|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
32-266 |
9.16e-106 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 337.25 E-value: 9.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 32 CYPATGNLLIGRAInlTTSSTCGLDGPEPYCIVSHLKDSEKCFICDSENPYDanyhrdSHRVENVIYPMDSTGElTWWQA 111
Cdd:pfam00055 1 CYPAFGNLAFGREV--SATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNE-TWWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 112 VNGE---ENVSVRLNLEAEFHFTHLIMKFKTFRPAAMIIERSSDFGRTWRIYRYFAYNCTKTFPRVPAHSLRF-IDEVIC 187
Cdd:pfam00055 72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIkDDEVIC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 188 EERYSDIEPSTDGEVIYKVL--DPAIHVKDpYSLDIQDLLRITNLRINFTKLHTLGDNLLDrRPDVLQKYYYALYELVVR 265
Cdd:pfam00055 152 TSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLD-DPSVLRKYYYAISDISVG 229
|
.
gi 528517788 266 G 266
Cdd:pfam00055 230 G 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
26-266 |
4.58e-83 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 272.70 E-value: 4.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 26 GCMDGSCYPATGNLLIGRAInlTTSSTCGLDGPEPYCI-VSHLKDSEKCFICDSENPYDanyhrdSHRVENVIYPmDSTG 104
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREV--TATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDG-NNPN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 105 ELTWWQA---VNGEENVSVRLNLEAEFHFTHLIMKFKTFRPAAMIIERSsDFGRTWRIYRYFAYNCTKTFPRVPAHSLR- 180
Cdd:smart00136 72 NPTWWQSeplSNGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITk 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 181 -FIDEVICEERYSDIEPSTDGEVIYKVLDPAIHVKD-PYSLDIQDLLRITNLRINFTKLHTLGDNLLDRRPDVLQKYYYA 258
Cdd:smart00136 151 gNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 528517788 259 LYELVVRG 266
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1766-1835 |
9.10e-29 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 110.45 E-value: 9.10e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1766 NQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
816-861 |
1.66e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 69.26 E-value: 1.66e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517788 816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGFGPYGC 861
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1492-1818 |
3.37e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.14 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1492 DNADEVHKNLTAVSEELQT----MAKKLRDIATLTQT---VKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEE 1564
Cdd:TIGR04523 96 DKINKLNSDLSKINSEIKNdkeqKNKLEVELNKLEKQkkeNKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1565 GADPESIEKVAQQVLAISLPVNR--TVIVNLVEQIKDsivnltnvegvfnHTSEQlAKVNDLLKKAQDAKTQADGVSDNI 1642
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKleLLLSNLKKKIQK-------------NKSLE-SQISELKKQNNQLKDNIEKKQQEI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1643 NKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNlsngvdlLKNKTEQNreMAKEA 1722
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD-------LNNQKEQD--WNKEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1723 KAQSDNATREAEGLQEELTNAETLYKQLKEKV-----DSAGGTGEGNVNQKAIEMKK-EAEDLLKKATMGMETLKKLERK 1796
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQIsqlkkELTNSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQ 392
|
330 340
....*....|....*....|..
gi 528517788 1797 FNKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQI 414
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
816-861 |
5.29e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.76 E-value: 5.29e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517788 816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGFG---PYGC 861
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdpPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
864-912 |
8.29e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.38 E-value: 8.29e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517788 864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFPNCRQCQC 912
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
816-862 |
1.22e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.61 E-value: 1.22e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517788 816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGF--GPYGCT 862
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
864-905 |
1.16e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.91 E-value: 1.16e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517788 864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFP 905
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1493-1828 |
1.12e-11 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 70.63 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1493 NADEVHKNLTAVSEELQTMAKKLRDIA------------TLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDF 1560
Cdd:PTZ00440 1259 IKLQVFSYLQQVIKENNKMENALHEIKnmyeflisidseKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQA 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1561 ----------LNEEGADPE--SIEKVAQQVLAIslpvnRTVIVNLVEQIKDsivNLTNVEGVFNHTSEQLAKVNDLLKKA 1628
Cdd:PTZ00440 1339 kehknkiygsLEDKQIDDEikKIEQIKEEISNK-----RKEINKYLSNIKS---NKEKCDLHVRNASRGKDKIDFLNKHE 1410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1629 QDAKTQA-----DGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNI-----TAMVDDKLLNLDNNLTDVMMRl 1698
Cdd:PTZ00440 1411 AIEPSNSkevniIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNIlnnssILGKKTKLEKKKKEATNIMDD- 1489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1699 VNLSNGVdlLKNKTEQNREMAKEAKAQSdNATREaeglQEELTNAETlyKQLKEKVDSAGGTGEGNVnQKAIEMKKEAED 1778
Cdd:PTZ00440 1490 INGEHSI--IKTKLTKSSEKLNQLNEQP-NIKRE----GDVLNNDKS--TIAYETIQYNLGRVKHNL-LNILNIKDEIET 1559
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 528517788 1779 LLKKATMGMETLKKLERKF-NKNEQKMQQQRDELTDLEKNVTGIREYIRSK 1828
Cdd:PTZ00440 1560 ILNKAQDLMRDISKISKIVeNKNLENLNDKEADYVKYLDNILKEKQLMEAE 1610
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
395-452 |
1.43e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 1.43e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517788 395 CDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGLSLDDPLGC 452
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
864-905 |
1.74e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 1.74e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517788 864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFP 905
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1175-1215 |
1.89e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 1.89e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 528517788 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTGN 1215
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1506-1819 |
4.44e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 68.46 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1506 EELQTMAKKLRDIATLTQTVKT---QAKETLDKAQNKKDMFEKSNKML----KNFIQKIKDFLNEEGADPESIEKVAQQV 1578
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKlkeQAKKALEYYQLKEKLELEEEYLLyldyLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1579 LAISLPVNRTVIVNLVE-----------------QIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDN 1641
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEeekekklqeeelkllakEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1642 INKTKEALETSQNAIKKAEEEMStalknlkniqnitamvdDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKE 1721
Cdd:pfam02463 340 LEKELKELEIKREAEEEEEEELE-----------------KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1722 AKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNE 1801
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330
....*....|....*...
gi 528517788 1802 QKMQQQRDELTDLEKNVT 1819
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQ 500
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1175-1223 |
1.47e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 1.47e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517788 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTGNFPKCVPCH 1223
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1175-1219 |
2.66e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 2.66e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517788 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTG-NFPKC 1219
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
454-505 |
4.47e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 4.47e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 528517788 454 PCNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSHDLAGCR 505
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
394-453 |
1.18e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.44 E-value: 1.18e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 394 PCDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGLSLdDPLGCQ 453
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
455-504 |
2.64e-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: 54.28 E-value: 2.64e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 528517788 455 CNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSHDLA-GC 504
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPqGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1126-1168 |
7.87e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.13 E-value: 7.87e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 528517788 1126 PCGCVQPNALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDP 1168
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1122-1175 |
1.10e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528517788 1122 CGCEPCGcvqpnALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDPRVQCEEC 1175
Cdd:pfam00053 1 CDCNPHG-----SLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1489-1795 |
2.10e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.61 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDK-----------AQNKKDMFEKSNKmLKNFIQKI 1557
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKrdelnekvkelKEERDELNEKLNE-LREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1558 KDFLNEEGADPESIEKV---------AQQVLAISLPVNRtvivNLVEQIKdsivnltnvegvfnhtseQLAKvndLLKKA 1628
Cdd:COG1340 98 RKELAELNKAGGSIDKLrkeierlewRQQTEVLSPEEEK----ELVEKIK------------------ELEK---ELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1629 QDAKTQADGVSDNINKTKEaletsqnaIKKAEEEMSTALKNLKN-IQNITAmvddkllnldnnltdvmmRLVNLSNGVDL 1707
Cdd:COG1340 153 KKALEKNEKLKELRAELKE--------LRKEAEEIHKKIKELAEeAQELHE------------------EMIELYKEADE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1708 LKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKvdsaggtgegnvnQKAIEMKKEAEDLLKKATMGM 1787
Cdd:COG1340 207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK-------------QRALKREKEKEELEEKAEEIF 273
|
....*...
gi 528517788 1788 ETLKKLER 1795
Cdd:COG1340 274 EKLKKGEK 281
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1127-1172 |
2.24e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 2.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517788 1127 CGCVQPNALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDPRVQC 1172
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
395-452 |
2.55e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 2.55e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517788 395 CDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGlslDDPLGC 452
Cdd:smart00180 1 CDCDPGGSA-SGTCDPDT--------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
910-954 |
2.62e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 2.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 528517788 910 CQCNSHA---ESCDPESGACyDCRDNTAGQLCERCVDGYYGNPALGSG 954
Cdd:cd00055 2 CDCNGHGslsGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
910-957 |
2.69e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 2.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 528517788 910 CQCNSHA---ESCDPESGACyDCRDNTAGQLCERCVDGYYGNPAlGSGEHC 957
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
455-498 |
8.09e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 8.09e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 528517788 455 CNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLS 498
Cdd:smart00180 1 CDCDPGG--SASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
960-1016 |
1.33e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 1.33e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 960 CPCPGHPdsghSNGASCEvdyaSNQILCQCGQGYAGPRCDRCAPGYYGDPEHPGGSC 1016
Cdd:pfam00053 1 CDCNPHG----SLSDTCD----PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1089-1129 |
2.64e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.89 E-value: 2.64e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 528517788 1089 QCDKQTGQCPCKQNIIGHNCDQCATNHWNFGSDCgcePCGC 1129
Cdd:pfam00053 12 TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP---PQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1019-1063 |
3.83e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 3.83e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 528517788 1019 CQCNGNIDPQDpeSCDPRTGLCLkCLYNTDGDSCSECKLGYYGNA 1063
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
506-545 |
4.82e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 4.82e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 528517788 506 PCNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
910-952 |
7.42e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.42e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517788 910 CQCN---SHAESCDPESGACyDCRDNTAGQLCERCVDGYYGNPALG 952
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
507-545 |
7.71e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.71e-07
10 20 30
....*....|....*....|....*....|....*....
gi 528517788 507 CNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
959-1014 |
8.60e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 8.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517788 959 PCPCPGHPdsghSNGASCevDYASNQilCQCGQGYAGPRCDRCAPGYYGDPEHPGG 1014
Cdd:cd00055 1 PCDCNGHG----SLSGQC--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1070-1120 |
1.42e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 1.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 528517788 1070 RCTCVTAGTLPNsctdgvcQCDKQTGQCPCKQNIIGHNCDQCATNHWNFGS 1120
Cdd:cd00055 1 PCDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1489-1648 |
1.52e-06 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 51.99 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIAT-----LTQTVKTQAKETLDKAQNK-KDMFEKSNKMLKNFIQKIKDFLN 1562
Cdd:cd22656 132 KYQDKAAKVVDKLTDFENQTEKDQTALETLEKalkdlLTDEGGAIARKEIKDLQKElEKLNEEYAAKLKAKIDELKALIA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1563 EEGADPESIEKVAQQVLAISlpvnrTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQD-------AKTQA 1635
Cdd:cd22656 212 DDEAKLAAALRLIADLTAAD-----TDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISkipaailAKLEL 286
|
170
....*....|...
gi 528517788 1636 DGVSDNINKTKEA 1648
Cdd:cd22656 287 EKAIEKWNELAEK 299
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
267-320 |
1.69e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 1.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 267 SCFCYGHAS---ECAPVpgvttrdsgmiHGRCVCKHNTVGLNCERCRDFYHDAPWRP 320
Cdd:cd00055 1 PCDCNGHGSlsgQCDPG-----------TGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1018-1069 |
2.02e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.19 E-value: 2.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 528517788 1018 PCQCNGNIDPqdPESCDPRTGLCLkCLYNTDGDSCSECKLGYYGNALI-QDCR 1069
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1071-1118 |
4.29e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 4.29e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 528517788 1071 CTCVTAGTLPNsctdgvcQCDKQTGQCPCKQNIIGHNCDQCATNHWNF 1118
Cdd:smart00180 1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
332-384 |
1.48e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.88 E-value: 1.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517788 332 CNCNGH---SNQCHFDmavylatgnvsGGVCNnCLHNTMGRNCESCKPFYYQDPEK 384
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
507-545 |
1.85e-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: 1.85e-05
10 20 30
....*....|....*....|....*....|....*....
gi 528517788 507 CNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1245-1436 |
7.50e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1245 DIIAMILEKGEVpgvsdkRILELEKKLAQAQELVRDGDREGTFNL--ISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHN 1322
Cdd:COG4372 2 DRLGEKVGKARL------SLFGLRPKTGILIAALSEQLRKALFELdkLQEELEQLREELEQAREELEQLEEELEQARSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1323 NDLKQNLTALEKELKDLNNTLHQLRRELENyltaglAEQFANVLKYYQRSLNSEQrcnasvygpqspvEQSQDTRNRtea 1402
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELES------LQEEAEELQEELEELQKER-------------QDLEQQRKQ--- 133
|
170 180 190
....*....|....*....|....*....|....
gi 528517788 1403 lLKDKKDSLLRTATANNKSLSELEGKAHEINRKV 1436
Cdd:COG4372 134 -LEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
332-382 |
7.60e-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: 41.96 E-value: 7.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528517788 332 CNCNGH---SNQCHFdmavylatgnvSGGVCNnCLHNTMGRNCESCKPFYYQDP 382
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1252-1442 |
1.06e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1252 EKGEVPGVSDkRILELEKKLA--------------QAQELVRDGDREgtFNLISQTVDDLRAEIALTDGRLMGVIRDLNV 1317
Cdd:TIGR02169 672 EPAELQRLRE-RLEGLKRELSslqselrrienrldELSQELSDASRK--IGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1318 TTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENyLTAGLAEQF-------ANVLKYYQRSLNS-----EQRCNASVYG 1385
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALND-LEARLSHSRipeiqaeLSKLEEEVSRIEArlreiEQKLNRLTLE 827
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 1386 PQSPVEQSQDTRNRTEAlLKDKKDSLLRTATANNKSLSELEGKAHEINRKVHHLSNK 1442
Cdd:TIGR02169 828 KEYLEKEIQELQEQRID-LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
960-1012 |
1.80e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 1.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 528517788 960 CPCpghpDSGHSNGASCEVDYasnqILCQCGQGYAGPRCDRCAPGYYGDPEHP 1012
Cdd:smart00180 1 CDC----DPGGSASGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
332-385 |
6.78e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 6.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 332 CNCNG---HSNQCHFDmavylatgnvsGGVCNnCLHNTMGRNCESCKPFYYQDPEKD 385
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
292-318 |
9.75e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.45 E-value: 9.75e-04
10 20
....*....|....*....|....*..
gi 528517788 292 HGRCVCKHNTVGLNCERCRDFYHDAPW 318
Cdd:smart00180 17 TGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
291-322 |
2.24e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.72 E-value: 2.24e-03
10 20 30
....*....|....*....|....*....|..
