|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
44-278 |
4.57e-107 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 339.94 E-value: 4.57e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 44 CLPEFENAAFGRRAEASHTCG-RPPEDFCPHVGAPGAGlQCQRCDDADPGRRHDASYLTDFHSPDDSTWWQSPSMAfgVQ 122
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEGGK-KCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 123 YPtSVNLTLSLGKAYEITYVRLKFHTSRPESFAIYKRTYASGPWEPYQYYSASCQKTYGRPEGHYLRPGEDErvAFCTSE 202
Cdd:pfam00055 78 YE-NVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKDDE--VICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66272331 203 FSDISPLNGGNVAFSTLEGRPSAYNFEESPVLQEWVTSTDILISLDRLNTFGDDIFKDPRVLQSYYYAVSDFSVGG 278
Cdd:pfam00055 155 YSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
39-278 |
2.54e-97 |
|
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: 312.76 E-value: 2.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 39 GRAQRCLPEFENAAFGRRAEASHTCGRP-PEDFCPHVGAPGAGLQCQRCDDADPGRRHDASYLTDFHSPDDSTWWQSPSM 117
Cdd:smart00136 2 GRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 118 AFGVQYptsVNLTLSLGKAYEITYVRLKFHTSRPeSFAIYKRTYASGPWEPYQYYSASCQKTYGR-PEGHYLRPGEDErv 196
Cdd:smart00136 82 SNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRpPRGPITKGNEDE-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 197 AFCTSEFSDISPLNGGNVAFSTLEGRPSAYNFEESPVLQEWVTSTDILISLDRLNTFGDDIFKD-PRVLQSYYYAVSDFS 275
Cdd:smart00136 156 VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDIA 235
|
...
gi 66272331 276 VGG 278
Cdd:smart00136 236 VGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
550-683 |
4.65e-29 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 113.52 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 550 SAPKKFLGDQRLSYGQPVILTLQVP--PGGSPPPI--QLRLEGAGLALSLRPSSLPSPQDTrQPRRVQLQFLLQETSEEA 625
Cdd:pfam00052 3 SAPEQFLGNKLTSYGGYLTYTVRYEplPGGGSLNSepDVILEGNGLRLSYSSPDQPPPDPG-QEQTYSVRLHEENWRDSD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 66272331 626 ESPLPTFHFQRLLSNLTALSIWTSgqGPGHSGQVLLCEVQLTSAWPqRELAPPASWVE 683
Cdd:pfam00052 82 GAPVSREDFMMVLANLTAILIRAT--YSTGSGQVSLSNVSLDSAVP-GGSGPPASWVE 136
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
928-976 |
6.41e-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: 6.41e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 928 CKCHPLGSLENKCHPKTGQCPCRPGVTGQACDRCQLGFFGFSIKGCRDC 976
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
928-973 |
2.18e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.80 E-value: 2.18e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 66272331 928 CKCHPLGSLENKCHPKTGQCPCRPGVTGQACDRCQLGFFGFSIKGC 973
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
927-977 |
5.30e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 64.68 E-value: 5.30e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 66272331 927 SCKCHPLGSLENKCHPKTGQCPCRPGVTGQACDRCQLGFFGFSIKGcRDCR 977
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG-GGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1103-1575 |
6.74e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 6.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1103 EQLQVLRGHVHCAQAGAQKTCIQLAELEETLQSSEEEVLRAASALSFLASLQKGSStpTNWSHLASEAQILARSHRDTAT 1182
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE--EELEELAEELLEALRAAAELAA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1183 KIEATSER----------------ALLASNASYELLKLMEGRVASEAQQELEDRYQEVQAAQTALGIAVAEALpKAEKAL 1246
Cdd:COG1196 401 QLEELEEAeeallerlerleeeleELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA-LLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1247 ATVKQVIGDAAPHLGLLvtpEAMNFQARGLSWKVKALEQKLEQkePEVGQSVGALQVEAGRALEKMEPFMQ--LRNKTTA 1324
Cdd:COG1196 480 AELLEELAEAAARLLLL---LEAEADYEGFLEGVKAALLLAGL--RGLAGAVAVLIGVEAAYEAALEAALAaaLQNIVVE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1325 AFTRASSAVQAAKVTVIGAETLLAdLEGMKLRSPLPKEQAALKKKAG-----------SIRTRLLEDTKRKTKQAERMLG 1393
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLP-LDKIRARAALAAALARGAIGAAvdlvasdlreaDARYYVLGDTLLGRTLVAARLE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1394 NAASLSSSTKKKSKEAEL---------------MSKDNAKLSRALLREGKQGYRHASRLASQTQATLRRASRLLLTSEAH 1458
Cdd:COG1196 634 AALRRAVTLAGRLREVTLegeggsaggsltggsRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1459 KQELEEAKQVTSGLSTVERQIRESRISLEKDTKVLSELLVKLgslgvhQAPAQTLNETQRALESLRLQLDSHGALHHK-L 1537
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE------LPEPPDLEELERELERLEREIEALGPVNLLaI 787
|
490 500 510
....*....|....*....|....*....|....*....
gi 66272331 1538 RQLEEESAR-QELQIQSfeDDLAEIRADkhnLETILSSL 1575
Cdd:COG1196 788 EEYEELEERyDFLSEQR--EDLEEARET---LEEAIEEI 821
|
|
| LamB |
smart00281 |
Laminin B domain; |
550-671 |
4.84e-12 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 64.59 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 550 SAPKKFLGDQRLSYGQPVILTLQ-VPPGGSPPPIQ--LRLEGAGLALSLRPSSLPSPqdtRQPRRVQLQFLLQETSEEAE 626
Cdd:smart00281 8 VAPEQFLGDKVTSYGGKLRYTLSfDGRRGGTHVSApdVILEGNGLRISHPAEGPPLP---DELTTVEVRFREENWQYYGG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 66272331 627 SPLPTFHFQRLLSNLTALSIWTS-GQgpgHSGQVLLCEVQLTSAWP 671
Cdd:smart00281 85 RPVTREDLMMVLANLTAILIRATySQ---QMAGSRLSDVSLEVAVP 127
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
878-925 |
7.60e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.60 E-value: 7.60e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66272331 878 CSCDLRGSVSEkTCNPVTGQCVCLPYVSGRDCSRCSPGFYDLQ--SGRGC 925
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1080-1575 |
1.01e-11 |
|
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: 70.09 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1080 LQETRGTFLQQMVGLEDSVKATWEQLQVLRGHVHCAQAGAQKTCIQLAELEETLQSSEEEVLRAASALsFLASLQKGSst 1159
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-AQLELQIAS-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1160 ptnwshLASEAQILarshRDTATKIEATSERalLASNASYELLKLMEGRVAsEAQQELEDRYQEVQAAQTALgIAVAEAL 1239
Cdd:TIGR02168 398 ------LNNEIERL----EARLERLEDRRER--LQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEEL-ERLEEAL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1240 PKAEKALATVKQVIGDAAPHL----GLLVTPEAMNFQARGLSWKVKALEQKLEQKEPEVGQSVGALQVEAG--RALEK-M 1312
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELaqlqARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeAAIEAaL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1313 EPFMQL---RNKTTAAftrasSAVQAAKVTVIGAETLLAdLEGMKLRSPLPKEQAALKKKAG--SIRTRLLEDTKRKTKQ 1387
