2.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167879687 647 ACPCPeTRKNFAKGCHVKGSEvsCICKPGYAGKLCERCVKGYYGFPELEDGrCE 700
Cdd:cd00055 1 PCDCN-GHGSLSGQCDPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
178-223 |
4.35e-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: 42.73 E-value: 4.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167879687 178 CEQCASPSYVCDPDTGRCMCPPNSHGHECRSCVANTWGNVFQR-GCQ 223
Cdd:cd00055 4 CNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
648-692 |
9.27e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 9.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 167879687 648 CPCPeTRKNFAKGCHVKGSEvsCICKPGYAGKLCERCVKGYYGFP 692
Cdd:smart00180 1 CDCD-PGGSASGTCDPDTGQ--CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1359-1491 |
2.29e-04 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 43.07 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1359 QGEERRFIAVEMVKRRIRLVWNLGDEVVVITHPTEIKprdpkyDDAWYFIEANRTfnlcnlnvrrmTHSGVL-VHSNPVT 1437
Cdd:pfam00054 15 TQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLN------DGKWHSVELERN-----------GRSGTLsVDGEARP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 167879687 1438 GASNPeQSKLTMGPSSR-IWVGGVPDELRVPQLQAAGTGLGVILSQLYVDQRQIG 1491
Cdd:pfam00054 78 TGESP-LGATTDLDVDGpLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
178-222 |
1.74e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 1.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 167879687 178 CEQCASPSYVCDPDTGRCMCPPNSHGHECRSCVANTWGNVFQrGC 222
Cdd:smart00180 3 CDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
786-1340 |
1.82e-03 |
|
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: 43.88 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 786 ELEKF-EREAEELGYavgQLLDVKDRL--VNFDNSLLDSMKrnsTRLNKRLNKISNRADDFRDNAVIKTLDR-SIALRDD 861
Cdd:TIGR00606 305 DLYHNhQRTVREKER---ELVDCQRELekLNKERRLLNQEK---TELLVEQGRLQLQADRHQEHIRARDSLIqSLATRLE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 862 IGGLRNDVRSTIEVlnnygtgDHHIKLPI-----AVKEADELLADIKFKYGQSKPNPEVLECSLRQHDH-WNNVSEVVKR 935
Cdd:TIGR00606 379 LDGFERGPFSERQI-------KNFHTLVIerqedEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtIELKKEILEK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 936 QADRLDDLKFEFATLRGRMDDFDRLNREVFN---NATLTESFTSMNRRKLAELERKFQQADemVDEMQVFLDED------ 1006
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKaerELSKAEKNSLTETLKKEVKSLQNEKAD--LDRKLRKLDQEmeqlnh 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1007 ----------ILADSAVKYEQIIDNYKQ-------LEQNRENLKWLNDALEDTIKEFDRRFEELMQdvVPKAIARGHQLK 1069
Cdd:TIGR00606 530 htttrtqmemLTKDKMDKDEQIRKIKSRhsdeltsLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK--LNKELASLEQNK 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1070 eeaDEYQRKFKHTEdgaANALKASlayDNIIKAIVSAQELADIAT--DSAKAANIKVHPLGGISVAERS--EHSLNVSSN 1145
Cdd:TIGR00606 608 ---NHINNELESKE---EQLSSYE---DKLFDVCGSQDEESDLERlkEEIEKSSKQRAMLAGATAVYSQfiTQLTDENQS 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1146 IEKKANKELEKARELEEIligkekkVESLQYQLRLAGvDNNKVME---EQGQINRGEAMKKLQGTLDQANIVSNQMKFVR 1222
Cdd:TIGR00606 679 CCPVCQRVFQTEAELQEF-------ISDLQSKLRLAP-DKLKSTEselKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1223 EEAVGLNSDVYKLKLKLAKLEPEWDTKfgMAEENVSQSL----GNILNAKKELNGVEKLARTQSEKFQAWNASFSaqLQE 1298
Cdd:TIGR00606 751 NKLQKVNRDIQRLKNDIEEQETLLGTI--MPEEESAKVCltdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRT--VQQ 826
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 167879687 1299 LKDKIARAKHAAEGIRVSLESQDECMRSY-APVSYGPSTTNKI 1340
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIELNRKLIQDQqEQIQHLKSKTNEL 869
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1117-1322 |
2.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1117 AKAANIKVHPLGGISVAERSEhslNVSSNIE--KKANKELEKAR-ELEEiligKEKKVESLQYQLRLAgvdNNKVMEEQG 1193
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSE---QLRKALFelDKLQEELEQLReELEQ----AREELEQLEEELEQA---RSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1194 QINrgEAMKKLQGTLDQANIVSNQMKFVREEAvglnsdvyklklklaklepewdtkfgmaeENVSQSLGNILNAKKELNG 1273
Cdd:COG4372 81 ELE--ELNEQLQAAQAELAQAQEELESLQEEA-----------------------------EELQEELEELQKERQDLEQ 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167879687 1274 VEKLARTQSEKFQAWNASFSAQLQELKDKIARAKHAAEGIRVSLESQDE 1322
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1023-1318 |
4.74e-03 |
|
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: 42.35 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1023 KQLEQNRENLKWLNDALEDTIKEFDR---------RFEELMQDVVPKAIA----RGHQLKEEADEYQRKFK---HTEDGA 1086
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSlerqaekaeRYKELKAELRELELAllvlRLEELREELEELQEELKeaeEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1087 ANALKASLA-YDNIIKAIVSAQELADIATDSAKAANIKVHPL-GGISVAERSEHSLN-----VSSNIEKKANKELEKARE 1159
Cdd:TIGR02168 259 TAELQELEEkLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLErqleeLEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1160 LEEIligkEKKVESLQyqlrlagvdNNKVMEEqgqinrgEAMKKLQGTLDQANivsNQMKFVREEAVGLNSDVYKlklkl 1239
Cdd:TIGR02168 339 LAEL----EEKLEELK---------EELESLE-------AELEELEAELEELE---SRLEELEEQLETLRSKVAQ----- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1240 aklepewdtkfgmAEENVSQSLGNILNAKKELNGVEK-LARTQSEKFQAWNASFSAQLQELKDKIARAKHAAEGIRVSLE 1318
Cdd:TIGR02168 391 -------------LELQIASLNNEIERLEARLERLEDrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2114-2271 |
1.82e-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: 118.67 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 2114 GSYFPGDAYAIYKRNFNVGKFMDVDLELRTSEVNGILMSVAD-PINGFpaFSLEISNGNVVLSIDVGDGyPIRVQSTlps 2192
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSqNGGDF--LALELEDGRLVLRYDLGSG-SLVLSSK--- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 2193 nYTLCDNRWHNVSALYEDHQIVLRVDHYPPNTLLVQSNDVLRRvaTKAPLYIGGLPDTAPSGTLLLRENFKGCIRNVVI 2271
Cdd:cd00110 75 -TPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLN--LDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
416-556 |
1.88e-30 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 118.14 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 416 YFQLPPQFLGDRTTSYGGLLNYTLVTVGAFQnipEASLRQFPMVQLHTHDeLVLDYYEDRIVY--DKEVNRYSARLHESL 493