gi 528517788 291 IHGRCVCKHNTVGLNCERCRDFYHDAPWRPAE 322
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1590-1682 |
3.61e-03 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 41.12 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1590 IVNLVEQIKDSIVNL-TNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALK 1668
Cdd:smart00283 2 VSEAVEEIAAGAEEQaEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
|
90 100
....*....|....*....|.
gi 528517788 1669 NLK-------NIQNITAMVDD 1682
Cdd:smart00283 82 AVEeleessdEIGEIVSVIDD 102
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1747-1832 |
8.99e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1747 YKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKK-ATMGMETLKKLERKFNKNEQKMQQQRDELT-DLEKNVTGIREY 1824
Cdd:smart00935 16 GKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDaATLSEAAREKKEKELQKKVQEFQRKQQKLQqDLQKRQQEELQK 95
|
....*...
gi 528517788 1825 IRSKVLAY 1832
Cdd:smart00935 96 ILDKINKA 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
32-266 |
9.16e-106 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 337.25 E-value: 9.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 32 CYPATGNLLIGRAInlTTSSTCGLDGPEPYCIVSHLKDSEKCFICDSENPYDanyhrdSHRVENVIYPMDSTGElTWWQA 111
Cdd:pfam00055 1 CYPAFGNLAFGREV--SATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNE-TWWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 112 VNGE---ENVSVRLNLEAEFHFTHLIMKFKTFRPAAMIIERSSDFGRTWRIYRYFAYNCTKTFPRVPAHSLRF-IDEVIC 187
Cdd:pfam00055 72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIkDDEVIC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 188 EERYSDIEPSTDGEVIYKVL--DPAIHVKDpYSLDIQDLLRITNLRINFTKLHTLGDNLLDrRPDVLQKYYYALYELVVR 265
Cdd:pfam00055 152 TSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLD-DPSVLRKYYYAISDISVG 229
|
.
gi 528517788 266 G 266
Cdd:pfam00055 230 G 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
26-266 |
4.58e-83 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 272.70 E-value: 4.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 26 GCMDGSCYPATGNLLIGRAInlTTSSTCGLDGPEPYCI-VSHLKDSEKCFICDSENPYDanyhrdSHRVENVIYPmDSTG 104
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGREV--TATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDG-NNPN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 105 ELTWWQA---VNGEENVSVRLNLEAEFHFTHLIMKFKTFRPAAMIIERSsDFGRTWRIYRYFAYNCTKTFPRVPAHSLR- 180
Cdd:smart00136 72 NPTWWQSeplSNGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITk 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 181 -FIDEVICEERYSDIEPSTDGEVIYKVLDPAIHVKD-PYSLDIQDLLRITNLRINFTKLHTLGDNLLDRRPDVLQKYYYA 258
Cdd:smart00136 151 gNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 528517788 259 LYELVVRG 266
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1766-1835 |
9.10e-29 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 110.45 E-value: 9.10e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1766 NQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
816-861 |
1.66e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 69.26 E-value: 1.66e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517788 816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGFGPYGC 861
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1492-1818 |
3.37e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.14 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1492 DNADEVHKNLTAVSEELQT----MAKKLRDIATLTQT---VKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEE 1564
Cdd:TIGR04523 96 DKINKLNSDLSKINSEIKNdkeqKNKLEVELNKLEKQkkeNKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1565 GADPESIEKVAQQVLAISLPVNR--TVIVNLVEQIKDsivnltnvegvfnHTSEQlAKVNDLLKKAQDAKTQADGVSDNI 1642
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKleLLLSNLKKKIQK-------------NKSLE-SQISELKKQNNQLKDNIEKKQQEI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1643 NKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNlsngvdlLKNKTEQNreMAKEA 1722
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD-------LNNQKEQD--WNKEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1723 KAQSDNATREAEGLQEELTNAETLYKQLKEKV-----DSAGGTGEGNVNQKAIEMKK-EAEDLLKKATMGMETLKKLERK 1796
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQIsqlkkELTNSESENSEKQRELEEKQnEIEKLKKENQSYKQEIKNLESQ 392
|
330 340
....*....|....*....|..
gi 528517788 1797 FNKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQI 414
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
816-861 |
5.29e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.76 E-value: 5.29e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517788 816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGFG---PYGC 861
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdpPQGC 49
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1495-1819 |
8.25e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.98 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1495 DEVHKNLTAVSEELQTMAKKLRDI-ATLT-------------QTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDf 1560
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLdKNLNkdeekinnsnnkiKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1561 lneegaDPESIEKvaqqvlaislpvNRTVIVNLVEQIKdsivnltnvegvfnHTSEQLAKVNDLLKKAQDAKTQADGVSD 1640
Cdd:TIGR04523 115 ------DKEQKNK------------LEVELNKLEKQKK--------------ENKKNIDKFLTEIKKKEKELEKLNNKYN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1641 NINKTKEALETSQNaikKAEEEMSTALKNLKNIQNITAMVDDKLLNLD------NNLTDVMMRL----VNLSNGVDLLKN 1710
Cdd:TIGR04523 163 DLKKQKEELENELN---LLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiqknKSLESQISELkkqnNQLKDNIEKKQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1711 KTEQ-------NREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDsaggtgegNVNQKAIEMKKEAE-DLLKK 1782
Cdd:TIGR04523 240 EINEktteisnTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN--------QLKSEISDLNNQKEqDWNKE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 528517788 1783 ATMGMETLKK----LERKFNKNEQKMQQQRDELTDLEKNVT 1819
Cdd:TIGR04523 312 LKSELKNQEKkleeIQNQISQNNKIISQLNEQISQLKKELT 352
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
864-912 |
8.29e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 67.38 E-value: 8.29e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517788 864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFPNCRQCQC 912
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
816-862 |
1.22e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 66.61 E-value: 1.22e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517788 816 CQCDPQGSLSAECDRVGGQCRCKPNVIGRKCNQCAPGTYGF--GPYGCT 862
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1314-1828 |
1.04e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.52 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1314 DLNVTTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENYLTAGLA-EQFANVLKYY---QRSLNSE----QRCNASVyg 1385
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlELLLSNLKKKiqkNKSLESQiselKKQNNQL-- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1386 pQSPVEQSQDTRNRTEALLKDKKDSLLRTATANNKSLSELEGKAHEINRKVHHLSNKvcgghaNGNVNgsceespcggag 1465
Cdd:TIGR04523 231 -KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL------EKQLN------------ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1466 crgsdgvlkcggrgcngTVGASVKALDN--ADEVHKNLtavSEELQTMAKKLRDIAT-LTQTVK--TQAKETLdkAQNKK 1540
Cdd:TIGR04523 292 -----------------QLKSEISDLNNqkEQDWNKEL---KSELKNQEKKLEEIQNqISQNNKiiSQLNEQI--SQLKK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1541 dmfEKSNKMLKNfiQKIKDFLNEEGADPESIEKVAQQVlaislpvnrtvivnlveqiKDSIVNLTNvegvfnhtseqlaK 1620
Cdd:TIGR04523 350 ---ELTNSESEN--SEKQRELEEKQNEIEKLKKENQSY-------------------KQEIKNLES-------------Q 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1621 VNDLLKKAQDAKtqadgvsdNINKTKealetsQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDvmmrlvn 1700
Cdd:TIGR04523 393 INDLESKIQNQE--------KLNQQK------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV------- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1701 LSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVdsaggtgegnvnqkaIEMKKEAEDLL 1780
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK---------------KELEEKVKDLT 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 528517788 1781 KKATMGMETLKKLERKFNKNEQKMQQQRDELT--DLEKNVTGIREYIRSK 1828
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEK 566
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
864-905 |
1.16e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 63.91 E-value: 1.16e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517788 864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFP 905
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1495-1816 |
3.47e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.59 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1495 DEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQaKETLdkaQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPESIEKV 1574
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ-KEEL---ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1575 AQQVLAISLPVN-----RTVIVNLVEQIKDSIVNLTNVegvFNHTSEQLakvNDLLKKAQDAKTQADGVSDNINKTKEAL 1649
Cdd:TIGR04523 210 IQKNKSLESQISelkkqNNQLKDNIEKKQQEINEKTTE---ISNTQTQL---NQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1650 ETSQNAIKKAEEEMSTaLKNLKNiQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQ--------------- 1714
Cdd:TIGR04523 284 KELEKQLNQLKSEISD-LNNQKE-QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQlkkeltnsesensek 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1715 NREMAK-------------EAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggTGEGNVNQKAIE--------MK 1773
Cdd:TIGR04523 362 QRELEEkqneieklkkenqSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL--QQEKELLEKEIErlketiikNN 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 1774 KEAEDL-------------LKKATMGMET-LKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:TIGR04523 440 SEIKDLtnqdsvkeliiknLDNTRESLETqLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1493-1828 |
1.12e-11 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 70.63 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1493 NADEVHKNLTAVSEELQTMAKKLRDIA------------TLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDF 1560
Cdd:PTZ00440 1259 IKLQVFSYLQQVIKENNKMENALHEIKnmyeflisidseKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQA 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1561 ----------LNEEGADPE--SIEKVAQQVLAIslpvnRTVIVNLVEQIKDsivNLTNVEGVFNHTSEQLAKVNDLLKKA 1628
Cdd:PTZ00440 1339 kehknkiygsLEDKQIDDEikKIEQIKEEISNK-----RKEINKYLSNIKS---NKEKCDLHVRNASRGKDKIDFLNKHE 1410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1629 QDAKTQA-----DGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNI-----TAMVDDKLLNLDNNLTDVMMRl 1698
Cdd:PTZ00440 1411 AIEPSNSkevniIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNIlnnssILGKKTKLEKKKKEATNIMDD- 1489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1699 VNLSNGVdlLKNKTEQNREMAKEAKAQSdNATREaeglQEELTNAETlyKQLKEKVDSAGGTGEGNVnQKAIEMKKEAED 1778
Cdd:PTZ00440 1490 INGEHSI--IKTKLTKSSEKLNQLNEQP-NIKRE----GDVLNNDKS--TIAYETIQYNLGRVKHNL-LNILNIKDEIET 1559
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 528517788 1779 LLKKATMGMETLKKLERKF-NKNEQKMQQQRDELTDLEKNVTGIREYIRSK 1828
Cdd:PTZ00440 1560 ILNKAQDLMRDISKISKIVeNKNLENLNDKEADYVKYLDNILKEKQLMEAE 1610
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
395-452 |
1.43e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 1.43e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517788 395 CDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGLSLDDPLGC 452
Cdd:pfam00053 1 CDCNPHGSL-SDTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
864-905 |
1.74e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 1.74e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 528517788 864 CDCHSQGSVGHHCDPVTGQCMCRHGAIGRQCSECQPGQWGFP 905
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1175-1215 |
1.89e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 1.89e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 528517788 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTGN 1215
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGL 41
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1506-1819 |
4.44e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 68.46 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1506 EELQTMAKKLRDIATLTQTVKT---QAKETLDKAQNKKDMFEKSNKML----KNFIQKIKDFLNEEGADPESIEKVAQQV 1578
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKlkeQAKKALEYYQLKEKLELEEEYLLyldyLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1579 LAISLPVNRTVIVNLVE-----------------QIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDN 1641
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEeekekklqeeelkllakEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1642 INKTKEALETSQNAIKKAEEEMStalknlkniqnitamvdDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKE 1721
Cdd:pfam02463 340 LEKELKELEIKREAEEEEEEELE-----------------KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1722 AKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNE 1801
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330
....*....|....*...
gi 528517788 1802 QKMQQQRDELTDLEKNVT 1819
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQ 500
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1766-1835 |
8.01e-11 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 59.29 E-value: 8.01e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1766 NQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22301 1 NERLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1288-1821 |
8.40e-11 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 67.55 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1288 NLISQTVDDLRAE----IALTDG---RLMGVIR-----DLNVTTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENYLT 1355
Cdd:PTZ00440 684 DNIDNIIKNLKKElqnlLSLKENiikKQLNNIEqdisnSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFIL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1356 AgLAEQFANV----------LKYYQRSLNSEQRCNASVYGPQSPVEQSQDTRNRTEAL---LKD---KKDSLLRTATA-- 1417
Cdd:PTZ00440 764 H-LYENDKDLpdgkntyeefLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILiqkLEAhteKNDEELKQLLQkf 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1418 ----NNKSLSELEGKAHEINRKVHHLSNKVcgGHANGNVNgsceespcggagcrgsdgVLKcggrGCNGTVGASVKALDN 1493
Cdd:PTZ00440 843 ptedENLNLKELEKEFNENNQIVDNIIKDI--ENMNKNIN------------------IIK----TLNIAINRSNSNKQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1494 ADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNK--KDMFEKSNKMLKNFIQKI-------------K 1558
Cdd:PTZ00440 899 VEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKieKQLSDTKINNLKMQIEKTleyydkskeningN 978
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1559 DFLNEEGADPESIEKVAQQVLAISLPVNRTV----IVNLVEQIKDSIVNLTN--VEGVFNHTSEQLAKVNDLLKKAQDaK 1632
Cdd:PTZ00440 979 DGTHLEKLDKEKDEWEHFKSEIDKLNVNYNIlnkkIDDLIKKQHDDIIELIDklIKEKGKEIEEKVDQYISLLEKMKT-K 1057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1633 TQADGVSDNINKTKEAleTSQNAIKKAEEEMSTALKNLKNIQNitamvddKLLNLDNNLTDVMmrlVNLSNGVDLLKNKT 1712
Cdd:PTZ00440 1058 LSSFHFNIDIKKYKNP--KIKEEIKLLEEKVEALLKKIDENKN-------KLIEIKNKSHEHV---VNADKEKNKQTEHY 1125
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1713 EQNREMAKEAKAQSDNATREAEGLQEELT------NAETLYK---------QLKEKVDSAGGTGEgnvnqkAIEMKKEAE 1777
Cdd:PTZ00440 1126 NKKKKSLEKIYKQMEKTLKELENMNLEDItlnevnEIEIEYErilidhiveQINNEAKKSKTIME------EIESYKKDI 1199
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 528517788 1778 DLLKKaTMGMETLKKLeRKFNKNeqkmqQQRDELTDLEKNVTGI 1821
Cdd:PTZ00440 1200 DQVKK-NMSKERNDHL-TTFEYN-----AYYDKATASYENIEEL 1236
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1492-1818 |
1.37e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.58 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1492 DNADEVhKNLTAVSEELQTMAKKLRDIatlTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDfLNEEGADPEsi 1571
Cdd:TIGR04523 437 KNNSEI-KDLTNQDSVKELIIKNLDNT---RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK-LNEEKKELE-- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1572 EKVAqqvlaislpvnrtvivNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKT--QADGVSDNINKTKEAL 1649
Cdd:TIGR04523 510 EKVK----------------DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNKEIEEL 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1650 ETSQNAIKKAEEEMSTALKNL-KNIQNIT---AMVDDKLLNLDNNLTDVMM---RLVNLSNGVDLLKNKTEQNREMAKEa 1722
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKeKEKKDLIkeiEEKEKKISSLEKELEKAKKeneKLSSIIKNIKSKKNKLKQEVKQIKE- 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1723 kaqsdnatrEAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKatmgmETLKKLERKFNKNEQ 1802
Cdd:TIGR04523 653 ---------TIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRI-----KDLPKLEEKYKEIEK 718
|
330
....*....|....*.