Cdd:TIGR02168 544 GGRLQAvvvENLNAAK-----KAIAFLKQNELGRVTFLP-LDSIKGTEIQGNDREILKNIEGflGVAKDLVKFDPKLRKA 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1388 AERMLG------NAASLSSSTKKKSKEAELMSKDNAKLSRALLREGKQGYRHASRLAsqTQATLRRASRLL--LTSEAH- 1458
Cdd:TIGR02168 618 LSYLLGgvlvvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE--RRREIEELEEKIeeLEEKIAe 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1459 -KQELEEAKQVTSGLSTVERQIRESRISLEKDTKVLSELLVKLGSlgVHQAPAQTLNETQRALESLRLQLDSHGALHHKL 1537
Cdd:TIGR02168 696 lEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--EVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 66272331 1538 RQ----LEEESARQELQIQSFEDDLAEIRADKHNLETILSSL 1575
Cdd:TIGR02168 774 EEelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
877-926 |
1.16e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.83 E-value: 1.16e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 66272331 877 PCSCDLRGSVSEkTCNPVTGQCVCLPYVSGRDCSRCSPGFYDLQS-GRGCQ 926
Cdd:cd00055 1 PCDCNGHGSLSG-QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
391-437 |
4.44e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 4.44e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66272331 391 PCDCHPAGSLSLQCD-NSGVCPCKPTVTGWKCDRCLPGFHSLSE--GGCR 437
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
439-486 |
5.86e-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: 58.90 E-value: 5.86e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 439 CACNVAGSLG-TCDPRSGNCPCKENVEGSLCDRCRPGTFNLQPHNPVGC 486
Cdd:pfam00053 1 CDCNPHGSLSdTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
718-765 |
9.60e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 9.60e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66272331 718 PCTCNQHGT----CDPNTGICLCGHHTEGPSCERCMPGFYGNAfsGRADDCQ 765
Cdd:cd00055 1 PCDCNGHGSlsgqCDPGTGQCECKPNTTGRRCDRCAPGYYGLP--SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
392-436 |
1.90e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 1.90e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 66272331 392 CDCHPAGSLSLQCD-NSGVCPCKPTVTGWKCDRCLPGFHSLSEGGC 436
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
392-439 |
1.95e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 57.36 E-value: 1.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 392 CDCHPAGSLSLQCD-NSGVCPCKPTVTGWKCDRCLPGFHSLSEGGCRPC 439
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
878-925 |
3.85e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.85e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 66272331 878 CSCDLRGSVSEkTCNPVTGQCVCLPYVSGRDCSRCSPGFYDlQSGRGC 925
Cdd:smart00180 1 CDCDPGGSASG-TCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
719-756 |
4.06e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 4.06e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66272331 719 CTCNQHGT----CDPNTGICLCGHHTEGPSCERCMPGFYGNA 756
Cdd:pfam00053 1 CDCNPHGSlsdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
438-486 |
4.46e-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: 4.46e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66272331 438 PCACNVAGSL-GTCDPRSGNCPCKENVEGSLCDRCRPGTFNLqPHNPVGC 486
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
719-759 |
1.79e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 1.79e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66272331 719 CTCNQHGT----CDPNTGICLCGHHTEGPSCERCMPGFYGNAFSG 759
Cdd:smart00180 1 CDCDPGGSasgtCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
439-481 |
6.84e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 6.84e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66272331 439 CACNVAGSL-GTCDPRSGNCPCKENVEGSLCDRCRPGTFNLQPH 481
Cdd:smart00180 1 CDCDPGGSAsGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
822-864 |
2.58e-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: 2.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 66272331 822 CQCSGNVDLNavGNCDPHSGHCLrCLYNTTGAHCEHCREGFYG 864
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
821-864 |
9.08e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 9.08e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66272331 821 RCQCSGNVDLNavGNCDPHSGHCLrCLYNTTGAHCEHCREGFYG 864
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
279-326 |
1.19e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.66 E-value: 1.19e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 66272331 279 RCKCNGHASECEPNAAGQLACRCQHNTTGVDCERCLPFFQDRPWARGT 326
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
976-1022 |
1.21e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.66 E-value: 1.21e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 976 CRCSPLGAASSQCHENS-TCVCRPGFVGYKCDRCQDNFF-LADGDTGCQ 1022
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTgQCECKPNTTGRRCDRCAPGYYgLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
976-1013 |
1.64e-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: 49.27 E-value: 1.64e-07
10 20 30
....*....|....*....|....*....|....*....
gi 66272331 976 CRCSPLGAASSQCHENS-TCVCRPGFVGYKCDRCQDNFF 1013
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETgQCLCKPGVTGRHCDRCKPGYY 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1125-1577 |
2.90e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1125 QLAELEETLQSSEEEVLRAAsalsflASLQKGSSTPTNWSHLASEAQILARSHRDTATKIEAT-SERALLASnasyellk 1203
Cdd:PRK02224 214 ELAELDEEIERYEEQREQAR------ETRDEADEVLEEHEERREELETLEAEIEDLRETIAETeREREELAE-------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1204 lmEGRVASEAQQELEDRYQEVqAAQTALGIAVAEALPKA----EKALATVKQVIGDAAPHLGllvtpeAMNFQARGLSWK 1279
Cdd:PRK02224 280 --EVRDLRERLEELEEERDDL-LAEAGLDDADAEAVEARreelEDRDEELRDRLEECRVAAQ------AHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1280 VKALEQKLEQKEpevgqsvgalqvEAGRALEkmepfmqlrnkttaaftrasSAVQAAKVTVIGAETLLADLEgmklrspl 1359
Cdd:PRK02224 351 ADDLEERAEELR------------EEAAELE--------------------SELEEAREAVEDRREEIEELE-------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1360 pKEQAALKKKAGSIRTRL---------LEDTKRKTKQAERMLgnaaslssstkkkskEAELMSKDNA-KLSRALLREGK- 1428
Cdd:PRK02224 391 -EEIEELRERFGDAPVDLgnaedfleeLREERDELREREAEL---------------EATLRTARERvEEAEALLEAGKc 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1429 -------QGYRHASRLASQTQ--ATLRRA-SRLLLTSEAHKQELEEAKQvtsgLSTVERQIResriSLEKDTKVLSELLV 1498
Cdd:PRK02224 455 pecgqpvEGSPHVETIEEDRErvEELEAElEDLEEEVEEVEERLERAED----LVEAEDRIE----RLEERREDLEELIA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1499 KlgslgvHQApaqTLNETQRALESLRLQ---LDSHGALHHKLRQLEEESARQELQ-IQSFEDDLAEIRADKHNLETILSS 1574
Cdd:PRK02224 527 E------RRE---TIEEKRERAEELRERaaeLEAEAEEKREAAAEAEEEAEEAREeVAELNSKLAELKERIESLERIRTL 597
|
...