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPG---GGSLNSEPDVILEGNG-LRLSYSSPDQPPpdPGQEQTYSVRLHEEN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167879687 494 WKnHYDGQHITRAILMVALQNVRHIFVRGTITTDFRQVVLTNVTLDAGifVAGAENNRAYGIE 556
Cdd:pfam00052 77 WR-DSDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSA--VPGGSGPPASWVE 136
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2141-2271 |
5.00e-28 |
|
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: 110.59 E-value: 5.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 2141 LRTSEVNGILMSVADPINGFpaFSLEISNGNVVLSIDVGDGypirVQSTLPSNYTLCDNRWHNVSALYEDHQIVLRVDHY 2220
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDF--LALELVNGRLVLRYDLGSG----PESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 167879687 2221 PPNTLLVQSNDVLRRvaTKAPLYIGGLPDTAPSGTLLLRENFKGCIRNVVI 2271
Cdd:pfam02210 75 TVVSSLPPGESLLLN--LNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1942-2089 |
8.75e-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: 110.97 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1942 HSIVTVAARNLWQRNFNIQFDFRTFYPNGVLFAAlGSKDKaKHFITLALRDGTLALTIR-GRKRDQLLLPVKLNDGQWHH 2020
Cdd:cd00110 7 SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYA-GSQNG-GDFLALELEDGRLVLRYDlGSGSLVLSSKTPLNDGQWHS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 2021 VSLNSVKKKATLSVHVGNSLSSAQIRLPKKLNAANNLFVGGIPDEALLPKELQPKPeeFKGCLRKFSVN 2089
Cdd:cd00110 85 VSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPG--FVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1708-1870 |
2.22e-27 |
|
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: 109.82 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1708 AGFYGNGWVEFP-SHSLRKRANFGFVFRTLEPNCSLLVSGfpSSLSSDFdskdlrgnYSVFLYEGKLNLWVDSGAGRVEL 1786
Cdd:cd00110 2 VSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAG--SQNGGDF--------LALELEDGRLVLRYDLGSGSLVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1787 ESNNTLNDGEYHVISVIKRGRTVELRIDDELQGSKGLPKAQALVNLPGEaggLFLGGVPDDpAFDSLSKTFSGLKGVIAN 1866
Cdd:cd00110 72 SSKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGP---LYLGGLPED-LKSPGLPVSPGFVGCIRD 147
|
....
gi 167879687 1867 VVFN 1870
Cdd:cd00110 148 LKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2136-2274 |
1.78e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 106.65 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 2136 DVDLELRTSEVNGILMSvADPINGFPAFSLEISNGNVVLSIDVGDGyPIRVQSTlpsNYTLCDNRWHNVSALYEDHQIVL 2215
Cdd:smart00282 1 SISFSFRTTSPNGLLLY-AGSKGGGDYLALELRDGRLVLRYDLGSG-PARLTSD---PTPLNDGQWHRVAVERNGRSVTL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 2216 RVDHYPPntLLVQSNDVLRRVATKAPLYIGGLPDTAPSGTLLLRENFKGCIRNVVIRNE 2274
Cdd:smart00282 76 SVDGGNR--VSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
1958-2091 |
2.56e-25 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 103.19 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1958 NIQFDFRTFYPNGVLFAAlGSKDKaKHFITLALRDGTLALTIRGRKRDQLLL--PVKLNDGQWHHVSLNSVKKKATLSVH 2035
Cdd:smart00282 1 SISFSFRTTSPNGLLLYA-GSKGG-GDYLALELRDGRLVLRYDLGSGPARLTsdPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 167879687 2036 VGNSLSSAQIRLPKKLNAANNLFVGGIPDEALLPKELQPKPeeFKGCLRKFSVNNN 2091
Cdd:smart00282 79 GGNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPG--FRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1519-1681 |
5.07e-23 |
|
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: 97.49 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1519 RHFNGDGYAVLQKSSSHRSNkqFSLTLSFKTLDENALIFLALDETNNRSISLTLYQGRLVFRVDYGGdSKLEINTTNRYN 1598
Cdd:cd00110 2 VSFSGSSYVRLPTLPAPRTR--LSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGS-GSLVLSSKTPLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1599 TGQWVVVEAARSFSKGStengiLKVDNQE--EHRGAPTKPINsgmlpNLGVNYYLGGVPPGFKSGTTKAPgadHAFLGCL 1676
Cdd:cd00110 79 DGQWHSVSVERNGRSVT-----LSVDGERvvESGSPGGSALL-----NLDGPLYLGGLPEDLKSPGLPVS---PGFVGCI 145
|
....*
gi 167879687 1677 KGVHI 1681
Cdd:cd00110 146 RDLKV 150
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1963-2091 |
5.83e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 93.25 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1963 FRTFYPNGVLFAALGSKdkaKHFITLALRDGTLALTIRGRKRDQLLL--PVKLNDGQWHHVSLNSVKKKATLSVHVGNSL 2040
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG---SDFLALELVNGRLVLRYDLGSGPESLLssGKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 167879687 2041 SSAQIRLPKKLNAANNLFVGGIPDEALLPKELQPKPeeFKGCLRKFSVNNN 2091
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAG--FVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
1728-1872 |
9.96e-21 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 90.09 E-value: 9.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1728 NFGFVFRTLEPNCSLLVSGfpSSLSSDFdskdlrgnYSVFLYEGKLNLWVDSGAGRVELES-NNTLNDGEYHVISVIKRG 1806
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAG--SKGGGDY--------LALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNG 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167879687 1807 RTVELRIDDELQGSKGLPKAQALVNLPgeaGGLFLGGVPDDPAFDSLsKTFSGLKGVIANVVFNNR 1872
Cdd:smart00282 71 RSVTLSVDGGNRVSGESPGGLTILNLD---GPLYLGGLPEDLKLPPL-PVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1733-1872 |
2.69e-20 |
|
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: 88.63 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1733 FRTLEPNCSLLVSGfpsSLSSDFdskdlrgnYSVFLYEGKLNLWVDSGAGRVEL-ESNNTLNDGEYHVISVIKRGRTVEL 1811
Cdd:pfam02210 1 FRTRQPNGLLLYAG---GGGSDF--------LALELVNGRLVLRYDLGSGPESLlSSGKNLNDGQWHSVRVERNGNTLTL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167879687 1812 RIDDELQGSKGLPKAQALVNLPGEaggLFLGGVPDDPAFDSLSkTFSGLKGVIANVVFNNR 1872
Cdd:pfam02210 70 SVDGQTVVSSLPPGESLLLNLNGP---LYLGGLPPLLLLPALP-VRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
1542-1684 |
3.13e-20 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 88.55 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1542 SLTLSFKTLDENALIFLALDETNNRSISLTLYQGRLVFRVDYGGDSKLEINTTNRYNTGQWVVVEAARSFSKGStengiL 1621
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVT-----L 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167879687 1622 KVDNQEEHRGapTKPINSGMLpNLGVNYYLGGVPPGFKSGTTKAPgadHAFLGCLKGVHITGV 1684
Cdd:smart00282 76 SVDGGNRVSG--ESPGGLTIL-NLDGPLYLGGLPEDLKLPPLPVT---PGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1963-2094 |