gi 528517788 1803 KMQQQRDELTDLEKNV 1818
Cdd:TIGR04523 719 ELKKLDEFSKELENII 734
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1175-1223 |
1.47e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.13 E-value: 1.47e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 528517788 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTGNFPKCVPCH 1223
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1260-1828 |
1.91e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.15 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1260 SDKRILELEKKLAQAQELVRDGDREgtfNLISQTVDDLRAEIALTDGRLMgvirdlnvttdHNNDLKQNLTALEKELKDL 1339
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKL---QSLCKELDILQREQATIDTRTS-----------AFRDLQGQLAHAKKQQELQ 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1340 NNTLHQLRRELENYLTAGLAEqfanvlkyyqrslNSEQRcnasvygpqspvEQSQDTRNRTEaLLKDKKDSLL---RTAT 1416
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLE-------------KIHLQ------------ESAQSLKEREQ-QLQTKEQIHLqetRKKA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1417 ANNKSLSELEGKAHEINRKVHHLSNKVcggHANGNVNGSCeeSPCggagCRGSDGVLKcggrgcNGTVGASVKAldNADE 1496
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPAR---QDIDNPGPLT--RRM----QRGEQTYAQ------LETSEEDVYH--QLTS 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1497 VHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKET---LDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPESI-- 1571
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLqniTVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRlh 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1572 EKVAQQVLAISLPVNRTVIVNLV-EQIKDSIVNLTNVEgvfnhtSEQLAKVNDLLKKAQDAKTQADGVsdninktKEALE 1650
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLTqERVREHALSIRVLP------KELLASRQLALQKMQSEKEQLTYW-------KEMLA 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1651 TSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVdlLKNKT---EQNRE---MAKEAKA 1724
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTV--LKARTeahFNNNEevtAALQTGA 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1725 QSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLL-----KKATMGMET--LKKLERKF 1797
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleeKSATLGEIThqLLKYEECS 858
|
570 580 590
....*....|....*....|....*....|.
gi 528517788 1798 NKNEQKMQQQRdELTDLEKNVTGIREYIRSK 1828
Cdd:TIGR00618 859 KQLAQLTQEQA-KIIQLSDKLNGINQIKIQF 888
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1175-1219 |
2.66e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 2.66e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517788 1175 CNCHPLGSETSQCDRTTGACVCKDGASGQRCDECARGFTG-NFPKC 1219
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1488-1823 |
2.99e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1488 VKALDNADEVhknLTAVSEELQTMAKKLRDIATLTQTVKtqakETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGAD 1567
Cdd:PRK02224 233 RETRDEADEV---LEEHEERREELETLEAEIEDLRETIA----ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1568 PESIEKVAQQVLAISlpvnrtvivNLVEQIKDSIVNLTNVEGVFNHTSEQLAK-VNDLLKKAQDAKTQADGVSDNINKTK 1646
Cdd:PRK02224 306 DADAEAVEARREELE---------DRDEELRDRLEECRVAAQAHNEEAESLREdADDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1647 EALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAK--- 1723
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpe 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1724 -AQS----------DNATREAEGLQEELTNAETLYKQLKEKVDSAggtgegnvnQKAIEMKKEAEDLLKKATMGMETLKK 1792
Cdd:PRK02224 457 cGQPvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERA---------EDLVEAEDRIERLEERREDLEELIAE 527
|
330 340 350
....*....|....*....|....*....|.
gi 528517788 1793 LERKFNKNEQKMQQQRDELTDLEKNVTGIRE 1823
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
454-505 |
4.47e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 4.47e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 528517788 454 PCNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSHDLAGCR 505
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1767-1836 |
6.41e-10 |
|
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.
Pssm-ID: 411974 [Multi-domain] Cd Length: 71 Bit Score: 57.07 E-value: 6.41e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1767 QKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNCQ 1836
Cdd:cd22303 2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTCK 71
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
394-453 |
1.18e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.44 E-value: 1.18e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 394 PCDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGLSLdDPLGCQ 453
Cdd:cd00055 1 PCDCNGHGSL-SGQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1767-1835 |
1.79e-09 |
|
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.
Pssm-ID: 411971 [Multi-domain] Cd Length: 73 Bit Score: 55.56 E-value: 1.79e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517788 1767 QKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22300 4 KKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTC 72
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
455-504 |
2.64e-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: 54.28 E-value: 2.64e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 528517788 455 CNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLSHDLA-GC 504
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPqGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1523-1816 |
4.00e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1523 QTVKTQAKET--LDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPESIEKVAQQVLAISLpvNRTVIVNLVEQIKDS 1600
Cdd:PTZ00121 1233 EEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA--KKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1601 IVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKN---LKNIQNIT 1677
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaAKKKAEEK 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1678 AMVDD--KLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREmAKEAKAQSDNATR--EAEGLQEELTNAETLYKQLKEK 1753
Cdd:PTZ00121 1391 KKADEakKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEA 1469
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528517788 1754 VDSAGGTGEGNVNQKAIEMKKEAEDLLKKATmgmETLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKAD---EAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1481-1824 |
6.59e-09 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 61.39 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1481 NGTVGASVKALDNADEVHKNLTAVSEELqtmaKKLRDIATLTQTVKTQAKETLDKAQNKKDMFEKS----------NKML 1550
Cdd:PTZ00440 470 KSFYDLIISEKDSMDSKEKKESSDSNYQ----EKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIeglkneieglIELI 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1551 KNFIQKIKDFLNEEGADPESIEKVAQQVLAIS---------LPVNRTvIVNLVEQIKDSI-VNLTNVEGVFNHTSEQLAK 1620
Cdd:PTZ00440 546 KYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEenvdhikdiISLNDE-IDNIIQQIEELInEALFNKEKFINEKNDLQEK 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1621 VNDLLKKAQDAKTQ--ADGVSDNINKTKEALETsqnaiKKAEEEMSTALKNLKNIQN-ITAMVDDkllNLDNNLTDVMMR 1697
Cdd:PTZ00440 625 VKYILNKFYKGDLQelLDELSHFLDDHKYLYHE-----AKSKEDLQTLLNTSKNEYEkLEFMKSD---NIDNIIKNLKKE 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1698 LVNLSNGVDLLKNKTEQNreMAKEAKAQSDNATREAeglqEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAE 1777
Cdd:PTZ00440 697 LQNLLSLKENIIKKQLNN--IEQDISNSLNQYTIKY----NDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDK 770
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 528517788 1778 DLLKKATMGMETLKKLERKFNKnEQKMQQQRDELTDLEKNVTGIREY 1824
Cdd:PTZ00440 771 DLPDGKNTYEEFLQYKDTILNK-ENKISNDINILKENKKNNQDLLNS 816
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1126-1168 |
7.87e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.13 E-value: 7.87e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 528517788 1126 PCGCVQPNALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDP 1168
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1612-1829 |
8.43e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1612 NHTSEQLAKVNDLL--------------KKAQDAKTQADGVSD--------NINKTKEALETSQNAIKKAEEEMSTALKN 1669
Cdd:TIGR02168 182 ERTRENLDRLEDILnelerqlkslerqaEKAERYKELKAELRElelallvlRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1670 LKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNgvdlLKNKTEQNREMAKEAKAQSDnatREAEGLQEELTNAETLYKQ 1749
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALAN----EISRLEQQKQILRERLANLE---RQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1750 LKEKVDSaggtgegnVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIR---EYIR 1826
Cdd:TIGR02168 335 LAEELAE--------LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneiERLE 406
|
...
gi 528517788 1827 SKV 1829
Cdd:TIGR02168 407 ARL 409
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1122-1175 |
1.10e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528517788 1122 CGCEPCGcvqpnALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDPRVQCEEC 1175
Cdd:pfam00053 1 CDCNPHG-----SLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1262-1693 |
1.44e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1262 KRILELEKKLAQAQELVRDGDR-----EGTFNLISQTVDDLRAEIAL----------TDGRLMGVIRDLNVTTDHnndLK 1326
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEqikklQQEKELLEKEIERLKETIIKnnseikdltnQDSVKELIIKNLDNTRES---LE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1327 QNLTALEKELKDLNNTLHQLRRELE---------NYLTAGLAEQFANvLKYYQRSLNSEQrcnasvygpqspvEQSQDTR 1397
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKskekelkklNEEKKELEEKVKD-LTKKISSLKEKI-------------EKLESEK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1398 NRTEALLKDKKDSLLRTATANNKSLseLEGKAHEINRKVHHLSNkvcgghangnvngsceespcggagcrgsdgvlkcgg 1477
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQ------------------------------------ 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1478 rgcngtvgasvkalDNadevhKNLTAVSEELQTMAKKLRD--------IATLTQTVKTQAKEtLDKAqnkkdmfEKSNKM 1549
Cdd:TIGR04523 576 --------------TQ-----KSLKKKQEEKQELIDQKEKekkdlikeIEEKEKKISSLEKE-LEKA-------KKENEK 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1550 LKNFIQKIKdflneegadpESIEKVAQQvlaislpvnrtvivnlVEQIKDSIVNLTNvegvfnhtseqlaKVNDLLKKAQ 1629
Cdd:TIGR04523 629 LSSIIKNIK----------SKKNKLKQE----------------VKQIKETIKEIRN-------------KWPEIIKKIK 669
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528517788 1630 DAKTQadgVSDNINKTKEALETSQNAIKKAEEEMsTALKNL-------KNIQNITAMVDDKLLNLDNNLTD 1693
Cdd:TIGR04523 670 ESKTK---IDDIIELMKDWLKELSLHYKKYITRM-IRIKDLpkleekyKEIEKELKKLDEFSKELENIIKN 736
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1483-1818 |
1.68e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 60.07 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1483 TVGASVKALDNADEVHKNLTAVSEELQTMAKKLRDIATLT-QTVKTQAKETLDKAQNKK--DMFEKSNKMLKNF-----I 1554
Cdd:TIGR01612 1241 MIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNiSHDDDKDHHIISKKHDENisDIREKSLKIIEDFseesdI 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1555 QKIKDFLNEEGADPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDSIVNLTN-VEGVFNHTSEQLAKVNDLLKKAQD--- 1630
Cdd:TIGR01612 1321 NDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEYTKeIEENNKNIKDELDKSEKLIKKIKDdin 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1631 ---AKTQADGVSD--NINKTKEALETSQNAIKKAEEEMSTALKNLK-NIQNITAMVDDklLNLDNNLTDVMMRLV--NLS 1702
Cdd:TIGR01612 1401 leeCKSKIESTLDdkDIDECIKKIKELKNHILSEESNIDTYFKNADeNNENVLLLFKN--IEMADNKSQHILKIKkdNAT 1478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1703 NGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEeltnaetLYKQLKEKVDSAggtgegnVNQ-KAIEMKKEAEDLLK 1781
Cdd:TIGR01612 1479 NDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKE-------LFEQYKKDVTEL-------LNKySALAIKNKFAKTKK 1544
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 528517788 1782 KATMGMETLKKLERKF----NKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR01612 1545 DSEIIIKEIKDAHKKFileaEKSEQKIKEIKKEKFRIEDDA 1585
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1496-1828 |
2.09e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1496 EVHKNLTAVSEELQTMAKKLRDIAT----LTQTVKT--QAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPE 1569
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREelekLEKEVKEleELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1570 SIEKVAQQVLAISLPVNRTVIvnLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADgvsdNINKTKEAL 1649
Cdd:PRK03918 277 ELEEKVKELKELKEKAEEYIK--LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1650 ETSQNAIKKAEEEMSTALKNLKNIQNITAM--------VDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQ------- 1714
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEELERLKKRltgltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaiee 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1715 -----------NREMAKEAKAQSDNA-TREAEGLQEELTNAETLYKQLKE---KVDSA-GGTGEGNVNQKAIEMKKEAED 1778
Cdd:PRK03918 431 lkkakgkcpvcGRELTEEHRKELLEEyTAELKRIEKELKEIEEKERKLRKelrELEKVlKKESELIKLKELAEQLKELEE 510
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 528517788 1779 LLKKatMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSK 1828
Cdd:PRK03918 511 KLKK--YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1489-1795 |
2.10e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.61 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDK-----------AQNKKDMFEKSNKmLKNFIQKI 1557
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKrdelnekvkelKEERDELNEKLNE-LREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1558 KDFLNEEGADPESIEKV---------AQQVLAISLPVNRtvivNLVEQIKdsivnltnvegvfnhtseQLAKvndLLKKA 1628
Cdd:COG1340 98 RKELAELNKAGGSIDKLrkeierlewRQQTEVLSPEEEK----ELVEKIK------------------ELEK---ELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1629 QDAKTQADGVSDNINKTKEaletsqnaIKKAEEEMSTALKNLKN-IQNITAmvddkllnldnnltdvmmRLVNLSNGVDL 1707
Cdd:COG1340 153 KKALEKNEKLKELRAELKE--------LRKEAEEIHKKIKELAEeAQELHE------------------EMIELYKEADE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1708 LKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKvdsaggtgegnvnQKAIEMKKEAEDLLKKATMGM 1787
Cdd:COG1340 207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKK-------------QRALKREKEKEELEEKAEEIF 273
|
....*...