gi 66272331 1575 LPE 1577
Cdd:PRK02224 598 LAA 600
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1127-1532 |
3.59e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.22 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1127 AELEETLQS---SEEEVLRAASALSFLASLQKGSSTPTNW-SHLASEAQILARSHRDTATKI--EATSERALLASNASYE 1200
Cdd:NF041483 621 AERIRTLQAqaeQEAERLRTEAAADASAARAEGENVAVRLrSEAAAEAERLKSEAQESADRVraEAAAAAERVGTEAAEA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1201 LlklmegrvaSEAQQELEDRYQEvqaAQTALGIAVAEALPKAEKA-------LATVKQVIGDAAPHLGLLVtpEAMNFQA 1273
Cdd:NF041483 701 L---------AAAQEEAARRRRE---AEETLGSARAEADQERERAreqseelLASARKRVEEAQAEAQRLV--EEADRRA 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1274 RGLswkVKALEQKLEQkepeVGQSVGALQVEAgralekMEPFMQLRnkttaaftraSSAVQAAKVTVIGAETlladlEGM 1353
Cdd:NF041483 767 TEL---VSAAEQTAQQ----VRDSVAGLQEQA------EEEIAGLR----------SAAEHAAERTRTEAQE-----EAD 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1354 KLRSPLPKEQAALKKKAGSIRTRLLEDTKRKTKQAERMLGNAAslssstkkksKEAELMSKDNAKLSRALLREGKQGYRH 1433
Cdd:NF041483 819 RVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSEAI----------AEAERLRSDASEYAQRVRTEASDTLAS 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1434 ASRLASQTQATLRR-ASRllLTSEAHKQ-------ELEEAKQVTSGLST-VERQIRESRISLEKDTKVLSELLVKLGSLG 1504
Cdd:NF041483 889 AEQDAARTRADAREdANR--IRSDAAAQadrligeATSEAERLTAEARAeAERLRDEARAEAERVRADAAAQAEQLIAEA 966
|
410 420 430
....*....|....*....|....*....|....
gi 66272331 1505 VHQA------PAQTLNETQRALESLRLQLDSHGA 1532
Cdd:NF041483 967 TGEAerlraeAAETVGSAQQHAERIRTEAERVKA 1000
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
976-1021 |
1.11e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.11e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 66272331 976 CRCSPLGAASSQCHENS-TCVCRPGFVGYKCDRCQDNFFLADGDtGC 1021
Cdd:smart00180 1 CDCDPGGSASGTCDPDTgQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1212-1569 |
1.34e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.26 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1212 EAQQELEDRYQEVQAAQTAL---GIAVAEALPKAEKALATVKQVIGDAAPHLGLLVTPEAmnfQARGLSWKVKALEQKLE 1288
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAEK---QRRDLGEELEALKTELE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1289 --------------QKEPEVGQSVGALQVEAGRALEKMEpfmQLRNKTTAAFTRASSAVQAAKVTVIGAETLLADLEG-- 1352
Cdd:pfam01576 310 dtldttaaqqelrsKREQEVTELKKALEEETRSHEAQLQ---EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESen 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1353 ------MKLRSPLPKEQAALKKKAGS----IRTRLLEDTKRKTKQAERmLGNAASLSSSTKKKSKEAElmsKDNAKLSRA 1422
Cdd:pfam01576 387 aelqaeLRTLQQAKQDSEHKRKKLEGqlqeLQARLSESERQRAELAEK-LSKLQSELESVSSLLNEAE---GKNIKLSKD 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1423 LLREGKQGYRHASRLASQTQATLRRASRLLLTSEAHK------QELEEAKQ-VTSGLSTVERQIRESRISLEKDTKVLse 1495
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNslqeqlEEEEEAKRnVERQLSTLQAQLSDMKKKLEEDAGTL-- 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66272331 1496 llvklgslgvhQAPAQTLNETQRALESLRLQLDSHGALHHKLrqleeESARQELQiQSFED---DLAEIRADKHNLE 1569
Cdd:pfam01576 541 -----------EALEEGKKRLQRELEALTQQLEEKAAAYDKL-----EKTKNRLQ-QELDDllvDLDHQRQLVSNLE 600
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
822-865 |
2.09e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 2.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66272331 822 CQCsgNVDLNAVGNCDPHSGHCLrCLYNTTGAHCEHCREGFYGS 865
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
336-392 |
1.44e-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: 1.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 336 CNCSGH---SEECTFdrelyrstgHGGHCQrCRDHTTGPHCERCEKNYYRwSPKTPCQPC 392
Cdd:pfam00053 1 CDCNPHgslSDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYG-LPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
766-814 |
2.74e-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: 43.11 E-value: 2.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 766 PCPCPGQSACATIPESGDVVCtHCPPGQRGRRCESCEDGFFGDPLGLSG 814
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
280-321 |
2.78e-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: 42.73 E-value: 2.78e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66272331 280 CKCNGHASECEPNAAGQLACRCQHNTTGVDCERCLPFFQDRP 321
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
335-382 |
8.83e-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: 41.57 E-value: 8.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 66272331 335 PCNCSGH---SEECTFdrelyrstgHGGHCQrCRDHTTGPHCERCEKNYYR 382
Cdd:cd00055 1 PCDCNGHgslSGQCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
767-819 |
9.41e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.49 E-value: 9.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 66272331 767 CPCPGQSACATIPESGDVVCtHCPPGQRGRRCESCEDGFFGDPlglSGAPQPC 819
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| TNFRSF5 |
cd13407 |
Tumor necrosis factor receptor superfamily member 5 (TNFRSF5), also known as CD40; TNFRSF5 ... |
721-832 |
1.33e-03 |
|
Tumor necrosis factor receptor superfamily member 5 (TNFRSF5), also known as CD40; TNFRSF5 (commonly known as CD40 and also as CDW40, p50, Bp50) is widely expressed in diverse cell types including B lymphocytes, dendritic cells, platelets, monocytes, endothelial cells, and fibroblasts. It is essential in mediating a wide variety of immune and inflammatory responses, including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation. Its natural immunomodulating ligand is CD40L, and a primary defect in the CD40/CD40L system is associated with X-linked hyper-IgM (XHIM) syndrome. It is also involved in tumorigenesis; CD40 expression is significantly higher in gastric carcinomas and it is associated with the lymphatic metastasis of cancer cells and their tumor node metastasis (TNM) classification. Upregulated levels of CD40/CD40L on B cells and T cells may play an important role in the immune pathogenesis of breast cancer. Consequently, the CD40/CD40L system serves as a link between tumorigenesis, atherosclerosis, and the immune system, and offers a potential target for drug therapy for related diseases, such as cancer, atherosclerosis, diabetes mellitus, and immunological rejection.
Pssm-ID: 276912 [Multi-domain] Cd Length: 161 Bit Score: 41.23 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 721 CNQHGTCDPNTG-------------ICLC--GHHTEGPSCERCMPGfygnafsgraddcQPCPcPGQSACATIPESGDVV 785
Cdd:cd13407 52 CHQHRYCDPNLGlrvqtegtaetdtTCTCqeGQHCTSEACETCALH-------------TSCK-PGFGVKQIATGVSDTI 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 66272331 786 CTHCPpgqrgrrcesceDGFFGDplgLSGAPQPCR---RCQCSGNVDLNA 832
Cdd:cd13407 118 CEPCP------------VGFFSN---VSSAFEKCHpwtSCETKGLVELQA 152
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
280-317 |
1.59e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 1.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 66272331 280 CKCN--GHASE-CEPNAaGQlaCRCQHNTTGVDCERCLPFF 317
Cdd:smart00180 1 CDCDpgGSASGtCDPDT-GQ--CECKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
335-385 |
3.47e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66272331 335 PCNCSGH-SEECTFDrelyrstghGGHCQrCRDHTTGPHCERCEKNYYRWSP 385
Cdd:smart00180 2 DCDPGGSaSGTCDPD---------TGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
44-278 |
4.57e-107 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 339.94 E-value: 4.57e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 44 CLPEFENAAFGRRAEASHTCG-RPPEDFCPHVGAPGAGlQCQRCDDADPGRRHDASYLTDFHSPDDSTWWQSPSMAfgVQ 122
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEGGK-KCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGV--IQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 123 YPtSVNLTLSLGKAYEITYVRLKFHTSRPESFAIYKRTYASGPWEPYQYYSASCQKTYGRPEGHYLRPGEDErvAFCTSE 202
Cdd:pfam00055 78 YE-NVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGIKDDE--VICTSE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66272331 203 FSDISPLNGGNVAFSTLEGRPSAYNFEESPVLQEWVTSTDILISLDRLNTFGDDIFKDPRVLQSYYYAVSDFSVGG 278
Cdd:pfam00055 155 YSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
39-278 |
2.54e-97 |
|
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: 312.76 E-value: 2.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 39 GRAQRCLPEFENAAFGRRAEASHTCGRP-PEDFCPHVGAPGAGLQCQRCDDADPGRRHDASYLTDFHSPDDSTWWQSPSM 117
Cdd:smart00136 2 GRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 118 AFGVQYptsVNLTLSLGKAYEITYVRLKFHTSRPeSFAIYKRTYASGPWEPYQYYSASCQKTYGR-PEGHYLRPGEDErv 196
Cdd:smart00136 82 SNGPQN---VNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRpPRGPITKGNEDE-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 197 AFCTSEFSDISPLNGGNVAFSTLEGRPSAYNFEESPVLQEWVTSTDILISLDRLNTFGDDIFKD-PRVLQSYYYAVSDFS 275
Cdd:smart00136 156 VICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrPEVTRRYYYAISDIA 235
|
...