5.74e-20 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 87.76 E-value: 5.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1963 FRTFYPNGVLFaaLGSKDKAKHFITLALRDGTLALTIR-GRKRDQLLLPVKLNDGQWHHVSLNSVKKKATLSV-----HV 2036
Cdd:pfam00054 1 FRTTEPSGLLL--YNGTQTERDFLALELRDGRLEVSYDlGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVdgearPT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 2037 GNSLSSAQIrlpkKLNAANNLFVGGIPDEA--LLPKELQPKpeeFKGCLRKFSVNNNTQD 2094
Cdd:pfam00054 79 GESPLGATT----DLDVDGPLYVGGLPSLGvkKRRLAISPS---FDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
414-539 |
2.90e-19 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 85.78 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 414 PLYFQLPPQFLGDRTTSYGGLLNYTLVTVGAFQNIPEaslrQFPMVQLH-THDELVLDYYEDRIVYDKEVNRYsaRLHES 492
Cdd:smart00281 4 PVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHV----SAPDVILEgNGLRISHPAEGPPLPDELTTVEV--RFREE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 167879687 493 LWKnHYDGQHITRAILMVALQNVRHIFVRGTITTDFRQVVLTNVTLD 539
Cdd:smart00281 78 NWQ-YYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLE 123
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
130-175 |
1.49e-18 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 80.82 E-value: 1.49e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167879687 130 CTCDPSGSVHQECDAFSGQCYCKPGVEGPSCDRCQPGYYGFSSQGC 175
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1547-1684 |
6.77e-18 |
|
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: 81.70 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1547 FKTLDENALIFLALDETNNrSISLTLYQGRLVFRVDYGGDSKLEINTTNRYNTGQWVVVEAARSFSkgsteNGILKVDNQ 1626
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD-FLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGN-----TLTLSVDGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 167879687 1627 EEHRGAPTKPINsgmLPNLGVNYYLGGVPPgfkSGTTKAPGADHAFLGCLKGVHITGV 1684
Cdd:pfam02210 75 TVVSSLPPGESL---LLNLNGPLYLGGLPP---LLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
130-176 |
3.11e-17 |
|
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: 77.39 E-value: 3.11e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 130 CTCDPSGSVHQECDAFSGQCYCKPGVEGPSCDRCQPGYYGFSSQ--GCK 176
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
130-178 |
3.69e-17 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 77.01 E-value: 3.69e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 130 CTCDPSGSVHQECDAFSGQCYCKPGVEGPSCDRCQPGYYGFSSQGCKRC 178
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
225-273 |
7.22e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.16 E-value: 7.22e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 225 CECDIAGSIGQSCNAQTGQCNCKEGFTGRQCNECAAGYYGYPNCQRCGC 273
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2142-2273 |
3.83e-15 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 74.28 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 2142 RTSEVNGILMSVADpINGFPAFSLEISNGNVVLSIDVGDGypirvQSTLPSNYTLCDNRWHNVSALYEDHQIVLRVDHYP 2221
Cdd:pfam00054 2 RTTEPSGLLLYNGT-QTERDFLALELRDGRLEVSYDLGSG-----AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 167879687 2222 PNTlLVQSNDVLRRVATKAPLYIGGLPDtapSGTLLLREN----FKGCIRNVVIRN 2273
Cdd:pfam00054 76 RPT-GESPLGATTDLDVDGPLYVGGLPS---LGVKKRRLAispsFDGCIRDVIVNG 127
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
225-266 |
4.37e-15 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 71.23 E-value: 4.37e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 167879687 225 CECDIAGSIGQSCNAQTGQCNCKEGFTGRQCNECAAGYYGYP 266
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
225-266 |
1.46e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 69.65 E-value: 1.46e-14
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 167879687 225 CECDIAGSIGQSCNAQTGQCNCKEGFTGRQCNECAAGYYGYP 266
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
81-127 |
2.13e-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: 66.22 E-value: 2.13e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 81 CNCHVQGSLNRICNQQRGLCVCKPFVEGRQCNRCVAGYWNL--ESGVGC 127
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
80-127 |
9.10e-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: 64.68 E-value: 9.10e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167879687 80 ACNCHVQGSLNRICNQQRGLCVCKPFVEGRQCNRCVAGYWNL-ESGVGC 127
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGC 49
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1547-1687 |
1.38e-12 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 66.96 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1547 FKTLDENALIFLALDETNNRSISLTLYQGRLVFRVDYG-GDSKLEINTtnRYNTGQWVVVEAARSFSKGStengiLKVDN 1625
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGsGAAVVRSGD--KLNDGKWHSVELERNGRSGT-----LSVDG 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167879687 1626 QEEHRGapTKPINSGMLPNLGVNYYLGGVPpgfkSGTTKAPGADH--AFLGCLKGVHITGVSYD 1687
Cdd:pfam00054 74 EARPTG--ESPLGATTDLDVDGPLYVGGLP----SLGVKKRRLAIspSFDGCIRDVIVNGKPLD 131
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
81-127 |
6.94e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 6.94e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167879687 81 CNCHVQGSLNRICNQQRGLCVCKPFVEGRQCNRCVAGYWNlESGVGC 127
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
702-736 |
2.78e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 2.78e-11
10 20 30
....*....|....*....|....*....|....*
gi 167879687 702 CDCNREGSLSDECETKSGQCQCKPGIMGKRCDRCE 736
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCA 35
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
600-646 |
4.62e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 4.62e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167879687 600 PCDCNGR---SEECHPETGHCLnCRNNTGGDSCQNCAEGFFGNP-NYGSCE 646
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
702-736 |
9.16e-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: 58.90 E-value: 9.16e-11
10 20 30
....*....|....*....|....*....|....*
gi 167879687 702 CDCNREGSLSDECETKSGQCQCKPGIMGKRCDRCE 736
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCA 36
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
702-736 |
2.55e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 57.75 E-value: 2.55e-10
10 20 30