gi 528517788 1788 ETLKKLER 1795
Cdd:COG1340 274 EKLKKGEK 281
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1127-1172 |
2.24e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 2.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517788 1127 CGCVQPNALSTHCNMFSGQCHCQPGFGGRQCNECEAFHWGDPRVQC 1172
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
395-452 |
2.55e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 2.55e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 528517788 395 CDCDPVGSVeGGVCDSHTdldlgmigGQCRCKQNVRGQRCDYCKEGHYGlslDDPLGC 452
Cdd:smart00180 1 CDCDPGGSA-SGTCDPDT--------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
910-954 |
2.62e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 2.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 528517788 910 CQCNSHA---ESCDPESGACyDCRDNTAGQLCERCVDGYYGNPALGSG 954
Cdd:cd00055 2 CDCNGHGslsGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
910-957 |
2.69e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.59 E-value: 2.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 528517788 910 CQCNSHA---ESCDPESGACyDCRDNTAGQLCERCVDGYYGNPAlGSGEHC 957
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1619-1810 |
5.05e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1619 AKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNI---QNITAMVDDKLLNL--DNNLTD 1693
Cdd:COG3883 37 AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraLYRSGGSVSYLDVLlgSESFSD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1694 VMMRlvnlsngVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgegnvNQKAIEMK 1773
Cdd:COG3883 117 FLDR-------LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL--------EAQQAEQE 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 528517788 1774 KEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDE 1810
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1505-1816 |
5.46e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.46 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1505 SEELQTMAKKLRDiatltqtvktQAKETLDKAQNKKDMFEKSNKMLKNFIQKiKDFLNEEGAdpESIEKvAQQVLAIslp 1584
Cdd:COG1340 3 TDELSSSLEELEE----------KIEELREEIEELKEKRDELNEELKELAEK-RDELNAQVK--ELREE-AQELREK--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1585 vnRTVIVNLVEQIKDSIvnltnvegvfnhtSEQLAKVNDLLKKAQDAKTQADgvsdNINKTKEALETSQNAIKKAEEEMS 1664
Cdd:COG1340 66 --RDELNEKVKELKEER-------------DELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLEWRQQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1665 TALKNLKN-------IQNITAMVDD--KLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEG 1735
Cdd:COG1340 127 TEVLSPEEekelvekIKELEKELEKakKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1736 LQEELTNAETLYKQLKEKVDsaggtgegNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKfnKNEQKMQQQRDELtdLE 1815
Cdd:COG1340 207 LRKEADELHKEIVEAQEKAD--------ELHEEIIELQKELRELRKELKKLRKKQRALKRE--KEKEELEEKAEEI--FE 274
|
.
gi 528517788 1816 K 1816
Cdd:COG1340 275 K 275
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1260-1816 |
5.98e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1260 SDKRILELEKKLAQAQELVRDGDREGTFNLISQ------------TVDDLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQ 1327
Cdd:TIGR00606 533 TRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqledWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINN 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1328 NLTALEKEL-------------KDLNNTLHQLRRELE-----------------NYLTAgLAEQFANVLKYYQRSLNSEQ 1377
Cdd:TIGR00606 613 ELESKEEQLssyedklfdvcgsQDEESDLERLKEEIEksskqramlagatavysQFITQ-LTDENQSCCPVCQRVFQTEA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1378 RCNASVYGPQSPVEQSQDTRNRTEALLKDK---KDSLLRTATANN-------KSLSELEGKAHEINRKVHHLSNKVCGGH 1447
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKekrRDEMLGLAPGRQsiidlkeKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1448 AN-GNVNGScEESpcggagcrgsdgvlkcgGRGCNGTVGASVKALDNADEVHKNLTAVSEELQTmAKKLRDIATLTQTVK 1526
Cdd:TIGR00606 772 TLlGTIMPE-EES-----------------AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVNQEKQ 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1527 tQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEGADPESIEKVAQQVLAislpvnrtvivnLVEQIKDSIVNLTN 1606
Cdd:TIGR00606 833 -EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ------------FEEQLVELSTEVQS 899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1607 VEGVFNHTSEQLAKVNDLLKKAQDAKTQAdgvsdnINKTKEALETSQNAIKKAEEEMSTALKNLKNIQN-ITAMVDDKLL 1685
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEKEEL------ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkIQDGKDDYLK 973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1686 NLDNNLTDVMMRLvnlsngvdllkNKTEQNREMAKE----AKAQSDNATREAEGLQEELTnAETLYKQLKEkVDSAGGTG 1761
Cdd:TIGR00606 974 QKETELNTVNAQL-----------EECEKHQEKINEdmrlMRQDIDTQKIQERWLQDNLT-LRKRENELKE-VEEELKQH 1040
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517788 1762 EGNVNQKAI-EMKKEAEDLlkkatmgMETLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:TIGR00606 1041 LKEMGQMQVlQMKQEHQKL-------EENIDLIKRNHVLALGRQKGYEKEIKHFKK 1089
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
455-498 |
8.09e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.00 E-value: 8.09e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 528517788 455 CNCDPRGitTLGVPCDQISGDCSCKRYVTGRYCNQCLPEYWGLS 498
Cdd:smart00180 1 CDCDPGG--SASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1487-1818 |
8.75e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.75 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1487 SVKALDNADEVHKNLTAVSEEL-----QTMAKKLRDIATLTQTVKTQAKETLDKAQNKkdmFEKSNKMLKNFIQKIKDFL 1561
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKmekvfQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLLNQEKTELL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1562 NEEGADPESIEKVAQQVLAISLPVNRTVI---VNLVEQIKDSIVNLTNVEGVFNHTSEQLAKV-----NDLLKKAQDAKT 1633
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRARDSLIQSLATrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTaaqlcADLQSKERLKQE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1634 QADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLkniQNITAMVDDkLLNLDNNLTDVMMRLVNLSNGVDLlknKTE 1713
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL---QQLEGSSDR-ILELDQELRKAERELSKAEKNSLT---ETL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1714 QNREMA-KEAKAQSDNATREAEGLQEELTNAETLYKQL----KEKVDSaggtgegnvNQKAIEMKKEAEDLLKKATMGME 1788
Cdd:TIGR00606 500 KKEVKSlQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMemltKDKMDK---------DEQIRKIKSRHSDELTSLLGYFP 570
|
330 340 350
....*....|....*....|....*....|
gi 528517788 1789 TLKKLERKFNKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDRLAKLNKEL 600
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1491-1814 |
9.24e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1491 LDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETL--------DKAQNKKDMFEKSNKMLKNFIQKIKDFLN 1562
Cdd:pfam12128 346 QEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdiagikDKLAKIREARDRQLAVAEDDLQALESELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1563 E--EGADPESIEKVAQQVLAISlpvNRTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSD 1640
Cdd:pfam12128 426 EqlEAGKLEFNEEEYRLKSRLG---ELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1641 N----INKTKEALETSQNAIKKAEEEMS----TALKNLKN-----IQNITAMVDDKLL---NLD-----------NNLTD 1693
Cdd:pfam12128 503 QaseaLRQASRRLEERQSALDELELQLFpqagTLLHFLRKeapdwEQSIGKVISPELLhrtDLDpevwdgsvggeLNLYG 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1694 VMMRL----VN--------LSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggTG 1761
Cdd:pfam12128 583 VKLDLkridVPewaaseeeLRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRL--FD 660
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 528517788 1762 EGNVNQKAIEMKKEAEdlLKKATMGMETLKKlERKFNKNEQK--MQQQRDELTDL 1814
Cdd:pfam12128 661 EKQSEKDKKNKALAER--KDSANERLNSLEA-QLKQLDKKHQawLEEQKEQKREA 712
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1512-1828 |
9.92e-08 |
|
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: 56.89 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1512 AKKLRDIATLTQTVKTQaketLDKAQNKKDMFEKSN---KMLKNFIQKIKDFLNEEGADPESIEKVAQQVLaiSLPVNRT 1588
Cdd:COG5185 85 ARKFLKEKKLDTKILQE----YVNSLIKLPNYEWSAdilISLLYLYKSEIVALKDELIKVEKLDEIADIEA--SYGEVET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1589 VIVNLVEQI-KDSIVNLTNVEGVFNHTSEQLAKVNDLlKKAQDAKTQadgvsdNINKTKEALET---SQNAIKKAEEEms 1664
Cdd:COG5185 159 GIIKDIFGKlTQELNQNLKKLEIFGLTLGLLKGISEL-KKAEPSGTV------NSIKESETGNLgseSTLLEKAKEII-- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1665 TALKNLKNIQNITAMVDDKllnldNNLTDVMMRLVNLSNgvDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAE 1744
Cdd:COG5185 230 NIEEALKGFQDPESELEDL-----AQTSDKLEKLVEQNT--DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1745 tlykqlkEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGmetLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREY 1824
Cdd:COG5185 303 -------KSIDIKKATESLEEQLAAAEAEQELEESKRETETG---IQNLTAEIEQGQESLTENLEAIKEEIENIVGEVEL 372
|
....
gi 528517788 1825 IRSK 1828
Cdd:COG5185 373 SKSS 376
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1264-1827 |
1.08e-07 |
|
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: 57.16 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1264 ILELEKKLAQAQELVRDGDREGTFNLISQTvDDLRAEIALTDGRLMGVIRDLNVTTDH----NNDLKQNLTA-LEKELKD 1338
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLD-DQWKEKRDELNGELSAADAAVAKDRSElealEDQHGAFLDAdIETAAAD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1339 LNNtLHQLRRELENY--LTAGLAEQFANVLKYYQ-RSLNSEQRCNASVYGPQSPVEQSQDTRNRTEALLKDKKDSL---L 1412
Cdd:pfam12128 346 QEQ-LPSWQSELENLeeRLKALTGKHQDVTAKYNrRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeseL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1413 RtatannkslSELEGKAHEINRKVHHLSNKVcgGHANGNVNGSCEESpcggagcrgsDGVLKcggrgcngtVGASVKALD 1492
Cdd:pfam12128 425 R---------EQLEAGKLEFNEEEYRLKSRL--GELKLRLNQATATP----------ELLLQ---------LENFDERIE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1493 NADEVHKNLTAVSEELQ---TMAKKLRDIATLTQTVKTQAKETLDKA--QNKKDMFEKSNKMLknfiqkikDFLNEEGAD 1567
Cdd:pfam12128 475 RAREEQEAANAEVERLQselRQARKRRDQASEALRQASRRLEERQSAldELELQLFPQAGTLL--------HFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1568 -PESIEKVAQQVLaislpVNRTVIVNLV--EQIKDSIvnltNVEGVFNHTseQLAKVNDLLKKAQDAKTQADgvsdninK 1644
Cdd:pfam12128 547 wEQSIGKVISPEL-----LHRTDLDPEVwdGSVGGEL----NLYGVKLDL--KRIDVPEWAASEEELRERLD-------K 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1645 TKEALETSQNAIKKAEEEMSTALKNLKNIQnitAMVDDKLLNLDNNltdvMMRLVNLSNGVDLLKNKTEQNREmakEAKA 1724
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKAS---REETFARTALKNA----RLDLRRLFDEKQSEKDKKNKALA---ERKD 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1725 QSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMET-----LKKLERKFNK 1799
Cdd:pfam12128 679 SANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSgakaeLKALETWYKR 758
|
570 580
....*....|....*....|....*...
gi 528517788 1800 NEQKMQQQRDELTDLEknvTGIREYIRS 1827
Cdd:pfam12128 759 DLASLGVDPDVIAKLK---REIRTLERK 783
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1506-1825 |
1.24e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 57.15 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1506 EELQTMAKKLRDIATLTQTV-KTQAKETLD---KAQNKKDMFEKSNKML----KNF-IQKIKDFLN---------EEGAD 1567
Cdd:PTZ00440 2226 QEIENSSEKYNDISKLFNNVvETQKKKLLDnknKINNIKDKINDKEKELinvdSSFtLESIKTFNEiyddiksniGDLYK 2305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1568 PESIEKVAQQVLAISLPvNRTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKaqdaktqadgVSDNINKTKE 1647
Cdd:PTZ00440 2306 LEDTNNDELKKVKLYIE-NITHLLNRINTLINDLDNYQDENYGKDKNIELNNENNSYIIK----------TKEKINNLKE 2374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1648 ALETSQNAIKKAEEEMSTalKNLKN-IQNITAMVDD-------------KLLNLDNNLTDV--MMRLVNLSNGVDLLKNK 1711
Cdd:PTZ00440 2375 EFSKLLKNIKRNNTLCNN--NNIKDfISNIGKSVETikqrfssnlpekeKLHQIEENLNEIknIMNETKRISNVDAFTNK 2452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1712 TEQNREMAKEakaqSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgeGNVNQKAIEMKKEAEDLLKKATMGMETLK 1791
Cdd:PTZ00440 2453 ILQDIDNEKN----KENNNMNAEKIDDLIENVTSHNEKIKSELLII-----NDALRRVKEKKDEMNKLFNSLTENNNNNN 2523
|
330 340 350
....*....|....*....|....*....|....
gi 528517788 1792 KLERKFNKNEQKMQQQrdeltdLEKNVTGIREYI 1825
Cdd:PTZ00440 2524 NSAKNIVDNSTYIINE------LESHVSKLNELL 2551
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
960-1016 |
1.33e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 49.66 E-value: 1.33e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 960 CPCPGHPdsghSNGASCEvdyaSNQILCQCGQGYAGPRCDRCAPGYYGDPEHPGGSC 1016
Cdd:pfam00053 1 CDCNPHG----SLSDTCD----PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1617-1795 |
1.60e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1617 QLAKVNDLLKKA----QDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQnitamvdDKLLNLDNNlt 1692
Cdd:COG1579 18 ELDRLEHRLKELpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-------EQLGNVRNN-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1693 dvmmR-LVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgEGNVNQKAIE 1771
Cdd:COG1579 89 ----KeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE----LAELEAELEE 160
|
170 180
....*....|....*....|....