gi 66272331 276 VGG 278
Cdd:smart00136 236 VGG 238
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
550-683 |
4.65e-29 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 113.52 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 550 SAPKKFLGDQRLSYGQPVILTLQVP--PGGSPPPI--QLRLEGAGLALSLRPSSLPSPQDTrQPRRVQLQFLLQETSEEA 625
Cdd:pfam00052 3 SAPEQFLGNKLTSYGGYLTYTVRYEplPGGGSLNSepDVILEGNGLRLSYSSPDQPPPDPG-QEQTYSVRLHEENWRDSD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 66272331 626 ESPLPTFHFQRLLSNLTALSIWTSgqGPGHSGQVLLCEVQLTSAWPqRELAPPASWVE 683
Cdd:pfam00052 82 GAPVSREDFMMVLANLTAILIRAT--YSTGSGQVSLSNVSLDSAVP-GGSGPPASWVE 136
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
928-976 |
6.41e-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: 6.41e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 928 CKCHPLGSLENKCHPKTGQCPCRPGVTGQACDRCQLGFFGFSIKGCRDC 976
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
928-973 |
2.18e-13 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 65.80 E-value: 2.18e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 66272331 928 CKCHPLGSLENKCHPKTGQCPCRPGVTGQACDRCQLGFFGFSIKGC 973
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
927-977 |
5.30e-13 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 64.68 E-value: 5.30e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 66272331 927 SCKCHPLGSLENKCHPKTGQCPCRPGVTGQACDRCQLGFFGFSIKGcRDCR 977
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG-GGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1103-1575 |
6.74e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 6.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1103 EQLQVLRGHVHCAQAGAQKTCIQLAELEETLQSSEEEVLRAASALSFLASLQKGSStpTNWSHLASEAQILARSHRDTAT 1182
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE--EELEELAEELLEALRAAAELAA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1183 KIEATSER----------------ALLASNASYELLKLMEGRVASEAQQELEDRYQEVQAAQTALGIAVAEALpKAEKAL 1246
Cdd:COG1196 401 QLEELEEAeeallerlerleeeleELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA-LLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1247 ATVKQVIGDAAPHLGLLvtpEAMNFQARGLSWKVKALEQKLEQkePEVGQSVGALQVEAGRALEKMEPFMQ--LRNKTTA 1324
Cdd:COG1196 480 AELLEELAEAAARLLLL---LEAEADYEGFLEGVKAALLLAGL--RGLAGAVAVLIGVEAAYEAALEAALAaaLQNIVVE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1325 AFTRASSAVQAAKVTVIGAETLLAdLEGMKLRSPLPKEQAALKKKAG-----------SIRTRLLEDTKRKTKQAERMLG 1393
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLP-LDKIRARAALAAALARGAIGAAvdlvasdlreaDARYYVLGDTLLGRTLVAARLE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1394 NAASLSSSTKKKSKEAEL---------------MSKDNAKLSRALLREGKQGYRHASRLASQTQATLRRASRLLLTSEAH 1458
Cdd:COG1196 634 AALRRAVTLAGRLREVTLegeggsaggsltggsRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1459 KQELEEAKQVTSGLSTVERQIRESRISLEKDTKVLSELLVKLgslgvhQAPAQTLNETQRALESLRLQLDSHGALHHK-L 1537
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE------LPEPPDLEELERELERLEREIEALGPVNLLaI 787
|
490 500 510
....*....|....*....|....*....|....*....
gi 66272331 1538 RQLEEESAR-QELQIQSfeDDLAEIRADkhnLETILSSL 1575
Cdd:COG1196 788 EEYEELEERyDFLSEQR--EDLEEARET---LEEAIEEI 821
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1080-1570 |
1.76e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1080 LQETRGTFLQQMVGLEDSVKATWEQLQVLRGHVHCAQAGAQKTCIQLAELEETLQSSEEEVLRAASALSflaslqkgsst 1159
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA----------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1160 ptnwSHLASEAQILARSHRDTATKIEATSERALLASNASYELLKLMEGRVASEAQQELEDRYQEVQAAQTALGIAVAEAL 1239
Cdd:COG1196 397 ----ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1240 PKAEKALATVKQVIGDAAPHLGLLvtpEAMNFQARGLSWKVKALEQKLEQkePEVGQSVGALQVEAGRALEKMEPFMQ-- 1317
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLL---LEAEADYEGFLEGVKAALLLAGL--RGLAGAVAVLIGVEAAYEAALEAALAaa 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1318 LRNKTTAAFTRASSAVQAAKVTVIGAETLLAdLEGMKLRSPLPKEQAALKKKAGSIrtrLLEDTKRKTKQAERMLGNAAS 1397
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLP-LDKIRARAALAAALARGAIGAAVD---LVASDLREADARYYVLGDTLL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1398 LSSSTKKKSKEAELMSKDNAKLSRALLREGKQGYRHASRLASQTQATLRRASRLLLTSEAHKQELEEAKQVTSGLsTVER 1477
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA-LLAE 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1478 QIRESRISLEKDTKVLSELLVKLGSLGVHQAPAQTLNETQRALESLRLQLDSHGALHHKLRQLEEESARQELQIQSF--- 1554
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpv 782
|
490 500
....*....|....*....|
gi 66272331 1555 ----EDDLAEIRADKHNLET 1570
Cdd:COG1196 783 nllaIEEYEELEERYDFLSE 802
|
|
| LamB |
smart00281 |
Laminin B domain; |
550-671 |
4.84e-12 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 64.59 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 550 SAPKKFLGDQRLSYGQPVILTLQ-VPPGGSPPPIQ--LRLEGAGLALSLRPSSLPSPqdtRQPRRVQLQFLLQETSEEAE 626
Cdd:smart00281 8 VAPEQFLGDKVTSYGGKLRYTLSfDGRRGGTHVSApdVILEGNGLRISHPAEGPPLP---DELTTVEVRFREENWQYYGG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 66272331 627 SPLPTFHFQRLLSNLTALSIWTS-GQgpgHSGQVLLCEVQLTSAWP 671
Cdd:smart00281 85 RPVTREDLMMVLANLTAILIRATySQ---QMAGSRLSDVSLEVAVP 127
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
878-925 |
7.60e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.60 E-value: 7.60e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66272331 878 CSCDLRGSVSEkTCNPVTGQCVCLPYVSGRDCSRCSPGFYDLQ--SGRGC 925
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1080-1575 |
1.01e-11 |
|
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: 70.09 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1080 LQETRGTFLQQMVGLEDSVKATWEQLQVLRGHVHCAQAGAQKTCIQLAELEETLQSSEEEVLRAASALsFLASLQKGSst 1159
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-AQLELQIAS-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1160 ptnwshLASEAQILarshRDTATKIEATSERalLASNASYELLKLMEGRVAsEAQQELEDRYQEVQAAQTALgIAVAEAL 1239