....*....|....*....|....*....|....*
gi 167879687 702 CDCNREGSLSDECETKSGQCQCKPGIMGKRCDRCE 736
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCK 35
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
601-648 |
5.79e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 5.79e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167879687 601 CDCNGR---SEECHPETGHCLnCRNNTGGDSCQNCAEGFFGNPNyGSCEAC 648
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1733-1872 |
6.34e-10 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 59.25 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1733 FRTLEPNCSLLVSGfpsslssdfdSKDLRGNYSVFLYEGKLNLWVDSGAGRVELESNNTLNDGEYHVISVIKRGRTVELR 1812
Cdd:pfam00054 1 FRTTEPSGLLLYNG----------TQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLS 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167879687 1813 IDDE--LQGSKGLPKAQALvNLPgeaGGLFLGGVPDDPAFDSLSKTFSGLKGVIANVVFNNR 1872
Cdd:pfam00054 71 VDGEarPTGESPLGATTDL-DVD---GPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGK 128
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-323 |
1.24e-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: 1.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167879687 271 CGCDERGSIprpdgSFDCDEH-GQCLCKSMVFGRQCDQCKSATFGLAAINPDGC 323
Cdd:pfam00053 1 CDCNPHGSL-----SDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
601-645 |
1.03e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.03e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 167879687 601 CDCNGR---SEECHPETGHCLnCRNNTGGDSCQNCAEGFFGNpNYGSC 645
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD-GPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
271-323 |
2.05e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 2.05e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167879687 271 CGCDERGSIprpdgSFDCD-EHGQCLCKSMVFGRQCDQCKSATFGlaaINPDGC 323
Cdd:smart00180 1 CDCDPGGSA-----SGTCDpDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1326-1469 |
5.90e-08 |
|
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: 53.96 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1326 SYAPVSYGPSTTNKIMLSVALSGDKPNSPLVFIQGEER-RFIAVEMVKRRIRLVWNLGDEVVVITHPTEIKprdpkyDDA 1404
Cdd:cd00110 8 SYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGgDFLALELEDGRLVLRYDLGSGSLVLSSKTPLN------DGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167879687 1405 WYFIEANRTFNLCNLNVRRmthsgvlvhSNPVTGASNPEQSKLTMGpsSRIWVGGVPDELRVPQL 1469
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDG---------ERVVESGSPGGSALLNLD--GPLYLGGLPEDLKSPGL 135
|
|
| LamG |
smart00282 |
Laminin G domain; |
1342-1469 |
1.12e-07 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 52.73 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1342 LSVALSGDKPNSPLVFIQGEER-RFIAVEMVKRRIRLVWNLGDEVVVITHPteikprDPKYDD-AWYFIEANRTFNLCNL 1419
Cdd:smart00282 2 ISFSFRTTSPNGLLLYAGSKGGgDYLALELRDGRLVLRYDLGSGPARLTSD------PTPLNDgQWHRVAVERNGRSVTL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 167879687 1420 NVRrmthsgvlvHSNPVTGASNPEQSKLTMGpsSRIWVGGVPDELRVPQL 1469
Cdd:smart00282 76 SVD---------GGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPL 114
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
820-1165 |
1.32e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.69 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 820 DSMKRNSTRLNKRLNKISNRADDFRD--NAVIKTLDRSIALRDDiggLRNDVRSTIEVLNNYgtgdhhiklpiaVKEADE 897
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEkrDELNEELKELAEKRDE---LNAQVKELREEAQEL------------REKRDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 898 LLADIKfKYGQSKpnpevlecslrqhdhwNNVSEVVKRQADRLDDLKFEFATLRGRMDDFDRLnrevfnnatltesftsm 977
Cdd:COG1340 69 LNEKVK-ELKEER----------------DELNEKLNELREELDELRKELAELNKAGGSIDKL----------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 978 nRRKLAELERKFQQAD-------EMVDEMQVfLDEDI--LADSAVKYEQIIDNYKQLEQNRENLKWLNDALEDTIKEFDR 1048
Cdd:COG1340 115 -RKEIERLEWRQQTEVlspeeekELVEKIKE-LEKELekAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1049 RFEElMQDVVPKAiargHQLKEEADEYQRKFKHTEDgAANALKAslAYDNIIKAIVSAQELADIAtdSAKAANIKVHplg 1128
Cdd:COG1340 193 LHEE-MIELYKEA----DELRKEADELHKEIVEAQE-KADELHE--EIIELQKELRELRKELKKL--RKKQRALKRE--- 259
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 167879687 1129 gisvAERSEhslnvssnIEKKANKELEKAR-----ELEEILI 1165
Cdd:COG1340 260 ----KEKEE--------LEEKAEEIFEKLKkgeklTTEELKL 289
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
270-324 |
2.57e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.27 E-value: 2.57e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167879687 270 RCGCDERGSIprpdgSFDCD-EHGQCLCKSMVFGRQCDQCKSATFGLaAINPDGCT 324
Cdd:cd00055 1 PCDCNGHGSL-----SGQCDpGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGCQ 50
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
955-1303 |
6.12e-06 |
|
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: 51.50 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 955 DDFDRLNREVFNNATLTESFtSMNRRKLAELERK------FQQADEMVDEMQVFLDEDILADSAvKYEQIIDNYKQLEQN 1028
Cdd:COG5185 163 DIFGKLTQELNQNLKKLEIF-GLTLGLLKGISELkkaepsGTVNSIKESETGNLGSESTLLEKA-KEIINIEEALKGFQD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1029 RENLKWLNDALEDTIKEFDRRFEELMQDVVPKAIARGHQLKEEADEYQRKFKHTEDGAANALKAS------LAYDNIIKA 1102
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIdikkatESLEEQLAA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1103 IVSAQELADI--ATDSAKAANIKVHPLGGISVAERSE------HSLNVSSNIEKK------ANKELEKARE-LEEILIGK 1167
Cdd:COG5185 321 AEAEQELEESkrETETGIQNLTAEIEQGQESLTENLEaikeeiENIVGEVELSKSseeldsFKDTIESTKEsLDEIPQNQ 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1168 EKKVESLQYQLRlagvDNNKVMEEQgqinrgeaMKKLQGTLDQANivsNQMKFVREEAVGLNSDVYKLKLKLAKLEPE-W 1246
Cdd:COG5185 401 RGYAQEILATLE----DTLKAADRQ--------IEELQRQIEQAT---SSNEEVSKLLNELISELNKVMREADEESQSrL 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 167879687 1247 DTKFGMAEENVSQSLGNIlnaKKELNGVEKLARTQSEKFQAWNASFSAQLQELKDKI 1303
Cdd:COG5185 466 EEAYDEINRSVRSKKEDL---NEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
928-1078 |
8.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 928 NVSEVVKRQADRLDDLKFEFATLRGRMDDFDRLNREVFNNATLTESFTSMNRRKLAELERKFQQADEMVDEMqvfldeDI 1007
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL------ER 593