gi 528517788 1772 MKKEAEDLLKKatMGMETLKKLER 1795
Cdd:COG1579 161 LEAEREELAAK--IPPELLALYER 182
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1261-1828 |
1.90e-07 |
|
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: 56.60 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1261 DKRILELEKKLAQAQelvrdgdreGTFNLISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKELKDLN 1340
Cdd:TIGR02168 273 RLEVSELEEEIEELQ---------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1341 NTLHQLRRELEnyltaGLAEQFANVLKYYQrslNSEQRcnasvygpqspVEQSQDTRNRtealLKDKKDSLLRTATANNK 1420
Cdd:TIGR02168 344 EKLEELKEELE-----SLEAELEELEAELE---ELESR-----------LEELEEQLET----LRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1421 SLSELEGKAHEINRKVHHLSNKVcgghangnvngsceespcGGAGCRGSDGVLKCGGRGCNGTvgasvkaldnaDEVHKN 1500
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEI------------------EELLKKLEEAELKELQAELEEL-----------EEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1501 LTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKD-FLNEEG-------------A 1566
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAlLKNQSGlsgilgvlselisV 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1567 DPE---SIEKV----AQQVL---------AIS----------------------LPVNRTVIVNLVEQIKDSIVNL---- 1604
Cdd:TIGR02168 532 DEGyeaAIEAAlggrLQAVVvenlnaakkAIAflkqnelgrvtflpldsikgteIQGNDREILKNIEGFLGVAKDLvkfd 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1605 TNVEGVFNHTSEQLAKVNDLLKKAQDAK---------TQaDGvsDNINK----TKEALETS------QNAIKKAEEEMST 1665
Cdd:TIGR02168 612 PKLRKALSYLLGGVLVVDDLDNALELAKklrpgyrivTL-DG--DLVRPggviTGGSAKTNssilerRREIEELEEKIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1666 ALKNLKNIQNITAMVDDKLLNLDNNLTDVMMR-------LVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQE 1738
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1739 ELTNAETLYKQLKEKVDSAggtgEGNVNQKAIEMKKEAEDLLKKAtmgmETLKKLERKFNKNEQKMQQQRDELTDLEKNV 1818
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEEL----EAQIEQLKEELKALREALDELR----AELTLLNEEAANLRERLESLERRIAATERRL 840
|
650
....*....|
gi 528517788 1819 TGIREYIRSK 1828
Cdd:TIGR02168 841 EDLEEQIEEL 850
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1089-1129 |
2.64e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.89 E-value: 2.64e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 528517788 1089 QCDKQTGQCPCKQNIIGHNCDQCATNHWNFGSDCgcePCGC 1129
Cdd:pfam00053 12 TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP---PQGC 49
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1489-1829 |
2.87e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 55.99 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1489 KALDNADEVHKNLTAVSEELQTMAKK-----LRDIATLTQTVKTQAKETLDKAQN--KKDMFEKSNKMLKNFiQKIKDFL 1561
Cdd:PTZ00440 659 KSKEDLQTLLNTSKNEYEKLEFMKSDnidniIKNLKKELQNLLSLKENIIKKQLNniEQDISNSLNQYTIKY-NDLKSSI 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1562 NEEGADPESIEKVAQQVLAI------SLPVNRTVIV---NLVEQI---KDSIVNLTN----------------------- 1606
Cdd:PTZ00440 738 EEYKEEEEKLEVYKHQIINRknefilHLYENDKDLPdgkNTYEEFlqyKDTILNKENkisndinilkenkknnqdllnsy 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1607 ---VEGVFNHTSEQLAKVNDLLKK----------AQDAKT--QADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLK 1671
Cdd:PTZ00440 818 nilIQKLEAHTEKNDEELKQLLQKfptedenlnlKELEKEfnENNQIVDNIIKDIENMNKNINIIKTLNIAINRSNSNKQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1672 NIqnitamvdDKLLNLDNNLTDVM---MRLVNLSNGVDllknkteqnremaKEAKAQ-SDNATREAEGLQEELTNA---- 1743
Cdd:PTZ00440 898 LV--------EHLLNNKIDLKNKLeqhMKIINTDNIIQ-------------KNEKLNlLNNLNKEKEKIEKQLSDTkinn 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1744 ------ETL--YKQLKEKVDSAGGTGEgnvnQKAIEMKKEAEDLLKKatmgmetLKKLERKFNKNEQKM----QQQRDEL 1811
Cdd:PTZ00440 957 lkmqieKTLeyYDKSKENINGNDGTHL----EKLDKEKDEWEHFKSE-------IDKLNVNYNILNKKIddliKKQHDDI 1025
|
410
....*....|....*....
gi 528517788 1812 TDL-EKNVTGIREYIRSKV 1829
Cdd:PTZ00440 1026 IELiDKLIKEKGKEIEEKV 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1616-1834 |
3.18e-07 |
|
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: 55.83 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1616 EQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNlknIQNITAMVDDKLLNLdNNLTDVM 1695
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE---VEQLEERIAQLSKEL-TELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1696 MRLVNLSNGVDLLKNKTEQNREmakEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAiEMKKE 1775
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIE---ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA-ATERR 839
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528517788 1776 AEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNN 1834
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1584-1832 |
3.60e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1584 PVNRTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQD----AKTQADGVSDNINKTKEALETSQNAIKKA 1659
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEeleqARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1660 EEEMSTALKNLKNIQnitamvdDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEE 1739
Cdd:COG4372 100 QEELESLQEEAEELQ-------EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1740 LTNAET--LYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKN 1817
Cdd:COG4372 173 LQALSEaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250
....*....|....*
gi 528517788 1818 VTGIREYIRSKVLAY 1832
Cdd:COG4372 253 EEVILKEIEELELAI 267
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1284-1821 |
3.63e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 55.61 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1284 EGTFNLISQTVDDLRAEIALTDGRLmGVIRDLNVTTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENYLTAGLAEQ-- 1361
Cdd:PTZ00440 855 EKEFNENNQIVDNIIKDIENMNKNI-NIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKln 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1362 FANVLKYYQRSLNsEQRCNASVYGPQSPVEQSQDTRNRTEALLKDKKDSLLRTATANNKSLSELEGKAHEINRKVHHLSN 1441
Cdd:PTZ00440 934 LLNNLNKEKEKIE-KQLSDTKINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNILNK 1012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1442 KVcgghaNGNVNGSCEESpcggagCRGSDGVLKCGGRGCNGTVGASVKALD----------NADEVHKNLTAVS-EELQT 1510
Cdd:PTZ00440 1013 KI-----DDLIKKQHDDI------IELIDKLIKEKGKEIEEKVDQYISLLEkmktklssfhFNIDIKKYKNPKIkEEIKL 1081
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1511 MAKKLRDI--------ATLTQtVKTQAKE---TLDKAQNK-KDMFEKSNKMLKNFIQKIKDFLNE-EGADPESIekVAQQ 1577
Cdd:PTZ00440 1082 LEEKVEALlkkidenkNKLIE-IKNKSHEhvvNADKEKNKqTEHYNKKKKSLEKIYKQMEKTLKElENMNLEDI--TLNE 1158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1578 VLAISLPVNRTVIVNLVEQIKDSIV-----------------------------NLTNVE--GVFNHTSEQLAKVNDLLK 1626
Cdd:PTZ00440 1159 VNEIEIEYERILIDHIVEQINNEAKksktimeeiesykkdidqvkknmskerndHLTTFEynAYYDKATASYENIEELTT 1238
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1627 KAQDAKTQADGvSDNINKTK----EALETSQNAIKKAEEeMSTALKNLKNIQNITAMVD------------DKLLNLDNN 1690
Cdd:PTZ00440 1239 EAKGLKGEANR-STNVDELKeiklQVFSYLQQVIKENNK-MENALHEIKNMYEFLISIDsekilkeilnstKKAEEFSND 1316
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1691 LTDVMMRLVNLSNGV--DLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAE-------TLYKQLKEKVDSA---- 1757
Cdd:PTZ00440 1317 AKKELEKTDNLIKQVeaKIEQAKEHKNKIYGSLEDKQIDDEIKKIEQIKEEISNKRkeinkylSNIKSNKEKCDLHvrna 1396
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 1758 --GGTGEGNVNQKAIEMKKEAEDL-LKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGI 1821
Cdd:PTZ00440 1397 srGKDKIDFLNKHEAIEPSNSKEVnIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNI 1463
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1019-1063 |
3.83e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 48.50 E-value: 3.83e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 528517788 1019 CQCNGNIDPQDpeSCDPRTGLCLkCLYNTDGDSCSECKLGYYGNA 1063
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
506-545 |
4.82e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 4.82e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 528517788 506 PCNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1530-1823 |
4.83e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.44 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1530 KETLDKaqNKKDM----FEKSNKMLKNFIQKI----KDFLNEEGADPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDSI 1601
Cdd:TIGR01612 1006 KANLGK--NKENMlyhqFDEKEKATNDIEQKIedanKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINI 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1602 VNLTNVEGVFNH-------TSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIkkaeEEMSTALKNLKNIQ 1674
Cdd:TIGR01612 1084 TNFNEIKEKLKHynfddfgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYI----DEIKAQINDLEDVA 1159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1675 NiTAMVDDkllnldnNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKE-AKAQSDNAT-REAEGLQeeLTNAETLYKQLKE 1752
Cdd:TIGR01612 1160 D-KAISND-------DPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEiAEIEKDKTSlEEVKGIN--LSYGKNLGKLFLE 1229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528517788 1753 KVDSAGGTGEGNVnqKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDL-------EKNVTGIRE 1823
Cdd:TIGR01612 1230 KIDEEKKKSEHMI--KAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhiiskkhDENISDIRE 1305
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1490-1803 |
5.22e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1490 ALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNF---IQKIKDFLNEEGA 1566
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELeedLHKLEEALNDLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1567 D--PESIEKVAQQVLAIslpvnRTVIVNLVEQIKDsivnltnVEGVFN--HTSEQLA--KVNDLLKKAQDAKTQADGVS- 1639
Cdd:TIGR02169 787 RlsHSRIPEIQAELSKL-----EEEVSRIEARLRE-------IEQKLNrlTLEKEYLekEIQELQEQRIDLKEQIKSIEk 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1640 --DNINKTKEALETSQNAIKKAEEEMSTALKNLKNiqnitamvddKLLNLDNNLTDVMMRLVNLSNGVDLLK---NKTEQ 1714
Cdd:TIGR02169 855 eiENLNGKKEELEEELEELEAALRDLESRLGDLKK----------ERDELEAQLRELERKIEELEAQIEKKRkrlSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1715 NREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEgnVNQKAIEMKKEAEDLL-----KKATMGMET 1789
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP--VNMLAIQEYEEVLKRLdelkeKRAKLEEER 1002
|
330
....*....|....
gi 528517788 1790 LKKLERKFNKNEQK 1803
Cdd:TIGR02169 1003 KAILERIEEYEKKK 1016
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1390-1830 |
5.86e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 54.84 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1390 VEQSQDTRNRTE-ALLKDKKDSLLRTATANNKSLSELEGKAHEinrkvhhlsNKVcgghangNVNGSCEESPCGGAGCRG 1468
Cdd:PTZ00440 1067 IKKYKNPKIKEEiKLLEEKVEALLKKIDENKNKLIEIKNKSHE---------HVV-------NADKEKNKQTEHYNKKKK 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1469 SDG-VLKcggrgcngTVGASVKALDNADEVHKNLTAVSE-ELQ-------TMAKKLRDIATLTQTVKTQAKETLDKA-QN 1538
Cdd:PTZ00440 1131 SLEkIYK--------QMEKTLKELENMNLEDITLNEVNEiEIEyerilidHIVEQINNEAKKSKTIMEEIESYKKDIdQV 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1539 KKDMFEKSNKMLKNFiqKIKDFLNEEGADPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDSI-VNLTNVEGVFNHTSEQ 1617
Cdd:PTZ00440 1203 KKNMSKERNDHLTTF--EYNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEIKLQVfSYLQQVIKENNKMENA 1280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1618 LAK---VNDLL----------------KKAQDAKTQADGV---SDNINKTKEA----LETSQNAIKKAEE--EMSTALKN 1669
Cdd:PTZ00440 1281 LHEiknMYEFLisidsekilkeilnstKKAEEFSNDAKKElekTDNLIKQVEAkieqAKEHKNKIYGSLEdkQIDDEIKK 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1670 LKNIQ----NITAMVDDKLLNLDNNLTDVMMRLVNLSNG---VDLLKNKTEQNREMAKEAKAQsdNATREAEGLQEELTN 1742
Cdd:PTZ00440 1361 IEQIKeeisNKRKEINKYLSNIKSNKEKCDLHVRNASRGkdkIDFLNKHEAIEPSNSKEVNII--KITDNINKCKQYSNE 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1743 AETLYKQLKEKVDSAggtgegnvnqkaIEMKKEAEDLLKKAT-MGMETlkKLERKfnkneqkmqqqRDELTDLEKNVTGI 1821
Cdd:PTZ00440 1439 AMETENKADENNDSI------------IKYEKEITNILNNSSiLGKKT--KLEKK-----------KKEATNIMDDINGE 1493
|
....*....
gi 528517788 1822 REYIRSKVL 1830
Cdd:PTZ00440 1494 HSIIKTKLT 1502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1494-1828 |
5.97e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1494 ADEVHKNLTAV---SEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDflNEEGADPES 1570
Cdd:PTZ00121 1485 ADEAKKKAEEAkkkADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK--AEELKKAEE 1562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1571 IEKVAQQVLAISlpvNRTVIVNLVEQIKDsiVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADgvsdNINKTKEALE 1650
Cdd:PTZ00121 1563 KKKAEEAKKAEE---DKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE----ELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1651 TSQNAIKKAEEEMSTA--LKNLKNIQNITAmvddkllnldnnltdvmmrlvnlsngvDLLKNKTEQNREMAKEAKAQSDN 1728
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAeeLKKAEEENKIKA---------------------------AEEAKKAEEDKKKAEEAKKAEED 1686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1729 ATREAEGLQ---EELTNAETLYKQLKEKVDSAGGT-GEGNVNQ-KAIEMKKEAEDLLKKAtmgmETLKKLERKFNKNEQK 1803
Cdd:PTZ00121 1687 EKKAAEALKkeaEEAKKAEELKKKEAEEKKKAEELkKAEEENKiKAEEAKKEAEEDKKKA----EEAKKDEEEKKKIAHL 1762
|
330 340
....*....|....*....|....*.
gi 528517788 1804 MQQQRDELTDLEKNVTG-IREYIRSK 1828
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAvIEEELDEE 1788
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1494-1813 |
6.07e-07 |
|
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: 54.58 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1494 ADEVHKNLTAvSEELQTmaKKLRDIATLTQTVKTQAKETLDKAQNKKDmfEKSNKMLKNFIQKIKDFLNEEGADPESIEK 1573
Cdd:COG5185 252 SDKLEKLVEQ-NTDLRL--EKLGENAESSKRLNENANNLIKQFENTKE--KIAEYTKSIDIKKATESLEEQLAAAEAEQE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1574 VAQQVLAISlpvnrTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQdaktQADGVSDNINKTKEALETSQ 1653
Cdd:COG5185 327 LEESKRETE-----TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSE----ELDSFKDTIESTKESLDEIP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1654 NAIKKAEEEmstalkNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVD-LLKNKTEQNREMAKEAKAQSDNATRE 1732
Cdd:COG5185 398 QNQRGYAQE------ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNeLISELNKVMREADEESQSRLEEAYDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1733 AE-GLQEELTNAETLYKQLKEKVDSAGGTGEGNVNqkaiEMKKEAEDLLKKATMGMETLKKLERK---FNKNEQKMQQQR 1808
Cdd:COG5185 472 INrSVRSKKEDLNEELTQIESRVSTLKATLEKLRA----KLERQLEGVRSKLDQVAESLKDFMRArgyAHILALENLIPA 547
|
....*
gi 528517788 1809 DELTD 1813
Cdd:COG5185 548 SELIQ 552
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
910-952 |
7.42e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.42e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528517788 910 CQCN---SHAESCDPESGACyDCRDNTAGQLCERCVDGYYGNPALG 952
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
507-545 |
7.71e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 7.71e-07
10 20 30
....*....|....*....|....*....|....*....
gi 528517788 507 CNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
959-1014 |
8.60e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 8.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517788 959 PCPCPGHPdsghSNGASCevDYASNQilCQCGQGYAGPRCDRCAPGYYGDPEHPGG 1014
Cdd:cd00055 1 PCDCNGHG----SLSGQC--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1663-1829 |
1.39e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1663 MSTALKNLKNIQNItamvDDKLLNLDNNLTDVMMRLVNLsngvdllKNKTEQNREMAKEAKAQSDNATREAEGLQEELTN 1742
Cdd:COG1579 2 MPEDLRALLDLQEL----DSELDRLEHRLKELPAELAEL-------EDELAALEARLEAAKTELEDLEKEIKRLELEIEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1743 AETLYKQLKEKVDSAGGTGEGNVNQKAIEM----KKEAEDLLKKAtmgMETLKKLERKFNKNEQKMQQQRDELTDLEKNV 1818
Cdd:COG1579 71 VEARIKKYEEQLGNVRNNKEYEALQKEIESlkrrISDLEDEILEL---MERIEELEEELAELEAELAELEAELEEKKAEL 147
|
170
....*....|.