Cdd:TIGR02168 398 ------LNNEIERL----EARLERLEDRRER--LQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEEL-ERLEEAL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1240 PKAEKALATVKQVIGDAAPHL----GLLVTPEAMNFQARGLSWKVKALEQKLEQKEPEVGQSVGALQVEAG--RALEK-M 1312
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELaqlqARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeAAIEAaL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1313 EPFMQL---RNKTTAAftrasSAVQAAKVTVIGAETLLAdLEGMKLRSPLPKEQAALKKKAG--SIRTRLLEDTKRKTKQ 1387
Cdd:TIGR02168 544 GGRLQAvvvENLNAAK-----KAIAFLKQNELGRVTFLP-LDSIKGTEIQGNDREILKNIEGflGVAKDLVKFDPKLRKA 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1388 AERMLG------NAASLSSSTKKKSKEAELMSKDNAKLSRALLREGKQGYRHASRLAsqTQATLRRASRLL--LTSEAH- 1458
Cdd:TIGR02168 618 LSYLLGgvlvvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE--RRREIEELEEKIeeLEEKIAe 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1459 -KQELEEAKQVTSGLSTVERQIRESRISLEKDTKVLSELLVKLGSlgVHQAPAQTLNETQRALESLRLQLDSHGALHHKL 1537
Cdd:TIGR02168 696 lEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--EVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 66272331 1538 RQ----LEEESARQELQIQSFEDDLAEIRADKHNLETILSSL 1575
Cdd:TIGR02168 774 EEelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
877-926 |
1.16e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.83 E-value: 1.16e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 66272331 877 PCSCDLRGSVSEkTCNPVTGQCVCLPYVSGRDCSRCSPGFYDLQS-GRGCQ 926
Cdd:cd00055 1 PCDCNGHGSLSG-QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
391-437 |
4.44e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.29 E-value: 4.44e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66272331 391 PCDCHPAGSLSLQCD-NSGVCPCKPTVTGWKCDRCLPGFHSLSE--GGCR 437
Cdd:cd00055 1 PCDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPSqgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
439-486 |
5.86e-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: 58.90 E-value: 5.86e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 439 CACNVAGSLG-TCDPRSGNCPCKENVEGSLCDRCRPGTFNLQPHNPVGC 486
Cdd:pfam00053 1 CDCNPHGSLSdTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
718-765 |
9.60e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 9.60e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66272331 718 PCTCNQHGT----CDPNTGICLCGHHTEGPSCERCMPGFYGNAfsGRADDCQ 765
Cdd:cd00055 1 PCDCNGHGSlsgqCDPGTGQCECKPNTTGRRCDRCAPGYYGLP--SQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
392-436 |
1.90e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 1.90e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 66272331 392 CDCHPAGSLSLQCD-NSGVCPCKPTVTGWKCDRCLPGFHSLSEGGC 436
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
392-439 |
1.95e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 57.36 E-value: 1.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 392 CDCHPAGSLSLQCD-NSGVCPCKPTVTGWKCDRCLPGFHSLSEGGCRPC 439
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
878-925 |
3.85e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 3.85e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 66272331 878 CSCDLRGSVSEkTCNPVTGQCVCLPYVSGRDCSRCSPGFYDlQSGRGC 925
Cdd:smart00180 1 CDCDPGGSASG-TCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
719-756 |
4.06e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.59 E-value: 4.06e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66272331 719 CTCNQHGT----CDPNTGICLCGHHTEGPSCERCMPGFYGNA 756
Cdd:pfam00053 1 CDCNPHGSlsdtCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
438-486 |
4.46e-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: 4.46e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66272331 438 PCACNVAGSL-GTCDPRSGNCPCKENVEGSLCDRCRPGTFNLqPHNPVGC 486
Cdd:cd00055 1 PCDCNGHGSLsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
719-759 |
1.79e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 1.79e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66272331 719 CTCNQHGT----CDPNTGICLCGHHTEGPSCERCMPGFYGNAFSG 759
Cdd:smart00180 1 CDCDPGGSasgtCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
439-481 |
6.84e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 6.84e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66272331 439 CACNVAGSL-GTCDPRSGNCPCKENVEGSLCDRCRPGTFNLQPH 481
Cdd:smart00180 1 CDCDPGGSAsGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1028-1560 |
2.07e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1028 YALVKEEAAKLKARLMLMEGWLQRS------------DCGSPWGPLDILQGEAPLGDVYQGHHLLQETRGTFLQQMVGLE 1095
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLedrrerlqqeieELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1096 DSVKATWEQLQVLRGHVHcaQAGAQKTCIQ-LAELEETLQSSEEEVLRAASALS-FLASLQKGSSTPTNWShLASEA--- 1170
Cdd:TIGR02168 468 EELEEAEQALDAAERELA--QLQARLDSLErLQENLEGFSEGVKALLKNQSGLSgILGVLSELISVDEGYE-AAIEAalg 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1171 ------------------QILARSHRDTATKIEATSERALLASNASYELLKLMEGRVASEAqqELEDRYQEVQAAQTAL- 1231
Cdd:TIGR02168 545 grlqavvvenlnaakkaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAK--DLVKFDPKLRKALSYLl 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1232 -GIAVAEALpkaEKALATVKQVigdaaPHLGLLVTPE--------AMNFQARG--------------LSWKVKALEQKLE 1288
Cdd:TIGR02168 623 gGVLVVDDL---DNALELAKKL-----RPGYRIVTLDgdlvrpggVITGGSAKtnssilerrreieeLEEKIEELEEKIA 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1289 QKEpevgQSVGALQVEAGRALEKMEPFMQLRNKTTAAFTRASSAVQAAKVTVIGAETLLADLEgmKLRSPLPKEQAALKK 1368
Cdd:TIGR02168 695 ELE----KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS--KELTELEAEIEELEE 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1369 KAGSIRTRLLEDTKRKTKQAERMLGnaaslssstkkkskeaelmSKDNAKLSRALLREGKQGYRHASRLASQTQATLRRA 1448
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQ-------------------LKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1449 SRLLLTSEAHKQELEEAKQVTSG-LSTVERQIRESRISLEKDTKVLSELLVKLGSLGVHQAPA----QTLNETQRALESL 1523
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEdIESLAAEIEELEELIEELESELEALLNERASLEEALALLrselEELSEELRELESK 909
|
570 580 590
....*....|....*....|....*....|....*...