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167879687 1008 LADSAVKYEQIIDNYKQLEQNRENLKWLNDALEDTIKEFDRRFEELMQDVVPKAIARGHQLKEEADEYQRK 1078
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQ 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
981-1299 |
2.24e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 981 KLAELERKFQQADEMVDEMQVFLDEDI------LADSAVKYEQIIDNYKQLEQNRENLKwlnDALEDTIKEFDRRfEELM 1054
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVidlqtkLQEMQMERDAMADIRRRESQSQEDLR---NQLQNTVHELEAA-KCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1055 QDVVPKAIARGHQLKeeadeyqrkfkhtedgaanalKASLAYDNIIkaivsaQELADIATDSAKAANIKVHPLGGISvae 1134
Cdd:pfam15921 162 EDMLEDSNTQIEQLR---------------------KMMLSHEGVL------QEIRSILVDFEEASGKKIYEHDSMS--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1135 rSEHSLNVSSNIEKKAnKELE------KAR------ELEEILIGKEKKVESL--QYQLRLAGVDNNKVMEEQGQINRGEA 1200
Cdd:pfam15921 212 -TMHFRSLGSAISKIL-RELDteisylKGRifpvedQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1201 MKKlqgtldQANIVSNQMKFVREEAVGLNSdVYKLklklaklepewdtKFGMAEENVSQSLGNILNAKKEL-NGVEKL-- 1277
Cdd:pfam15921 290 ARS------QANSIQSQLEIIQEQARNQNS-MYMR-------------QLSDLESTVSQLRSELREAKRMYeDKIEELek 349
|
330 340 350
....*....|....*....|....*....|...
gi 167879687 1278 -----------ARTQSEKFQAWNASFSAQLQEL 1299
Cdd:pfam15921 350 qlvlanselteARTERDQFSQESGNLDDQLQKL 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
929-1225 |
2.32e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 929 VSEVVKRQADRLDDLKFEFATLRGRMD----DFDRLNREvfnnatLTESftsmnRRKLAELERKFQQADEMVDEMQVFLD 1004
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEqareELEQLEEE------LEQA-----RSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1005 --EDILADSAVKYEQIID-------NYKQLEQNRENLKWLNDALEDTIKEFDRRFEELMQDVVpkaiarghQLKEEADEY 1075
Cdd:COG4372 98 qaQEELESLQEEAEELQEeleelqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE--------SLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1076 QRKFKHTEDGAAN-ALKASLAYDNIIKAIVSAQELADIATDSAKAANIKVHPLGGISVAERSEHSLNVSSNIEKKANKEL 1154
Cdd:COG4372 170 EQELQALSEAEAEqALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167879687 1155 EKARELEEILIGKEKKVESLQYQLRLAGVDNNKVMEEQGQINRGEAMKKLQGTLDQANIVSNQMKFVREEA 1225
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
661-699 |
2.57e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.50 E-value: 2.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167879687 661 CHVKGSEVS--------CICKPGYAGKLCERCVKGYYGFPELEDGRC 699
Cdd:pfam00053 3 CNPHGSLSDtcdpetgqCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
647-700 |
2.59e-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: 43.50 E-value: 2.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167879687 647 ACPCPeTRKNFAKGCHVKGSEvsCICKPGYAGKLCERCVKGYYGFPELEDGrCE 700
Cdd:cd00055 1 PCDCN-GHGSLSGQCDPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
916-1194 |
4.14e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 916 LECSLRQHDHWNNVSEVVKRQADRlddlkfEFATLRGRMDDFDRLNREVfnnatltesftsmnRRKLAELERKFQQADEM 995
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREK------EKERYKRDREQWERQRREL--------------ESRVAELKEELRQSREK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 996 VDEMQvfldediladsavkyeqiiDNYKQLEQNRENLKWLNDALEDTIKEFDRRFEELMQDVvpKAIARGHQLKE-EAD- 1073
Cdd:pfam07888 96 HEELE-------------------EKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDI--KTLTQRVLEREtELEr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1074 --EYQRKF---KHTEDGAANALKASLAydniikaiVSAQELADIATDSAKAANikvhplggiSVAERSEHSLNVSSNIEK 1148
Cdd:pfam07888 155 mkERAKKAgaqRKEEEAERKQLQAKLQ--------QTEEELRSLSKEFQELRN---------SLAQRDTQVLQLQDTITT 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 1149 KANK---------ELEKARE----LEEILIGKEKKVESLQYQLRLAGVDNNKVMEEQGQ 1194
Cdd:pfam07888 218 LTQKlttahrkeaENEALLEelrsLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ 276
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
178-223 |
4.35e-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: 42.73 E-value: 4.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 167879687 178 CEQCASPSYVCDPDTGRCMCPPNSHGHECRSCVANTWGNVFQR-GCQ 223
Cdd:cd00055 4 CNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
918-1211 |
6.47e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 918 CSLRQH--DHWNNVSEVVKRQADRLDDLKFEFATLRGRMDDF-DRLNREVFnnaTLTESFtsmnRRKLAELERkfqqade 994
Cdd:pfam12128 261 SHLHFGykSDETLIASRQEERQETSAELNQLLRTLDDQWKEKrDELNGELS---AADAAV----AKDRSELEA------- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 995 MVDEMQVFLDEDIlaDSAVKYEQIIDNYK-QLEQNRENLKWLNDALEDTIKEFDRRFEELMQDVVPKaIARGHQLKEEAD 1073
Cdd:pfam12128 327 LEDQHGAFLDADI--ETAAADQEQLPSWQsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRD-IAGIKDKLAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1074 EYQRKFKHTEDGAANALKASLAyDNIIKAIVSAQELADIATDSAKAANIKVHplggiSVAERSEHSLNVSSNIEkkankE 1153
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELR-EQLEAGKLEFNEEEYRLKSRLGELKLRLN-----QATATPELLLQLENFDE-----R 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 167879687 1154 LEKARELEEiliGKEKKVESLQYQLRLAGVDNNKVMEEQGQINRgeAMKKLQGTLDQA 1211
Cdd:pfam12128 473 IERAREEQE---AANAEVERLQSELRQARKRRDQASEALRQASR--RLEERQSALDEL 525
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
648-692 |
9.27e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 9.27e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 167879687 648 CPCPeTRKNFAKGCHVKGSEvsCICKPGYAGKLCERCVKGYYGFP 692
Cdd:smart00180 1 CDCD-PGGSASGTCDPDTGQ--CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
926-1191 |
9.77e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 926 WNNVSEVVKRQADRLDDLKFEFAtlrgRMDDFDRLNREvfNNATLTESFTSMN--RRKLAELERKFQQADEMVDEMQvfl 1003
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIK----RTENIEELIKE--KEKELEEVLREINeiSSELPELREELEKLEKEVKELE--- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1004 dediladsAVKyEQIIDNYKQLEQNRENLKwlndALEDTIKEFDRRFEELMQDV--VPKAIARGHQLKEEADEYQR--KF 1079
Cdd:PRK03918 235 --------ELK-EEIEELEKELESLEGSKR----KLEEKIRELEERIEELKKEIeeLEEKVKELKELKEKAEEYIKlsEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1080 KHTEDGAANALKASLA-YDNIIKAIvsAQELADIATDSAKAANIKvhplggisvAERSEhslnvssnIEKKANKELEKAR 1158
Cdd:PRK03918 302 YEEYLDELREIEKRLSrLEEEINGI--EERIKELEEKEERLEELK---------KKLKE--------LEKRLEELEERHE 362
|
250 260 270
....*....|....*....|....*....|...