gi 528517788 1819 TGIREYIRSKV 1829
Cdd:COG1579 148 DEELAELEAEL 158
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1070-1120 |
1.42e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 1.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 528517788 1070 RCTCVTAGTLPNsctdgvcQCDKQTGQCPCKQNIIGHNCDQCATNHWNFGS 1120
Cdd:cd00055 1 PCDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1489-1648 |
1.52e-06 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 51.99 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIAT-----LTQTVKTQAKETLDKAQNK-KDMFEKSNKMLKNFIQKIKDFLN 1562
Cdd:cd22656 132 KYQDKAAKVVDKLTDFENQTEKDQTALETLEKalkdlLTDEGGAIARKEIKDLQKElEKLNEEYAAKLKAKIDELKALIA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1563 EEGADPESIEKVAQQVLAISlpvnrTVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQD-------AKTQA 1635
Cdd:cd22656 212 DDEAKLAAALRLIADLTAAD-----TDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISkipaailAKLEL 286
|
170
....*....|...
gi 528517788 1636 DGVSDNINKTKEA 1648
Cdd:cd22656 287 EKAIEKWNELAEK 299
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
267-320 |
1.69e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.58 E-value: 1.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 267 SCFCYGHAS---ECAPVpgvttrdsgmiHGRCVCKHNTVGLNCERCRDFYHDAPWRP 320
Cdd:cd00055 1 PCDCNGHGSlsgQCDPG-----------TGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1541-1813 |
1.76e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.13 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1541 DMFEK---SNKMLKNFIQkikdfLNEEGADPESieKVAQQVLAiSLPVNRTVIVNLVEQIKDsivNLTNVEGVFNHTSEQ 1617
Cdd:TIGR00606 380 DGFERgpfSERQIKNFHT-----LVIERQEDEA--KTAAQLCA-DLQSKERLKQEQADEIRD---EKKGLGRTIELKKEI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1618 LAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMS--TALKNLKNIQNITAMVDDKLLNLDNNLTDVM 1695
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLteTLKKEVKSLQNEKADLDRKLRKLDQEMEQLN 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1696 MRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEkvdsaggtgegnvnqkaiemKKE 1775
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKE--------------------INQ 588
|
250 260 270
....*....|....*....|....*....|....*...
gi 528517788 1776 AEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTD 1813
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1018-1069 |
2.02e-06 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 46.19 E-value: 2.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 528517788 1018 PCQCNGNIDPqdPESCDPRTGLCLkCLYNTDGDSCSECKLGYYGNALI-QDCR 1069
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1488-1817 |
2.77e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1488 VKALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKtQAKETLDKAQNKKDMFEKSNKM------LKNFIQKIKDFL 1561
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELyeeakaKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1562 NeegadPESIEKVAQQVLAISlpvnrtvivNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQD------AKTQA 1635
Cdd:PRK03918 382 T-----GLTPEKLEKELEELE---------KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgRELTE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1636 DGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMvDDKLLNLdNNLTDVMMRLVNLSNGVDL--LKNKTE 1713
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKL-KELAEQLKELEEKLKKYNLeeLEKKAE 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1714 QNREMAKEA---KAQSDNATREAEGLQE----------ELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEM-------- 1772
Cdd:PRK03918 526 EYEKLKEKLiklKGEIKSLKKELEKLEElkkklaelekKLDELEEELAELLKELEELGFESVEELEERLKELepfyneyl 605
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 528517788 1773 -----KKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKN 1817
Cdd:PRK03918 606 elkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1262-1834 |
2.89e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1262 KRILELEKKLAQAQELVRDgdREGTFNLISQtvddLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKELKDLNn 1341
Cdd:PRK03918 214 SELPELREELEKLEKEVKE--LEELKEEIEE----LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1342 tlhQLRRELENYLTagLAEQFANVLKYYQRSLNSEQRCNASVYGPQSPVEQSQDTRNRTEALLKDKKDSLlrtatannKS 1421
Cdd:PRK03918 287 ---ELKEKAEEYIK--LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE--------KR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1422 LSELEGKAHEINRKVHHLSNKvcgghangnvngsceespcggagcrgsDGVLKcggRGCNGTVGASVKALDnadEVHKNL 1501
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEEL---------------------------ERLKK---RLTGLTPEKLEKELE---ELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1502 TAVSEELQTMAKKLRDIATLTQTVKTqAKETLDKAQNK-------------KDMFEKSNKMLKNFIQKIKDFLNEEgadp 1568
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKK-AIEELKKAKGKcpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKE---- 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1569 ESIEKVAQQVlAISLPVNRTVIVN--LVEQIKdsivnltNVEgvfnhtsEQLAKVNdlLKKAQDAKTQADgvsdninKTK 1646
Cdd:PRK03918 476 RKLRKELREL-EKVLKKESELIKLkeLAEQLK-------ELE-------EKLKKYN--LEELEKKAEEYE-------KLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1647 EALETSQNAIKKAEEEmstaLKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNG-VDLLKNKTEQNREMAK---EA 1722
Cdd:PRK03918 532 EKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNeylEL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1723 KaqsdNATREAEGLQEELtnaetlyKQLKEKVDSAggTGEGNVNQKAIEM-KKEAEDLLKKATMgmETLKKLERKFNKNE 1801
Cdd:PRK03918 608 K----DAEKELEREEKEL-------KKLEEELDKA--FEELAETEKRLEElRKELEELEKKYSE--EEYEELREEYLELS 672
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528517788 1802 ----------QKMQQQRDE----LTDLEKNVTGIREY----------------IRSKVLAYNN 1834
Cdd:PRK03918 673 relaglraelEELEKRREEikktLEKLKEELEEREKAkkeleklekalerveeLREKVKKYKA 735
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1488-1825 |
3.48e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.36 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1488 VKALDNadEVHKNLTAVSE----------ELQTMAKKLRDIATLT------QTVKTQAKETLDKAQNKKDMFEKSNKMLk 1551
Cdd:TIGR01612 1120 IKNLDQ--KIDHHIKALEEikkksenyidEIKAQINDLEDVADKAisnddpEEIEKKIENIVTKIDKKKNIYDEIKKLL- 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1552 NFIQKIKDflneegaDPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDS-----------------------IVNLTNVE 1608
Cdd:TIGR01612 1197 NEIAEIEK-------DKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSehmikameayiedldeikekspeIENEMGIE 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1609 GVFNHTSEQLAKVNDLLKKAQD-AKTQADGVSD----------------NINKTKEALETSQNAIKKAEEEMSTALKNLK 1671
Cdd:TIGR01612 1270 MDIKAEMETFNISHDDDKDHHIiSKKHDENISDirekslkiiedfseesDINDIKKELQKNLLDAQKHNSDINLYLNEIA 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1672 NIQNItamvddkllnldnnltdvmMRLVNLSNGVDLLKNKTEQNREMAKEAKaqsdnatreaeglqEELTNAETLYKQLK 1751
Cdd:TIGR01612 1350 NIYNI-------------------LKLNKIKKIIDEVKEYTKEIEENNKNIK--------------DELDKSEKLIKKIK 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1752 EKV--DSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMET-------------------LKKLERKFNKNEQKMQQQRDE 1810
Cdd:TIGR01612 1397 DDInlEECKSKIESTLDDKDIDECIKKIKELKNHILSEESnidtyfknadennenvlllFKNIEMADNKSQHILKIKKDN 1476
|
410
....*....|....*.
gi 528517788 1811 LT-DLEKNVTGIREYI 1825
Cdd:TIGR01612 1477 ATnDHDFNINELKEHI 1492
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1487-1823 |
3.63e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.53 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1487 SVKALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKaQNKKDMfEKSNKMLKNFIQKIKDflneEGA 1566
Cdd:PTZ00440 2032 SVKTLKASENIKKIVENKKTSIDAINTNIEDIEKEIESINPSLDELLKK-GHKIEI-SRYTSIIDNVQTKISN----DSK 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1567 DPESIEKVAQQVLAiSLPVNRTVIVNLVEQI-----KDSIVN--LTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVS 1639
Cdd:PTZ00440 2106 NINDIEKKAQIYLA-YIKNNYNSIKKDISTLneyfdEKQVSNyiLTNIDKANKLSSELSEAVTNSEEIIENIKKEIIEIN 2184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1640 DN-----INKTKEALETSQNAIKKAE---------------EEM----------STALKN---------------LKNIQ 1674
Cdd:PTZ00440 2185 ENtemntLENTADKLKELYENLKKKKniinniykkinfiklQEIenssekyndiSKLFNNvvetqkkklldnknkINNIK 2264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1675 NITAMVDDKLLNLDNNLTDVMMRLVNlsNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKV 1754
Cdd:PTZ00440 2265 DKINDKEKELINVDSSFTLESIKTFN--EIYDDIKSNIGDLYKLEDTNNDELKKVKLYIENITHLLNRINTLINDLDNYQ 2342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528517788 1755 DsaggtgEGNVNQKAIEMKKEAEDLLKKATmgmETLKKLERKFNKNEQKMQQQ---------RDELTDLEKNVTGIRE 1823
Cdd:PTZ00440 2343 D------ENYGKDKNIELNNENNSYIIKTK---EKINNLKEEFSKLLKNIKRNntlcnnnniKDFISNIGKSVETIKQ 2411
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1071-1118 |
4.29e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.38 E-value: 4.29e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 528517788 1071 CTCVTAGTLPNsctdgvcQCDKQTGQCPCKQNIIGHNCDQCATNHWNF 1118
Cdd:smart00180 1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYGD 41
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1768-1836 |
4.90e-06 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 45.90 E-value: 4.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517788 1768 KAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNCQ 1836
Cdd:cd22299 4 KAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTCQ 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1492-1811 |
9.47e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1492 DNADEVHKNLtavsEELQTMAKK----------LRDI-ATLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDF 1560
Cdd:TIGR02168 193 DILNELERQL----KSLERQAEKaerykelkaeLRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1561 LNE-EGADPESIEKVAQQ---VLAISLPVNRtvivnLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQAD 1636
Cdd:TIGR02168 269 LEElRLEVSELEEEIEELqkeLYALANEISR-----LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1637 GVSDNINKTKEALETSQNAIKKAEEEMSTALKNLkniqnitamvDDKLLNLDNNLTDvmmrlvnLSNGVDLLKNKTEQNR 1716
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEEL----------EEQLETLRSKVAQ-------LELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1717 EMAKEAKAQSDNATREAEGLQEELTNAEtlYKQLKEKVDsaggtgegnvnqkaiEMKKEAEDLLKKATMGMETLKKLERK 1796
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELE---------------ELEEELEELQEELERLEEALEELREE 469
|
330
....*....|....*
gi 528517788 1797 FNKNEQKMQQQRDEL 1811
Cdd:TIGR02168 470 LEEAEQALDAAEREL 484
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
332-384 |
1.48e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.88 E-value: 1.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517788 332 CNCNGH---SNQCHFDmavylatgnvsGGVCNnCLHNTMGRNCESCKPFYYQDPEK 384
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
507-545 |
1.85e-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: 1.85e-05
10 20 30
....*....|....*....|....*....|....*....
gi 528517788 507 CNCDFGGATSSRCMMDSGQCDCRPHLIGRQCSEVQPAFF 545
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1767-1835 |
2.19e-05 |
|
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) and similar proteins; DmLAMB1, also called LanB1, is a glycoprotein required for nidogen (Ndg) localization to the basement membrane. It is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of DmLAMB1, which may be involved in the integrin binding activity.
Pssm-ID: 411973 [Multi-domain] Cd Length: 70 Bit Score: 44.15 E-value: 2.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517788 1767 QKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSKVLAYNNC 1835
Cdd:cd22302 2 ERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1516-1833 |
2.66e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1516 RDIATLTQTVKTQAKETLDKAQNKKDMFEKSNKMlKNFIQKIKDFLNEEGADPESIEKVAQQVLAISLPVNRTV------ 1589
Cdd:TIGR01612 751 KDLNKILEDFKNKEKELSNKINDYAKEKDELNKY-KSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTIsikede 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1590 ---IVNLVEQIKDSIVNLTNV---------EGVfNHTSEQLAKVNDLLKkAQDAKTQADGVSDNINKTKEALETSQNAIK 1657
Cdd:TIGR01612 830 ifkIINEMKFMKDDFLNKVDKfinfennckEKI-DSEHEQFAELTNKIK-AEISDDKLNDYEKKFNDSKSLINEINKSIE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1658 KAEEEMSTalknLKNIqnitamvdDKLLNLDNNLTDvmmRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEG-L 1736
Cdd:TIGR01612 908 EEYQNINT----LKKV--------DEYIKICENTKE---SIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNtL 972
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1737 QEELTNAETLYKqlkekvDSAGGTGEGNVNqkaiEMKKEAEDLlkKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:TIGR01612 973 IDKINELDKAFK------DASLNDYEAKNN----ELIKYFNDL--KANLGKNKENMLYHQFDEKEKATNDIEQKIEDANK 1040
|
330
....*....|....*..
gi 528517788 1817 NVTGIREYIRSKVlaYN 1833
Cdd:TIGR01612 1041 NIPNIEIAIHTSI--YN 1055
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1707-1823 |
3.48e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1707 LLKNKTE-QNREMAKEAKAQSDNATREAEGLQEE-LTNAETLYKQLKEKVdsaggtgEGNVNQKAIEMKK------EAED 1778
Cdd:PRK12704 24 VRKKIAEaKIKEAEEEAKRILEEAKKEAEAIKKEaLLEAKEEIHKLRNEF-------EKELRERRNELQKlekrllQKEE 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 528517788 1779 LLKKAtmgMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIRE 1823
Cdd:PRK12704 97 NLDRK---LELLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| OspD |
pfam03207 |
Borrelia outer surface protein D (OspD); |
1603-1793 |
3.52e-05 |
|
Borrelia outer surface protein D (OspD);
Pssm-ID: 367392 [Multi-domain] Cd Length: 254 Bit Score: 47.54 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1603 NLTNVEGVF-------NHTSEQ---LAKVNDLLKKAQDAKTQADGVSDNIN------KTKEALETSQNAIKKAEEEMSTA 1666
Cdd:pfam03207 32 NLNNQKGYLdnegansNYESKKqsiLSELNQLLKQTTNSLKEAKNTTDNLNasneanKVVEAVINAVNLISSAADQVKSA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1667 LKNLKNIQNITAMVDDKLlnldNNLTDVMMRLVNLSNGVDLLKNKTEQN-----REMAK--EAKAQSD------------ 1727
Cdd:pfam03207 112 TKNMHDLAQMAEIDLEKI----KNSSDKAIFASNLAKEAYSLTKAAEQNmqklyKEQQKisESESESDysdsaeikqake 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528517788 1728 ------NATREAeglQEELTNAETLYKQLKEKVDSaggtgEGNVNQKAIEMKKEAEDLLKKATMGMETLKKL 1793
Cdd:pfam03207 188 aveiawKATVEA---KDKLIDVENTVKETLDKIKT-----ETTNNTKLADIKEAAELVLQIAKNAKEIVQEV 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1567-1820 |
3.69e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1567 DPESIEKVAQQVLAIslpvnrtvivnlvEQIKDSIVNLTNVEGVFNHTSEQLAK-------VNDLLKKAQDAKTQadgVS 1639
Cdd:PRK03918 143 SDESREKVVRQILGL-------------DDYENAYKNLGEVIKEIKRRIERLEKfikrtenIEELIKEKEKELEE---VL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1640 DNINKTKEALETSQNAIKKAEEEmstaLKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMA 1719
Cdd:PRK03918 207 REINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1720 KEAK-------------AQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgeGNVNQKAIEMKKEAEDLLKKatmg 1786
Cdd:PRK03918 283 KELKelkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL-----EEKEERLEELKKKLKELEKR---- 353
|
250 260 270
....*....|....*....|....*....|....