gi 66272331 1524 RLQL-DSHGALHHKLRQLEEESARQELQIQSFEDDLAE 1560
Cdd:TIGR02168 910 RSELrRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
822-864 |
2.58e-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: 2.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 66272331 822 CQCSGNVDLNavGNCDPHSGHCLrCLYNTTGAHCEHCREGFYG 864
Cdd:pfam00053 1 CDCNPHGSLS--DTCDPETGQCL-CKPGVTGRHCDRCKPGYYG 40
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1190-1570 |
3.00e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1190 RALLASNASYELLKL--MEGRVASEAQQELEDRYQEVQAAQTALG--IAVAEALPKAEKALATVKQVIGDAAPHLGLLVT 1265
Cdd:COG4717 44 RAMLLERLEKEADELfkPQGRKPELNLKELKELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1266 PEamnfQARGLSWKVKALEQKLEQKEPEVGQSVGALQ--VEAGRALEKME-PFMQLRNKTTAAFTRASSAVQAAkvtvig 1342
Cdd:COG4717 124 LL----QLLPLYQELEALEAELAELPERLEELEERLEelRELEEELEELEaELAELQEELEELLEQLSLATEEE------ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1343 AETLLADLEGMKLR-SPLPKEQAALKKKAGSIRTRL--LEDTKRKTKQAER-------------MLGNAASLSSSTKKKS 1406
Cdd:COG4717 194 LQDLAEELEELQQRlAELEEELEEAQEELEELEEELeqLENELEAAALEERlkearlllliaaaLLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1407 KEAELM------------SKDNAKLSRALLREGKQGYRHASRLASQTQATLRRASRLLLTSEAHK-----QELEEAKQVT 1469
Cdd:COG4717 274 TIAGVLflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEllellDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1470 SGLSTVERQIRESRISLEKDtkvlsELLVKLG-----SLGVHQAPAQTLNETQRALESLRLQLDSHG------------- 1531
Cdd:COG4717 354 REAEELEEELQLEELEQEIA-----ALLAEAGvedeeELRAALEQAEEYQELKEELEELEEQLEELLgeleellealdee 428
|
410 420 430
....*....|....*....|....*....|....*....
gi 66272331 1532 ALHHKLRQLEEESARQELQIQSFEDDLAEIRADKHNLET 1570
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
821-864 |
9.08e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 50.05 E-value: 9.08e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66272331 821 RCQCSGNVDLNavGNCDPHSGHCLrCLYNTTGAHCEHCREGFYG 864
Cdd:cd00055 1 PCDCNGHGSLS--GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1087-1563 |
9.40e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1087 FLQQMvgLEDSVKATWEQLQVLRGhvhcaqagaQKTCIQLAELEEtlqsSEEEVLRAASALSFLASLQKgsstptnwshl 1166
Cdd:COG4717 42 FIRAM--LLERLEKEADELFKPQG---------RKPELNLKELKE----LEEELKEAEEKEEEYAELQE----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1167 asEAQILARSHRDTATKIEATSERALLASNASyELLKLMEGRVASEAQ-QELEDRYQEVQAAQTALgIAVAEALPKAEKA 1245
Cdd:COG4717 96 --ELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAElAELPERLEELEERLEEL-RELEEELEELEAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1246 LATVKQVIgDAAPHLGLLVTPEAMNFQARglswKVKALEQKLEQKEPEVGQsvgaLQVEAGRALEKMEpfmQLRNKTTAA 1325
Cdd:COG4717 172 LAELQEEL-EELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELEE----AQEELEELEEELE---QLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1326 ftRASSAVQAAKVT-VIGAETLLADLEGMKLRSPLPKEQAALKKKAGSIRTRLLEDTKRKTKQAERMLGNAASLSSSTKK 1404
Cdd:COG4717 240 --ALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1405 KSKEAELMSKD--NAKLSRALLREGKQGYRHASRLASQTQATLRRASRLLLtsEAHKQELEEAKQVTSgLSTVERQIR-- 1480
Cdd:COG4717 318 EEELEELLAALglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL--EQEIAALLAEAGVED-EEELRAALEqa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1481 ESRISLEKDTKVLSELLVKLGSLGVHQAPAQT-------LNETQRALESLRLQLDSH----GALHHKLRQLEEESARQEL 1549
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDeeeleeeLEELEEELEELEEELEELreelAELEAELEQLEEDGELAEL 474
|
490
....*....|....
gi 66272331 1550 QIQsFEDDLAEIRA 1563
Cdd:COG4717 475 LQE-LEELKAELRE 487
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
279-326 |
1.19e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.66 E-value: 1.19e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 66272331 279 RCKCNGHASECEPNAAGQLACRCQHNTTGVDCERCLPFFQDRPWARGT 326
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
976-1022 |
1.21e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.66 E-value: 1.21e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 976 CRCSPLGAASSQCHENS-TCVCRPGFVGYKCDRCQDNFF-LADGDTGCQ 1022
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTgQCECKPNTTGRRCDRCAPGYYgLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
976-1013 |
1.64e-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: 49.27 E-value: 1.64e-07
10 20 30
....*....|....*....|....*....|....*....
gi 66272331 976 CRCSPLGAASSQCHENS-TCVCRPGFVGYKCDRCQDNFF 1013
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETgQCLCKPGVTGRHCDRCKPGYY 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1028-1569 |
1.70e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1028 YALVKEEAAKLKARLMLMEG-WLQRSdcgspwgpLDILQGEAplgdvyqghHLLQETRGTFLQQMVGLEDSVKATWEQLQ 1106
Cdd:COG1196 215 YRELKEELKELEAELLLLKLrELEAE--------LEELEAEL---------EELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1107 VLRGHVHCAQAGAQKTCIQLAELEETLQSSEEEVLRAASAlsfLASLQkgsstptnwshlASEAQILARSHRDTATKIEA 1186
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELE------------EELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1187 TSERALLAsnASYELLKLMEGRVAsEAQQELEDRYQEVQAAQTALGIAVAEALPKAEKALATVKQVIGDAAPHLGLLvtp 1266
Cdd:COG1196 343 EEELEEAE--EELEEAEAELAEAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1267 EAMNFQARGLSWKVKALEQKLEQKEPEVGQSVGALQVEAGRALEKMEPFMQLRNKTT---AAFTRASSAVQAAKVTVIGA 1343
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAlleAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1344 ETLLADLEGMKLRSPLPKEQAALKKKAGSIRTRLLEDTKRKTKQAERMLGNAASLSSSTKKKSKEAELMSKDNAKLSRAL 1423
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1424 LREGKQGYRHASRLASQTQATLRRasRLLLTSEAHKQELEEAKQVTSGLSTVERQIRESRISLEKDTKVLSELLVKLGSL 1503
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAA--VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66272331 1504 GVHQAPAQTLNETQRALESLRLQLDSHGALHHKLRQLEEESARQELQIQSFEDDLAEIRADKHNLE 1569
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1125-1577 |
2.90e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1125 QLAELEETLQSSEEEVLRAAsalsflASLQKGSSTPTNWSHLASEAQILARSHRDTATKIEAT-SERALLASnasyellk 1203
Cdd:PRK02224 214 ELAELDEEIERYEEQREQAR------ETRDEADEVLEEHEERREELETLEAEIEDLRETIAETeREREELAE-------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1204 lmEGRVASEAQQELEDRYQEVqAAQTALGIAVAEALPKA----EKALATVKQVIGDAAPHLGllvtpeAMNFQARGLSWK 1279
Cdd:PRK02224 280 --EVRDLRERLEELEEERDDL-LAEAGLDDADAEAVEARreelEDRDEELRDRLEECRVAAQ------AHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1280 VKALEQKLEQKEpevgqsvgalqvEAGRALEkmepfmqlrnkttaaftrasSAVQAAKVTVIGAETLLADLEgmklrspl 1359
Cdd:PRK02224 351 ADDLEERAEELR------------EEAAELE--------------------SELEEAREAVEDRREEIEELE-------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1360 pKEQAALKKKAGSIRTRL---------LEDTKRKTKQAERMLgnaaslssstkkkskEAELMSKDNA-KLSRALLREGK- 1428
Cdd:PRK02224 391 -EEIEELRERFGDAPVDLgnaedfleeLREERDELREREAEL---------------EATLRTARERvEEAEALLEAGKc 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1429 -------QGYRHASRLASQTQ--ATLRRA-SRLLLTSEAHKQELEEAKQvtsgLSTVERQIResriSLEKDTKVLSELLV 1498
Cdd:PRK02224 455 pecgqpvEGSPHVETIEEDRErvEELEAElEDLEEEVEEVEERLERAED----LVEAEDRIE----RLEERREDLEELIA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1499 KlgslgvHQApaqTLNETQRALESLRLQ---LDSHGALHHKLRQLEEESARQELQ-IQSFEDDLAEIRADKHNLETILSS 1574
Cdd:PRK02224 527 E------RRE---TIEEKRERAEELRERaaeLEAEAEEKREAAAEAEEEAEEAREeVAELNSKLAELKERIESLERIRTL 597
|
...