gi 167879687 1159 ELEEIligKEKKVESLQYQLRLAGVDNNKVMEE 1191
Cdd:PRK03918 363 LYEEA---KAKKEELERLKKRLTGLTPEKLEKE 392
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
754-1124 |
1.00e-04 |
|
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: 47.64 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 754 TVILIDDLNELTWKLDRDTTHiDKDGIPAPWIELEKFEREAEELgYAVGQLLDVKDRLVNFDNSLLDSMKRNSTRLNKRL 833
Cdd:COG5185 203 TVNSIKESETGNLGSESTLLE-KAKEIINIEEALKGFQDPESEL-EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 834 N-KISNRADDFRDnaviktLDRSIALRDDIGGLRNDVRSTIEVLNNYGTGDHHIKLPIAV-KEADELLADIKfkygqsKP 911
Cdd:COG5185 281 NeNANNLIKQFEN------TKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETeTGIQNLTAEIE------QG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 912 NPEVLEcslRQHDHWNNVSEVVKRQADR-----LDDLKFEFATLRGRMDDFDRLNREVFNNATLTESFT-SMNRRKLAEL 985
Cdd:COG5185 349 QESLTE---NLEAIKEEIENIVGEVELSksseeLDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEEL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 986 ERKFQQADEMVDEMQVFLDEdiLADSAVKYEQIIDNYKQLEQNRENLKwLNDALEDTIKEFDRRFEEL------MQDVVP 1059
Cdd:COG5185 426 QRQIEQATSSNEEVSKLLNE--LISELNKVMREADEESQSRLEEAYDE-INRSVRSKKEDLNEELTQIesrvstLKATLE 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167879687 1060 KAIARG----HQLKEEADEYQRKFKHTEDgaanalkasLAYDNIIKAIVSAQELADIATDSAKAANIKV 1124
Cdd:COG5185 503 KLRAKLerqlEGVRSKLDQVAESLKDFMR---------ARGYAHILALENLIPASELIQASNAKTDGQA 562
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
832-1182 |
1.23e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 832 RLNKISNRADDFRDNAVIKTLDRSI--ALRDDIGGLRNDVRSTIEvlnnygtgDHHIKLPIAVKEADELLADIKFKYGQS 909
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAveARREELEDRDEELRDRLE--------ECRVAAQAHNEEAESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 910 KPNPE---VLECSLRqhdhwnNVSEVVKRQADRLDDLKFEFATLRGRMDD--FDRLNREVFNNATLTESftSMNRRKLAE 984
Cdd:PRK02224 359 EELREeaaELESELE------EAREAVEDRREEIEELEEEIEELRERFGDapVDLGNAEDFLEELREER--DELREREAE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 985 LERKFQQADEMVDEMQVFLDE----------------DILADSAVKYEQIIDNYKQLEQNRENLKWLNDALEDtIKEFDR 1048
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAED 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1049 RFEELMQ--DVVPKAIA-----------RGHQLKEEADEYQRKFKHTEDGAANALKASLAYDNIIKAIVSAQE------- 1108
Cdd:PRK02224 510 RIERLEErrEDLEELIAerretieekreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAelkerie 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1109 -LADIATDSAKAANIKvHPLGgiSVAERSEHsLNVSSNIEKKANKEL-EKARELEEILIG------KEKKVESLQYQLRL 1180
Cdd:PRK02224 590 sLERIRTLLAAIADAE-DEIE--RLREKREA-LAELNDERRERLAEKrERKRELEAEFDEarieeaREDKERAEEYLEQV 665
|
..
gi 167879687 1181 AG 1182
Cdd:PRK02224 666 EE 667
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1359-1491 |
2.29e-04 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 43.07 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1359 QGEERRFIAVEMVKRRIRLVWNLGDEVVVITHPTEIKprdpkyDDAWYFIEANRTfnlcnlnvrrmTHSGVL-VHSNPVT 1437
Cdd:pfam00054 15 TQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLN------DGKWHSVELERN-----------GRSGTLsVDGEARP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 167879687 1438 GASNPeQSKLTMGPSSR-IWVGGVPDELRVPQLQAAGTGLGVILSQLYVDQRQIG 1491
Cdd:pfam00054 78 TGESP-LGATTDLDVDGpLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
990-1171 |
3.40e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 990 QQADEMVDEMQVFLDEDI--LADSAVKYEQIIDNYKQLEQNRENLKwlnDALEDTIKEFDRRFEELMQDV---VPKAIAr 1064
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIasLEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQEEEDKLLEEAekeAQQAIK- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1065 ghQLKEEADEYQRKFKHTEDGAANALKASLAYDnIIKAIVSAQELADIATDSAKAAN--------IKVHPLG--GISVAE 1134
Cdd:PRK00409 581 --EAKKEADEIIKELRQLQKGGYASVKAHELIE-ARKRLNKANEKKEKKKKKQKEKQeelkvgdeVKYLSLGqkGEVLSI 657
|
170 180 190
....*....|....*....|....*....|....*....