gi 528517788 1787 METLKKLERKFNKNEQKMqqqrDELTDLEKNVTG 1820
Cdd:PRK03918 354 LEELEERHELYEEAKAKK----EELERLKKRLTG 383
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1488-1821 |
3.92e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.29 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1488 VKALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQN-KKDMFEKS----------NKMLKNFIQK 1556
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElRKSLLANRfsfgpaldelEKQLENLEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1557 IKDF--LNEEGaDP----ESIEKVAQQVLAISlpvnrtvivNLVEQIKDSIVNLTNVegvFnhtSEQLAKVNDLLKKAQD 1630
Cdd:PRK04778 181 FSQFveLTESG-DYvearEILDQLEEELAALE---------QIMEEIPELLKELQTE---L---PDQLQELKAGYRELVE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1631 AKTQADgvSDNINKTkeaLETSQNAIKKAEEEMSTaLKnLKNIQNITAMVDDKLlnldNNLTDVMMRLV--------NLS 1702
Cdd:PRK04778 245 EGYHLD--HLDIEKE---IQDLKEQIDENLALLEE-LD-LDEAEEKNEEIQERI----DQLYDILEREVkarkyvekNSD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1703 NGVDLLKNKTEQNREMAKEAK--AQS----DNATREAEGLQEELTNAETLYKQLKEKVDsaggtgEGNV-------NQKA 1769
Cdd:PRK04778 314 TLPDFLEHAKEQNKELKEEIDrvKQSytlnESELESVRQLEKQLESLEKQYDEITERIA------EQEIayselqeELEE 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528517788 1770 I-----EMKKEAEDLLkkatmgmETLKKLERKFNKNEQKMQQQRDELTD----LEK-NVTGI 1821
Cdd:PRK04778 388 IlkqleEIEKEQEKLS-------EMLQGLRKDELEAREKLERYRNKLHEikryLEKsNLPGL 442
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1676-1827 |
4.49e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1676 ITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNA-----------E 1744
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArseleqleeelE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1745 TLYKQLKEKVDSAGGTGE--GNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIR 1822
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEelESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
....*
gi 528517788 1823 EYIRS 1827
Cdd:COG4372 164 EELAA 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1245-1436 |
7.50e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1245 DIIAMILEKGEVpgvsdkRILELEKKLAQAQELVRDGDREGTFNL--ISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHN 1322
Cdd:COG4372 2 DRLGEKVGKARL------SLFGLRPKTGILIAALSEQLRKALFELdkLQEELEQLREELEQAREELEQLEEELEQARSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1323 NDLKQNLTALEKELKDLNNTLHQLRRELENyltaglAEQFANVLKYYQRSLNSEQrcnasvygpqspvEQSQDTRNRtea 1402
Cdd:COG4372 76 EQLEEELEELNEQLQAAQAELAQAQEELES------LQEEAEELQEELEELQKER-------------QDLEQQRKQ--- 133
|
170 180 190
....*....|....*....|....*....|....
gi 528517788 1403 lLKDKKDSLLRTATANNKSLSELEGKAHEINRKV 1436
Cdd:COG4372 134 -LEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
332-382 |
7.60e-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: 41.96 E-value: 7.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 528517788 332 CNCNGH---SNQCHFdmavylatgnvSGGVCNnCLHNTMGRNCESCKPFYYQDP 382
Cdd:pfam00053 1 CDCNPHgslSDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
1689-1807 |
8.09e-05 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 45.01 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1689 NNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQ-LKEKVDSAggtgegnvnQ 1767
Cdd:cd13769 15 NNLAQQVQKQLGLQNPEEVVNTLKEQSDNFANNLQEVSSSLKEEAKKKQGEVEEAWNEFKTkLSETVPEL---------R 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 528517788 1768 KAIEMKKEAEDLLKKATMGMETL----KKLERKFNKNEQKMQQQ 1807
Cdd:cd13769 86 KSLPVEEKAQELQAKLQSGLQTLvtesQKLAKAISENSQKAQEE 129
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1593-1828 |
8.75e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1593 LVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKA----QDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALK 1668
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALarriRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1669 NLKNIQNITAMvddKLLNLDNNLTDVMMRLvnlsngvDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYK 1748
Cdd:COG4942 112 ALYRLGRQPPL---ALLLSPEDFLDAVRRL-------QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1749 QLKEKvdsaggtgegnvnQKAIEMKKEAEDllkkatmgmETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIREYIRSK 1828
Cdd:COG4942 182 ELEEE-------------RAALEALKAERQ---------KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1252-1442 |
1.06e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1252 EKGEVPGVSDkRILELEKKLA--------------QAQELVRDGDREgtFNLISQTVDDLRAEIALTDGRLMGVIRDLNV 1317
Cdd:TIGR02169 672 EPAELQRLRE-RLEGLKRELSslqselrrienrldELSQELSDASRK--IGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1318 TTDHNNDLKQNLTALEKELKDLNNTLHQLRRELENyLTAGLAEQF-------ANVLKYYQRSLNS-----EQRCNASVYG 1385
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALND-LEARLSHSRipeiqaeLSKLEEEVSRIEArlreiEQKLNRLTLE 827
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 1386 PQSPVEQSQDTRNRTEAlLKDKKDSLLRTATANNKSLSELEGKAHEINRKVHHLSNK 1442
Cdd:TIGR02169 828 KEYLEKEIQELQEQRID-LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1616-1826 |
1.09e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1616 EQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQnaikkaeeEMSTALKNLkniqnitAMVDDKLLNLDNNLTdvm 1695
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLA--------EYSWDEIDV-------ASAEREIAELEAELE--- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1696 mRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGEGNVNQKAIEMKKE 1775
Cdd:COG4913 679 -RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528517788 1776 A--EDLLKKAtmgmetLKKLERKFNKNEQKMQQQRDELTDLeknvtgIREYIR 1826
Cdd:COG4913 758 AlgDAVEREL------RENLEERIDALRARLNRAEEELERA------MRAFNR 798
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1546-1833 |
1.74e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1546 SNKMLKNFIQKIKD-FLNE----EG-------ADPESIEKVAQQVLAI-SLPVNRTVIVNLVEQIKDSIVNLTNVEGVFN 1612
Cdd:PRK01156 114 TKYIEKNILGISKDvFLNSifvgQGemdslisGDPAQRKKILDEILEInSLERNYDKLKDVIDMLRAEISNIDYLEEKLK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1613 HTSEQLAKVNDLLkkAQDAKTQADgvsdnINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLT 1692
Cdd:PRK01156 194 SSNLELENIKKQI--ADDEKSHSI-----TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1693 DVMMRLVNlsngvdlLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNaetlYKQLKEKVDSAGGTGEGNVNQKA--- 1769
Cdd:PRK01156 267 MELEKNNY-------YKELEERHMKIINDPVYKNRNYINDYFKYKNDIEN----KKQILSNIDAEINKYHAIIKKLSvlq 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1770 ------IEMKKEAEDLLKK-------------ATMGMETLKKLERKFNKNEQKMQQQRDELTDLE----KNVTGIREYIR 1826
Cdd:PRK01156 336 kdyndyIKKKSRYDDLNNQilelegyemdynsYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpDAIKKELNEIN 415
|
....*..
gi 528517788 1827 SKVLAYN 1833
Cdd:PRK01156 416 VKLQDIS 422
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
960-1012 |
1.80e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 1.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 528517788 960 CPCpghpDSGHSNGASCEVDYasnqILCQCGQGYAGPRCDRCAPGYYGDPEHP 1012
Cdd:smart00180 1 CDC----DPGGSASGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1621-1751 |
1.98e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 45.44 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1621 VNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMvddkllnldnnltdvmmrlvn 1700
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIARKEI--------------------- 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 528517788 1701 lsngVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLK 1751
Cdd:cd22656 182 ----KDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1546-1757 |
2.80e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 45.10 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1546 SNKMLKnFIQKIKDFLNEEGA-----DPESIEKVAQQV--------LAISLPVNRTVIVN-LVEQIKDSIVNLTNVEG-- 1609
Cdd:TIGR04320 118 TEGSLD-FAQAVAKAYKKDNSgtgghDETAINKAAAENgldntyenLGSISSNNENTTMDdLKRAIYDSILGMLFNDAds 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1610 VFNHTsEQLAKVNDLLKKA------QDAK--------TQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQN 1675
Cdd:TIGR04320 197 NWGHA-QNLLGDDKINAGAylgvsiSNDGgvtihfvnFNDSYIADGNKFDKTPIPNPPNSLAALQAKLATAQADLAAAQT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1676 ITAMVDDKLLNLDNNLTDvmmrlvnlsngvdLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVD 1755
Cdd:TIGR04320 276 ALNTAQAALTSAQTAYAA-------------AQAALATAQKELANAQAQALQTAQNNLATAQAALANAEARLAKAKEALA 342
|
..
gi 528517788 1756 SA 1757
Cdd:TIGR04320 343 NL 344
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1641-1827 |
2.94e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1641 NINKTKEALETSQNAIKKAEEEMstalKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSngvDLLKNKTEQNREMAK 1720
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIKEKEKELEEVLREINEIS---SELPELREELEKLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1721 EAKaqsdnatrEAEGLQEELTNAEtlyKQLKEKVDSAGGTGEGNVN-QKAIEMKKEAEDLLKKATMGMETLKKLERKFNK 1799
Cdd:PRK03918 229 EVK--------ELEELKEEIEELE---KELESLEGSKRKLEEKIRElEERIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
170 180
....*....|....*....|....*...
gi 528517788 1800 NEQKMQQQRDELTDLEKNVTGIREYIRS 1827
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEING 325
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1626-1771 |
3.15e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.38 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1626 KKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQN---ITAMVDDKLLNLDNNLTDVMMRLVNLS 1702
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKpadTSSPKEDKQVAENQKREIEKAQIEIKK 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528517788 1703 NGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAGGTGegnvNQKAIE 1771
Cdd:pfam05262 293 NDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSL----NEDAID 357
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1618-1816 |
4.05e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1618 LAKVNDLLK-KAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMS-----------TALKNLKNIQNITAMVDDKLL 1685
Cdd:PHA02562 165 LSEMDKLNKdKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGeniarkqnkydELVEEAKTIKAEIEELTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1686 NLDNNLTDVMMRLVNLSNGVDLLKNKTEQnreMAKEAKAQSDNA-----TREAEGLQEELTNAETLYKQLKEKVDSAggt 1760
Cdd:PHA02562 245 NLVMDIEDPSAALNKLNTAAAKIKSKIEQ---FQKVIKMYEKGGvcptcTQQISEGPDRITKIKDKLKELQHSLEKL--- 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528517788 1761 gegnvnQKAIEMKKEAEDLLKKATMgmeTLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:PHA02562 319 ------DTAIDELEEIMDEFNEQSK---KLLELKNKISTNKQSLITLVDKAKKVKA 365
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
1550-1745 |
5.60e-04 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 42.31 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1550 LKNFIQKIKDFLNEegadpesiekVAQQVL-AISLPVNRTVivnlVEQIKDsivnltNVEGVFNHTSEQLAKVNDLLKKA 1628
Cdd:cd13769 3 LSELIQKAQEAINN----------LAQQVQkQLGLQNPEEV----VNTLKE------QSDNFANNLQEVSSSLKEEAKKK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1629 Q-DAKTQADGVSDNINKTKEALETSQNAIKKAEEemstalknlknIQNitamvddkllNLDNNLTDVMMRLVNLSNGVDl 1707
Cdd:cd13769 63 QgEVEEAWNEFKTKLSETVPELRKSLPVEEKAQE-----------LQA----------KLQSGLQTLVTESQKLAKAIS- 120
|
170 180 190
....*....|....*....|....*....|....*...
gi 528517788 1708 lKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAET 1745
Cdd:cd13769 121 -ENSQKAQEELQKATKQAYDIAVEAAQNLQNQLQTATQ 157
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
332-385 |
6.78e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.22 E-value: 6.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 528517788 332 CNCNG---HSNQCHFDmavylatgnvsGGVCNnCLHNTMGRNCESCKPFYYQDPEKD 385
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1675-1810 |
7.75e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1675 NITAMVDDKLLN--LDNNLTDVMMRlvnlSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEEL----TNAETLYK 1748
Cdd:pfam05262 173 DTDSISDKKVVEalREDNEKGVNFR----RDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKAdfaqDNADKQRD 248
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528517788 1749 QLKEKVDSA------GGTGEGNVNQK-AIEMKKEAEDLLKKATMGMETLKKLE-------RKFNKNEQKMQQQRDE 1810
Cdd:pfam05262 249 EVRQKQQEAknlpkpADTSSPKEDKQvAENQKREIEKAQIEIKKNDEEALKAKdhkafdlKQESKASEKEAEDKEL 324
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1261-1439 |
8.57e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1261 DKRILELEKKLAQAQELVRDGDREGT-----FNLISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKE 1335
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTeleaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1336 LKDLNNTLHQLRRELENYLT-AGLAEQFANVLKyYQRSLNSEQ--RCNASVYGPQSPVEQSQDTRNRtealLKDKKDSLL 1412
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERrIAATERRLEDLE-EQIEELSEDieSLAAEIEELEELIEELESELEA----LLNERASLE 886
|
170 180
....*....|....*....|....*..
gi 528517788 1413 RTATANNKSLSELEGKAHEINRKVHHL 1439
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSEL 913
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
292-318 |
9.75e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.45 E-value: 9.75e-04
10 20
....*....|....*....|....*..