gi 66272331 1575 LPE 1577
Cdd:PRK02224 598 LAA 600
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1127-1532 |
3.59e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 55.22 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1127 AELEETLQS---SEEEVLRAASALSFLASLQKGSSTPTNW-SHLASEAQILARSHRDTATKI--EATSERALLASNASYE 1200
Cdd:NF041483 621 AERIRTLQAqaeQEAERLRTEAAADASAARAEGENVAVRLrSEAAAEAERLKSEAQESADRVraEAAAAAERVGTEAAEA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1201 LlklmegrvaSEAQQELEDRYQEvqaAQTALGIAVAEALPKAEKA-------LATVKQVIGDAAPHLGLLVtpEAMNFQA 1273
Cdd:NF041483 701 L---------AAAQEEAARRRRE---AEETLGSARAEADQERERAreqseelLASARKRVEEAQAEAQRLV--EEADRRA 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1274 RGLswkVKALEQKLEQkepeVGQSVGALQVEAgralekMEPFMQLRnkttaaftraSSAVQAAKVTVIGAETlladlEGM 1353
Cdd:NF041483 767 TEL---VSAAEQTAQQ----VRDSVAGLQEQA------EEEIAGLR----------SAAEHAAERTRTEAQE-----EAD 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1354 KLRSPLPKEQAALKKKAGSIRTRLLEDTKRKTKQAERMLGNAAslssstkkksKEAELMSKDNAKLSRALLREGKQGYRH 1433
Cdd:NF041483 819 RVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSEAI----------AEAERLRSDASEYAQRVRTEASDTLAS 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1434 ASRLASQTQATLRR-ASRllLTSEAHKQ-------ELEEAKQVTSGLST-VERQIRESRISLEKDTKVLSELLVKLGSLG 1504
Cdd:NF041483 889 AEQDAARTRADAREdANR--IRSDAAAQadrligeATSEAERLTAEARAeAERLRDEARAEAERVRADAAAQAEQLIAEA 966
|
410 420 430
....*....|....*....|....*....|....
gi 66272331 1505 VHQA------PAQTLNETQRALESLRLQLDSHGA 1532
Cdd:NF041483 967 TGEAerlraeAAETVGSAQQHAERIRTEAERVKA 1000
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
976-1021 |
1.11e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.11e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 66272331 976 CRCSPLGAASSQCHENS-TCVCRPGFVGYKCDRCQDNFFLADGDtGC 1021
Cdd:smart00180 1 CDCDPGGSASGTCDPDTgQCECKPNVTGRRCDRCAPGYYGDGPP-GC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1212-1569 |
1.34e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 53.26 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1212 EAQQELEDRYQEVQAAQTAL---GIAVAEALPKAEKALATVKQVIGDAAPHLGLLVTPEAmnfQARGLSWKVKALEQKLE 1288
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAEK---QRRDLGEELEALKTELE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1289 --------------QKEPEVGQSVGALQVEAGRALEKMEpfmQLRNKTTAAFTRASSAVQAAKVTVIGAETLLADLEG-- 1352
Cdd:pfam01576 310 dtldttaaqqelrsKREQEVTELKKALEEETRSHEAQLQ---EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESen 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1353 ------MKLRSPLPKEQAALKKKAGS----IRTRLLEDTKRKTKQAERmLGNAASLSSSTKKKSKEAElmsKDNAKLSRA 1422
Cdd:pfam01576 387 aelqaeLRTLQQAKQDSEHKRKKLEGqlqeLQARLSESERQRAELAEK-LSKLQSELESVSSLLNEAE---GKNIKLSKD 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1423 LLREGKQGYRHASRLASQTQATLRRASRLLLTSEAHK------QELEEAKQ-VTSGLSTVERQIRESRISLEKDTKVLse 1495
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNslqeqlEEEEEAKRnVERQLSTLQAQLSDMKKKLEEDAGTL-- 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66272331 1496 llvklgslgvhQAPAQTLNETQRALESLRLQLDSHGALHHKLrqleeESARQELQiQSFED---DLAEIRADKHNLE 1569
Cdd:pfam01576 541 -----------EALEEGKKRLQRELEALTQQLEEKAAAYDKL-----EKTKNRLQ-QELDDllvDLDHQRQLVSNLE 600
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
822-865 |
2.09e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 2.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66272331 822 CQCsgNVDLNAVGNCDPHSGHCLrCLYNTTGAHCEHCREGFYGS 865
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1417-1581 |
6.16e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1417 AKLSRALLREGKQGYrhASRLASQTQATLRRASRLLLTSEAHKQELEEAKQvtsGLSTVERQIRESRISLEKDTKVLSEL 1496
Cdd:COG4372 11 ARLSLFGLRPKTGIL--IAALSEQLRKALFELDKLQEELEQLREELEQARE---ELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1497 LVKLGSLGVHQAPAQT-LNETQRALESLRLQL-----------DSHGALHHKLRQLEEESARQELQIQSFEDDLAEIRAD 1564
Cdd:COG4372 86 NEQLQAAQAELAQAQEeLESLQEEAEELQEELeelqkerqdleQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170
....*....|....*..
gi 66272331 1565 KHNLETILSSLPENCAS 1581
Cdd:COG4372 166 LAALEQELQALSEAEAE 182
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
336-392 |
1.44e-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: 1.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 336 CNCSGH---SEECTFdrelyrstgHGGHCQrCRDHTTGPHCERCEKNYYRwSPKTPCQPC 392
Cdd:pfam00053 1 CDCNPHgslSDTCDP---------ETGQCL-CKPGVTGRHCDRCKPGYYG-LPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
766-814 |
2.74e-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: 43.11 E-value: 2.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66272331 766 PCPCPGQSACATIPESGDVVCtHCPPGQRGRRCESCEDGFFGDPLGLSG 814
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
280-321 |
2.78e-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: 42.73 E-value: 2.78e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 66272331 280 CKCNGHASECEPNAAGQLACRCQHNTTGVDCERCLPFFQDRP 321
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
335-382 |
8.83e-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: 41.57 E-value: 8.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 66272331 335 PCNCSGH---SEECTFdrelyrstgHGGHCQrCRDHTTGPHCERCEKNYYR 382
Cdd:cd00055 1 PCDCNGHgslSGQCDP---------GTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1424-1575 |
1.57e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1424 LREGKQGYRHASRLASQTQATLRRAsrlLLTSEAHKQELEEAKQVTSgLSTVERQIRESRISLEKDTKVLSELLVKLgsl 1503
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELE---ELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEE--- 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66272331 1504 gvhqapAQTLNETQRALESLRLQLDSHGALHHKLRQLEEESARQELQIQSFEDDLAEIRADKHNLETILSSL 1575
Cdd:COG1196 291 ------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1408-1569 |
1.70e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1408 EAELMSKDNAKLSRaLLREGKQGYRHASRLASQTQATLRRASRLLLTSEAHKQEL--------EEAKQVTSGLSTVERQI 1479
Cdd:TIGR02169 675 ELQRLRERLEGLKR-ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeeklkERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1480 RESRISLEKDTKVLSELlvklgslgvhqapAQTLNETQRALESLRLQLDSHG--ALHHKLRQLEEESARQELQIQSFEDD 1557
Cdd:TIGR02169 754 ENVKSELKELEARIEEL-------------EEDLHKLEEALNDLEARLSHSRipEIQAELSKLEEEVSRIEARLREIEQK 820
|
170
....*....|..