gi 167879687 1135 RSEHSLNVSSNIEK-KAN-KELEKARELEEILIGKEKKV 1171
Cdd:PRK00409 658 PDDKEAIVQAGIMKmKVPlSDLEKIQKPKKKKKKKPKTV 696
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1350-1471 |
3.43e-04 |
|
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: 42.41 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1350 KPNSPLVFIQGEERRFIAVEMVKRRIRLVWNLGDEVVVITHPTEikprdpKYDD-AWYFIEANRTFNLCNLNVrrmthSG 1428
Cdd:pfam02210 5 QPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK------NLNDgQWHSVRVERNGNTLTLSV-----DG 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 167879687 1429 VLVHSnpvtgaSNPEQSKLTMGPSSRIWVGGVPDELRVPQLQA 1471
Cdd:pfam02210 74 QTVVS------SLPPGESLLLNLNGPLYLGGLPPLLLLPALPV 110
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
1014-1080 |
4.13e-04 |
|
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 41.11 E-value: 4.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167879687 1014 KYEQIIDNYKQLEQNRENLKWLNDALEDTIKEFDRRFEELMQDvvpkaiarGHQLKEEADEYQRKFK 1080
Cdd:COG3074 12 KVQQAVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSE--------NEQLKTENAEWQERIR 70
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
928-1165 |
4.59e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 44.62 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 928 NVSEVVKRQADRLDDL-KFEFATLRGRMDDFDRLNREVFNNATLTESFTSMNRrklaELERKFQQADEMVDEMQVFLDED 1006
Cdd:PRK06669 7 KRSNVINKEKLKTHEIqKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKE----IIEEAEEDAFEIVEAAEEEAKEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1007 ILadsavkyeQIIDnykQLEQNRENLkwlNDALEDTIKEFDRRFEELMQDVVPKAIARGHQL-KEEADEYQRKFKhtedG 1085
Cdd:PRK06669 83 LL--------KKTD---EASSIIEKL---QMQIEREQEEWEEELERLIEEAKAEGYEEGYEKgREEGLEEVRELI----E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1086 AANALKASL--AYDNIIKAivSAQELADIATDSAKaaniKVhplggisVAERSEHSLNVSSNIEKKANKELekaRELEEI 1163
Cdd:PRK06669 145 QLNKIIEKLikKREEILES--SEEEIVELALDIAK----KV-------IKEISENSKEIALALVKELLKEV---KDATDI 208
|
..
gi 167879687 1164 LI 1165
Cdd:PRK06669 209 TI 210
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
1015-1180 |
6.29e-04 |
|
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge
Pssm-ID: 405864 [Multi-domain] Cd Length: 183 Bit Score: 43.15 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1015 YEQIIDnykQLEQNRENLKWLNDALEDtikefdrrfeelmqdvvpkaiaRGHQLKEEADEYQRKFKHTEDGAANALKAS- 1093
Cdd:pfam15272 6 YLELLD---KLDKNNRALHLLNKDVRE----------------------RDEHYQLQETSYKKKYLQTRNELINELKQSk 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1094 LAYDNIIKAIVSAQELADIATDS----AKAANIKVHPLGGISVAERSEHSLN---VSSNIekkANKELEKARELEEILIg 1166
Cdd:pfam15272 61 KLYDNYYKLYSKYQQLKKISNESldlqSTITNLESQLVDQAIDKDREIHNLNekiLSLEL---RNQELETKREIDKMKY- 136
|
170
....*....|....
gi 167879687 1167 kEKKVESLQYQLRL 1180
Cdd:pfam15272 137 -ESRIDELERQLKE 149
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
934-1084 |
8.84e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 934 KRQADRLDDLKFEFATLRGRMDDFDRLNREVfnnATLtesftsmnRRKLAELERKFQQADEMVDEMQVFLD--------- 1004
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEEL---EEL--------EEELEELEAELEELREELEKLEKLLQllplyqele 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1005 --EDILADSAVKYEQIIDNYKQLEQNRENLkwlnDALEDTIKEFDRRFEELMQDVVPKAIARGHQLKEEADEYQRKFKHT 1082
Cdd:COG4717 136 alEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
..
gi 167879687 1083 ED 1084
Cdd:COG4717 212 EE 213
|
|
| TNFRSF1B_teleost |
cd15835 |
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B) in teleost; also known as ... |
160-272 |
1.22e-03 |
|
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B) in teleost; also known as TNFR2; This subfamily of TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) is found in teleosts. It binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism). Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kB in endothelial cells. In goldfish (Carassius aurutus L.), TNFRSF1B expression is substantially higher than that of TNFRSF1 in tissues and various immune cell types. Both receptors are most robustly expressed in monocytes; mRNA levels of TNFRSF1B are lowest in peripheral blood leukocytes.