gi 528517788 292 HGRCVCKHNTVGLNCERCRDFYHDAPW 318
Cdd:smart00180 17 TGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1709-1815 |
1.06e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.95 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1709 KNKTEQNREM-AKEAKAQSdnATREAEGLQEELtnaetlyKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGM 1787
Cdd:cd16269 191 QALTEKEKEIeAERAKAEA--AEQERKLLEEQQ-------RELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERAL 261
|
90 100 110
....*....|....*....|....*....|
gi 528517788 1788 ETLKKLERKFNK--NEQKMQQQRDELTDLE 1815
Cdd:cd16269 262 ESKLKEQEALLEegFKEQAELLQEEIRSLK 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1261-1442 |
1.19e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1261 DKRILELEKKLAQAQELVRD-------GDREGTFNLISQTVDDLRAEIALTDGRLmgvirdlnvttdhnNDLKQNLTALE 1333
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEfrqknglVDLSEEAKLLLQQLSELESQLAEARAEL--------------AEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1334 KELKDLNNTLHQLrreLENYLTAGLAEQFANVlkyyQRSLNSEQrcnaSVYGPQSP-VEQSQDTRNRTEALLKDKKDSLL 1412
Cdd:COG3206 247 AQLGSGPDALPEL---LQSPVIQQLRAQLAEL----EAELAELS----ARYTPNHPdVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190
....*....|....*....|....*....|....
gi 528517788 1413 RTATANNKSL----SELEGKAHEINRKVHHLSNK 1442
Cdd:COG3206 316 ASLEAELEALqareASLQAQLAQLEARLAELPEL 349
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1262-1442 |
1.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1262 KRILELEKKLAQAQELVRDGDREgtFNLISQTVDDLRAEIALTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKELKDLNN 1341
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEE--LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1342 TLHQLRRE---LENYLTAGLAEQFANVLKYYQRSLNSEQRCNASVYGPQSPVEQSQDTRNRTEALLKDKKDSLLRTATAN 1418
Cdd:COG4372 158 QLESLQEElaaLEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
170 180
....*....|....*....|....
gi 528517788 1419 NKSLSELEGKAHEINRKVHHLSNK 1442
Cdd:COG4372 238 LLDALELEEDKEELLEEVILKEIE 261
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1489-1806 |
1.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1489 KALDNADEVHKNLTAVSEELQTMAKKLRDIATLTQTVKT---QAKETLDKAQNKKDMFEKSNKMLKN---FIQKIKDFLN 1562
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAelaQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1563 EEGADPESIEKVAQQVLAiSLpvnRTVIVNLVEQIKDSIVNLTNVEgvfnhTSEQLAKVNDLLKKAQDAKTQAdgvsdNI 1642
Cdd:COG4372 136 AQIAELQSEIAEREEELK-EL---EEQLESLQEELAALEQELQALS-----EAEAEQALDELLKEANRNAEKE-----EE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1643 NKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEA 1722
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1723 KAQSDNATREAEGLQEEltnaetlYKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQ 1802
Cdd:COG4372 282 ALELEALEEAALELKLL-------ALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
....
gi 528517788 1803 KMQQ 1806
Cdd:COG4372 355 VLEL 358
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1505-1829 |
1.45e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1505 SEELQTMAKKLRDIATLTQTVKTQAKETLDkaqNKKDMFEKsnkmlkNFIQK-IKDFLNEEGADPESIEKVAQQVLAISl 1583
Cdd:PTZ00440 260 SNNYDNYLNRAKELLESGSDLINKIKKELG---DNKTIYSI------NFIQEeIGDIIKRYNFHLKKIEKGKEYIKRIQ- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1584 PVNRTVIVNLVEqIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQ------------DAKTQADGVSDN---------- 1641
Cdd:PTZ00440 330 NNNIPPQVKKDE-LKKKYFESAKHYASFKFSLEMLSMLDSLLIKKEkilnnlfnklfgDLKEKIETLLDSeyfiskytni 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1642 INKTKEALETSQNAIKKAEEEMS--TALKNLKnIQNITAMVDDKLLNLDNNLTDVMMRLVNLSNGVDLlkNKTEQNREMA 1719
Cdd:PTZ00440 409 ISLSEHTLKAAEDVLKENSQKIAdyALYSNLE-IIEIKKKYDEKINELKKSINQLKTLISIMKSFYDL--IISEKDSMDS 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1720 KEAKAQSDNATreaeglQEELTNAETLYKQLKEKVdsaggtgeGNVNQKAIEMKKEAEDLlkkatmgmETLKKLERKFNK 1799
Cdd:PTZ00440 486 KEKKESSDSNY------QEKVDELLQIINSIKEKN--------NIVNNNFKNIEDYYITI--------EGLKNEIEGLIE 543
|
330 340 350
....*....|....*....|....*....|
gi 528517788 1800 NEQKMQQQRDELTDLEKNVTGIREYIRSKV 1829
Cdd:PTZ00440 544 LIKYYLQSIETLIKDEKLKRSMKNDIKNKI 573
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1261-1373 |
1.54e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1261 DKRILELEKKLAQAQELVRDGDRegtfnlISQTVDDLRAEIA-LTDGRLMGVIRDLNVTTDHNNDLKQNLTALEKELKDL 1339
Cdd:COG4717 145 PERLEELEERLEELRELEEELEE------LEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
90 100 110
....*....|....*....|....*....|....
gi 528517788 1340 NNTLHQLRRELENYLTAGLAEQFANVLKYYQRSL 1373
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1616-1823 |
1.77e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1616 EQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNitamvddkllnldnnltdvm 1695
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-------------------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1696 mRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgegnvNQKAIEMKKE 1775
Cdd:COG1196 296 -ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--------EAELAEAEEA 366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528517788 1776 AEDLLKKATMGMETLKKLERKFNKNEQKMQQQRDELTDLEKNVTGIRE 1823
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1616-1816 |
2.20e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1616 EQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVM 1695
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1696 MRLVNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAEGLQEELTNAETLYKQLKEKVDSAggtgegnvNQKAIEMKKE 1775
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL--------AEELLEALRA 394
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 528517788 1776 AEDLLKKATmgmETLKKLERKFNKNEQKMQQQRDELTDLEK 1816
Cdd:COG1196 395 AAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
291-322 |
2.24e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.72 E-value: 2.24e-03
10 20 30
....*....|....*....|....*....|..
gi 528517788 291 IHGRCVCKHNTVGLNCERCRDFYHDAPWRPAE 322
Cdd:pfam00053 16 ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1587-1829 |
2.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1587 RTVIVNLVEQI-----KDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEE 1661
Cdd:PRK02224 186 RGSLDQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1662 EMSTALKNLKNIQNITAMVDDKLLNLDNNLTDVMMRL-------VNLSNGVDLLKNKTEQNREMAKEAKAQSDNATREAE 1734
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1735 GLQEELTNAETLYKQLKEkvdsaggtgegnvnqKAIEMKKEAEDLLKKATMGMETLKKLERKFNKNEQKMQ---QQRDEL 1811
Cdd:PRK02224 346 SLREDADDLEERAEELRE---------------EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapVDLGNA 410
|
250
....*....|....*...
gi 528517788 1812 TDLEKNVTGIREYIRSKV 1829
Cdd:PRK02224 411 EDFLEELREERDELRERE 428
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1589-1814 |
2.67e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.99 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1589 VIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKV---NDLLKKAQDAKTQADGVS-DNINKTKEALETSQNAIKKAEEEMS 1664
Cdd:pfam04108 57 VLNELKKDFKQLLKDLDAALERLEETLDKLRNTpvePALPPGEEKQKTLLDFIDeDSVEILRDALKELIDELQAAQESLD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1665 TALKNlkniqnitamVDDKLLNLDNNLTDVMMRLVNLSNGVDLLKNKTEQNREMAKEAKAQSD------NATREAEGLQE 1738
Cdd:pfam04108 137 SDLKR----------FDDDLRDLQKELESLSSPSESISLIPTLLKELESLEEEMASLLESLTNhydqcvTAVKLTEGGRA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1739 ELTN-----AETLYKQLKEKVDSAG--GTGEGNVnQKAIEMKKEAEDLLKKATMGMETLK-----------KLERKFNKN 1800
Cdd:pfam04108 207 EMLEvlendARELDDVVPELQDRLDemENNYERL-QKLLEQKNSLIDELLSALQLIAEIQsrlpeylaalkEFEERWEEE 285
|
250
....*....|....
gi 528517788 1801 EQKMQQQRDELTDL 1814
Cdd:pfam04108 286 KETIEDYLSELEDL 299
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1499-1563 |
3.32e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 3.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528517788 1499 KNLTAVSEELQTMAKKLRDIATLTQTVKTQAKETLDKAQNK---------KDMFEKSNKMLKNFIQKIKDFLNE 1563
Cdd:pfam03938 33 AELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQElqqlqqkaqQELQKKQQELLQPIQDKINKAIKE 106
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1590-1682 |
3.61e-03 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 41.12 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1590 IVNLVEQIKDSIVNL-TNVEGVFNHTSEQLAKVNDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALK 1668
Cdd:smart00283 2 VSEAVEEIAAGAEEQaEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVS 81
|
90 100
....*....|....*....|.
gi 528517788 1669 NLK-------NIQNITAMVDD 1682
Cdd:smart00283 82 AVEeleessdEIGEIVSVIDD 102
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1503-1682 |
3.68e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 41.93 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1503 AVSEELQTMAKKLRDIAT--LTQTVKTQAKETLDkaqnkkDMFEKSNKMLKNF---IQKIKDFLNEEGADPESIEKVAQQ 1577
Cdd:COG0840 205 SITRPLRELLEVLERIAEgdLTVRIDVDSKDEIG------QLADAFNRMIENLrelVGQVRESAEQVASASEELAASAEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1578 VLAISLPVNRTV--IVNLVEQIKDSIvnltnvegvfNHTSEQLAKVNDLlkkAQDAKTQADGVSDNINKTKEALETSQNA 1655
Cdd:COG0840 279 LAAGAEEQAASLeeTAAAMEELSATV----------QEVAENAQQAAEL---AEEASELAEEGGEVVEEAVEGIEEIRES 345
|
170 180
....*....|....*....|....*..
gi 528517788 1656 IKKAEEEMSTALKNLKNIQNITAMVDD 1682
Cdd:COG0840 346 VEETAETIEELGESSQEIGEIVDVIDD 372
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1509-1673 |
4.20e-03 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 40.86 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1509 QTMAKKLRDIA-TLTQTVKTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNeegadpesiekvaqqvlaiSLPVNR 1587
Cdd:cd21116 72 QSYYPDLIELAdNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKN-------------------DLDDDS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1588 TVIVNLVEQIKDSIVNLTNVEGVFNHTSEQLAKVNDLLKKAQDA----KTQADGVSDNINKTKEALET--SQNAIKKAEE 1661
Cdd:cd21116 133 RNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSNDwqtlDSDIKELITDLEDAESSIDAafLQADLKAAKA 212
|
170
....*....|..
gi 528517788 1662 EMSTALKNLKNI 1673
Cdd:cd21116 213 DWNQLYEQAKSL 224
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1487-1816 |
4.44e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1487 SVKALDNA-DEVHKNLTAVSEELQTMAKKLRDIATLTQTVkTQAKETLDKAQNKKDMFEKSNKMLKNFIQKIKDFLNEEG 1565
Cdd:PTZ00440 2285 SIKTFNEIyDDIKSNIGDLYKLEDTNNDELKKVKLYIENI-THLLNRINTLINDLDNYQDENYGKDKNIELNNENNSYII 2363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1566 ADPESIEKVAQQVLAISLPVNRTVIVNLVEQIKDSIVNLTN-VEGVFNHTSEQLAKvNDLLKKAQDAKTQADGVSDNINK 1644
Cdd:PTZ00440 2364 KTKEKINNLKEEFSKLLKNIKRNNTLCNNNNIKDFISNIGKsVETIKQRFSSNLPE-KEKLHQIEENLNEIKNIMNETKR 2442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1645 TKEALETSQNAIKKAEEEMSTAlKNLKNIQNITAMVDdkllNLDNNLTDVMMRLVNLSNGVDLLKNKTEqnrEMAKEAKA 1724
Cdd:PTZ00440 2443 ISNVDAFTNKILQDIDNEKNKE-NNNMNAEKIDDLIE----NVTSHNEKIKSELLIINDALRRVKEKKD---EMNKLFNS 2514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1725 QSDNATREAEGLQEELTNAETLYKQLKEKVdSAGGTGEGNVNQKAIEMKKEAEDLLKKATM-----GMETLKKLERKFNK 1799
Cdd:PTZ00440 2515 LTENNNNNNNSAKNIVDNSTYIINELESHV-SKLNELLSYIDNEIKELENEKLKLLEKAKIeesrkERERIESETQEDNT 2593
|
330
....*....|....*...
gi 528517788 1800 NE-QKMQQQRDELTDLEK 1816
Cdd:PTZ00440 2594 DEeQINRQQQERLQKEEE 2611
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1262-1435 |
4.51e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1262 KRILELEKKLAQAQELVRDgdregtfnlISQTVDDLRAEIALTDGRLmgvirdlnvttdhnNDLKQNLTALEKELKDLNN 1341
Cdd:COG4942 34 QEIAELEKELAALKKEEKA---------LLKQLAALERRIAALARRI--------------RALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1342 TLHQLRRELENyltagLAEQFANVLKYYQRslNSEQRCNASVYGPQSPVEQSqdtrnRTEALLKDKKDSLLRTATANNKS 1421
Cdd:COG4942 91 EIAELRAELEA-----QKEELAELLRALYR--LGRQPPLALLLSPEDFLDAV-----RRLQYLKYLAPARREQAEELRAD 158
|
170
....*....|....
gi 528517788 1422 LSELEGKAHEINRK 1435
Cdd:COG4942 159 LAELAALRAELEAE 172
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1622-1733 |
5.70e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.25 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1622 NDLLKKAQDAKTQADGVSDNINKTKEALETSQNAIKKAEEEMSTALKNLKNIQNItamvddKLLNLDNNLTDVmmrlvnl 1701
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQ------ALQTAQNNLATA------- 323
|
90 100 110
....*....|....*....|....*....|....
gi 528517788 1702 sngVDLLKNKTEQNREmAKEAKA--QSDNATREA 1733
Cdd:TIGR04320 324 ---QAALANAEARLAK-AKEALAnlNADLAKKQA 353
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1747-1832 |
8.99e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517788 1747 YKQLKEKVDSAGGTGEGNVNQKAIEMKKEAEDLLKK-ATMGMETLKKLERKFNKNEQKMQQQRDELT-DLEKNVTGIREY 1824
Cdd:smart00935 16 GKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDaATLSEAAREKKEKELQKKVQEFQRKQQKLQqDLQKRQQEELQK 95
|
....*...
gi 528517788 1825 IRSKVLAY 1832
Cdd:smart00935 96 ILDKINKA 103
|
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