Pssm-ID: 276931 [Multi-domain] Cd Length: 130 Bit Score: 41.27 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 160 CDRCQPGYygfssqgcKRCEQCASPS-YVCDPdtgrcmCPPNSHghecrscvANTWgNVFQR--GCQNCECDIAGSIGQS 236
Cdd:cd15835 21 CSKCRPGT--------RLKTKCSETSdTVCEP------CPSGQY--------SENW-NYYPNcfSCPKCKERKGLQYAQN 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 167879687 237 CNAQT-GQCNCKEGFTgrqcneCAAGYYGyPNCQRCG 272
Cdd:cd15835 78 CSSTTnAVCVCKPGMY------CIMGFDH-PSCSECK 107
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
178-222 |
1.74e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 1.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 167879687 178 CEQCASPSYVCDPDTGRCMCPPNSHGHECRSCVANTWGNVFQrGC 222
Cdd:smart00180 3 CDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
786-1340 |
1.82e-03 |
|
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: 43.88 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 786 ELEKF-EREAEELGYavgQLLDVKDRL--VNFDNSLLDSMKrnsTRLNKRLNKISNRADDFRDNAVIKTLDR-SIALRDD 861
Cdd:TIGR00606 305 DLYHNhQRTVREKER---ELVDCQRELekLNKERRLLNQEK---TELLVEQGRLQLQADRHQEHIRARDSLIqSLATRLE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 862 IGGLRNDVRSTIEVlnnygtgDHHIKLPI-----AVKEADELLADIKFKYGQSKPNPEVLECSLRQHDH-WNNVSEVVKR 935
Cdd:TIGR00606 379 LDGFERGPFSERQI-------KNFHTLVIerqedEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtIELKKEILEK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 936 QADRLDDLKFEFATLRGRMDDFDRLNREVFN---NATLTESFTSMNRRKLAELERKFQQADemVDEMQVFLDED------ 1006
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKaerELSKAEKNSLTETLKKEVKSLQNEKAD--LDRKLRKLDQEmeqlnh 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1007 ----------ILADSAVKYEQIIDNYKQ-------LEQNRENLKWLNDALEDTIKEFDRRFEELMQdvVPKAIARGHQLK 1069
Cdd:TIGR00606 530 htttrtqmemLTKDKMDKDEQIRKIKSRhsdeltsLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK--LNKELASLEQNK 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1070 eeaDEYQRKFKHTEdgaANALKASlayDNIIKAIVSAQELADIAT--DSAKAANIKVHPLGGISVAERS--EHSLNVSSN 1145
Cdd:TIGR00606 608 ---NHINNELESKE---EQLSSYE---DKLFDVCGSQDEESDLERlkEEIEKSSKQRAMLAGATAVYSQfiTQLTDENQS 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1146 IEKKANKELEKARELEEIligkekkVESLQYQLRLAGvDNNKVME---EQGQINRGEAMKKLQGTLDQANIVSNQMKFVR 1222
Cdd:TIGR00606 679 CCPVCQRVFQTEAELQEF-------ISDLQSKLRLAP-DKLKSTEselKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1223 EEAVGLNSDVYKLKLKLAKLEPEWDTKfgMAEENVSQSL----GNILNAKKELNGVEKLARTQSEKFQAWNASFSaqLQE 1298
Cdd:TIGR00606 751 NKLQKVNRDIQRLKNDIEEQETLLGTI--MPEEESAKVCltdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRT--VQQ 826
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 167879687 1299 LKDKIARAKHAAEGIRVSLESQDECMRSY-APVSYGPSTTNKI 1340
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIELNRKLIQDQqEQIQHLKSKTNEL 869
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1117-1322 |
2.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1117 AKAANIKVHPLGGISVAERSEhslNVSSNIE--KKANKELEKAR-ELEEiligKEKKVESLQYQLRLAgvdNNKVMEEQG 1193
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSE---QLRKALFelDKLQEELEQLReELEQ----AREELEQLEEELEQA---RSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1194 QINrgEAMKKLQGTLDQANIVSNQMKFVREEAvglnsdvyklklklaklepewdtkfgmaeENVSQSLGNILNAKKELNG 1273
Cdd:COG4372 81 ELE--ELNEQLQAAQAELAQAQEELESLQEEA-----------------------------EELQEELEELQKERQDLEQ 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167879687 1274 VEKLARTQSEKFQAWNASFSAQLQELKDKIARAKHAAEGIRVSLESQDE 1322
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
150-209 |
2.61e-03 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 40.46 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 150 YCKPG---------VEGPSCDRCQPGYYG--FSSQGCKRCEQC-----ASPSYVCDPDTGR-CMCPPNS-------HGHE 205
Cdd:cd13406 17 ECPPGegmesrctgTQDTVCSPCEPGFYNeaVNYEPCKPCTQCnqrsgSEEKQKCTKTSDTvCRCRPGTqpldsykPGVD 96
|
....
gi 167879687 206 CRSC 209
Cdd:cd13406 97 CVPC 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1023-1318 |
4.74e-03 |
|
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: 42.35 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1023 KQLEQNRENLKWLNDALEDTIKEFDR---------RFEELMQDVVPKAIA----RGHQLKEEADEYQRKFK---HTEDGA 1086
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSlerqaekaeRYKELKAELRELELAllvlRLEELREELEELQEELKeaeEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1087 ANALKASLA-YDNIIKAIVSAQELADIATDSAKAANIKVHPL-GGISVAERSEHSLN-----VSSNIEKKANKELEKARE 1159
Cdd:TIGR02168 259 TAELQELEEkLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLErqleeLEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1160 LEEIligkEKKVESLQyqlrlagvdNNKVMEEqgqinrgEAMKKLQGTLDQANivsNQMKFVREEAVGLNSDVYKlklkl 1239
Cdd:TIGR02168 339 LAEL----EEKLEELK---------EELESLE-------AELEELEAELEELE---SRLEELEEQLETLRSKVAQ----- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 1240 aklepewdtkfgmAEENVSQSLGNILNAKKELNGVEK-LARTQSEKFQAWNASFSAQLQELKDKIARAKHAAEGIRVSLE 1318
Cdd:TIGR02168 391 -------------LELQIASLNNEIERLEARLERLEDrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
|
| TNFRSF1A_teleost |
cd15834 |
Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) in teleosts; also known as ... |
623-755 |
6.33e-03 |
|
Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) in teleosts; also known as TNFR1; This subfamily of TNFRSF1 ((also known as type I TNFR, TNFR1, DR1, TNFRSF1A, CD120a, p55) is found in teleosts. It binds TNF-alpha, through the death domain (DD), and activates NF-kappaB, mediates apoptosis and activates signaling pathways controlling inflammatory, immune, and stress responses. It mediates signal transduction by interacting with antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRAF2 and TRADD that play regulatory roles. The human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS), or periodic fever syndrome, is associated with germline mutations of the extracellular domains of this receptor, possibly due to impaired receptor clearance. Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are also associated with cognitive impairment and dementia. Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kappaB in endothelial cells. Thus, this apoptotic pathway seems to be evolutionarily conserved, as TNFalpha promotes apoptosis of human endothelial cells and triggers caspase-2 and P53 activation in these cells via TNFRSF1A.
Pssm-ID: 276930 [Multi-domain] Cd Length: 150 Bit Score: 39.40 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167879687 623 NTGGDSCQNCAEGF-----FGNPNYGS-CEACPCPETRK--NFAKGC------HVKGSEVSCICKPgYAGKLCeRCVKGY 688
Cdd:cd15834 8 SENGICCNKCHPGYklkeeCTAPGERSqCTPCPEGTYLEqiNYSPNCrrctlcKVKNEEEVSPCKK-SSNTVC-RCKKGY 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167879687 689 Y----GFPELEDGRCEYCDCNREGSLSDECETKSgQCQCKPGimgkrcdrceqpkHIVQGYKCKPCDNCTV 755
Cdd:cd15834 86 YksriDSETRECLKCKTCGPGEIEIQPCTPESNT-VCECKDN-------------YYRNNNKCKPCQKCSL 142
|
|
| |