gi 66272331 1558 LAEIRADKHNLE 1569
Cdd:TIGR02169 821 LNRLTLEKEYLE 832
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1419-1575 |
2.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1419 LSRALLREGKQGYRHASRLASQTQATLRRASRLLLTSEAHKQELEEAKQVTSGLSTVERQIRESRISLEKDTKVLSELLV 1498
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1499 KLGSLGVHQAPAQTLNETQRALESLRLQLDSHGALHHKLRQLEEE---------------SARQELQIQSFEDDLAEIRA 1563
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElaelqeeleelleqlSLATEEELQDLAEELEELQQ 206
|
170
....*....|..
gi 66272331 1564 DKHNLETILSSL 1575
Cdd:COG4717 207 RLAELEEELEEA 218
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1211-1577 |
2.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1211 SEAQQELEDRYQEVQAAQTALgIAVAEALPKAEKALATVKQVIGDAAphlGLLVTPEAMNFQARGLSWKVKALEQKLEQK 1290
Cdd:PRK03918 196 KEKEKELEEVLREINEISSEL-PELREELEKLEKEVKELEELKEEIE---ELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1291 EPEVGQsvgaLQVEAGRaLEKMEP-------FMQLRNKTTAAFTRASSAVQAAKVTVIGAETLLADLEGMKLR-SPLPKE 1362
Cdd:PRK03918 272 KKEIEE----LEEKVKE-LKELKEkaeeyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERlEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1363 QAALKKKAGSI--RTRLLEDTKRKTKQAERMlgNAASLSSSTKKKSKEAELMSKDNAKLSRALLREGKQGYRHASRLASQ 1440
Cdd:PRK03918 347 LKELEKRLEELeeRHELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1441 TQAT--LRRAS-------RLLltSEAHKQEL-----EEAKQVTSGLSTVERQIRESRISLEKDTKVLSEL--LVKLGSLg 1504
Cdd:PRK03918 425 KKAIeeLKKAKgkcpvcgREL--TEEHRKELleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKEL- 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66272331 1505 vhqapAQTLNETQRALESLRLQLDSHGAlhHKLRQLEEESARQELQIQSFEDDLAEIRADKHNLETILSSLPE 1577
Cdd:PRK03918 502 -----AEQLKELEEKLKKYNLEELEKKA--EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1234-1470 |
4.52e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.94 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1234 AVAEALPKAEKALATVKqvigDAAPHLGLLVTPEAMNFQarglswKVKALEQKLEqkepEVGQSVGALQVEAGRALEKME 1313
Cdd:pfam06008 6 SLTGALPAPYKINYNLE----NLTKQLQEYLSPENAHKI------QIEILEKELS----SLAQETEELQKKATQTLAKAQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1314 pfmQLRNKTTAAFTRASSAVQAAK-----VTVIGAETLLADLEGMKL-RSPLPKEQAALKKKAGSIRTR----LLEDTKR 1383
Cdd:pfam06008 72 ---QVNAESERTLGHAKELAEAIKnlidnIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRdfgtQLQNAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1384 KTKQAERMLgNAASLSSSTKKKSKEA------ELMSKDNAKLS--RALLREGKQGYRHASRLASQTQATLRRASRlllts 1455
Cdd:pfam06008 149 ELKAAQDLL-SRIQTWFQSPQEENKAlanalrDSLAEYEAKLSdlRELLREAAAKTRDANRLNLANQANLREFQR----- 222
|
250
....*....|....*
gi 66272331 1456 eaHKQELEEAKQVTS 1470
Cdd:pfam06008 223 --KKEEVSEQKNQLE 235
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
836-926 |
4.75e-04 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 42.00 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 836 CDPHSGHCLRClYNTTGAHCEHCREGFYGSAVATRPvdkCAPCS-CDLR-GSVSEKTCNPVTGQ-CVCLP-------YVS 905
Cdd:cd13406 18 CPPGEGMESRC-TGTQDTVCSPCEPGFYNEAVNYEP---CKPCTqCNQRsGSEEKQKCTKTSDTvCRCRPgtqpldsYKP 93
|
90 100
....*....|....*....|.
gi 66272331 906 GRDCSRCSPGFYDLQSGRGCQ 926
Cdd:cd13406 94 GVDCVPCPPGHFSRGDNQACK 114
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1214-1478 |
4.96e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1214 QQELEdryqEVQAAQTALGIAVAEALPKAEKALATVK----------QVIgDAAPHLG--LLVTPEAMNFQARGLSWK-- 1279
Cdd:PRK10929 29 TQELE----QAKAAKTPAQAEIVEALQSALNWLEERKgslerakqyqQVI-DNFPKLSaeLRQQLNNERDEPRSVPPNms 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1280 VKALEQKL----------------EQ-KEPEVGQSVGAL---QVEAGRALEKMEPFMQLRNKTTAAFTRASSAVQAAKVT 1339
Cdd:PRK10929 104 TDALEQEIlqvssqlleksrqaqqEQdRAREISDSLSQLpqqQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1340 VIGA---ETLLADL------EGMKLRSPLPKEQAA-LKKKAGSIRTRLleDTKRKtKQAERMLGNaaslssstkkkskeA 1409
Cdd:PRK10929 184 ALKAlvdELELAQLsannrqELARLRSELAKKRSQqLDAYLQALRNQL--NSQRQ-REAERALES--------------T 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66272331 1410 ELMSKDNAKLSRALLREGKQGYRHASRLASQTQatlrrasRLLLTSEAHKQELEEAKQVTSGLSTVERQ 1478
Cdd:PRK10929 247 ELLAEQSGDLPKSIVAQFKINRELSQALNQQAQ-------RMDLIASQQRQAASQTLQVRQALNTLREQ 308
|
|
| TNFRSF6B |
cd10575 |
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor ... |
721-789 |
5.42e-04 |
|
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor 3 (DcR3); The subfamily TNFRSF6B is also known as decoy receptor 3 (DcR3), M68, or TR6. This protein is a soluble receptor without death domain and cytoplasmic domain, and secreted by cells. It acts as a decoy receptor that competes with death receptors for ligand binding. It is a pleiotropic immunomodulator and biomarker for inflammatory diseases, autoimmune diseases, and cancer. Over-expression of this gene has been noted in several cancers, including pancreatic carcinoma, and gastrointestinal tract tumors. It can neutralize the biological effects of three tumor necrosis factor superfamily (TNFSF) members: TNFSF6 (Fas ligand/FasL/CD95L) and TNFSF14 (LIGHT) which are both involved in apoptosis and inflammation, and TNFSF15 (TNF-like molecule 1A/TL1A), which is a T cell co-stimulator and involved in gut inflammation. DcR3 is a novel inflammatory marker; higher DcR3 levels strongly correlate with inflammation and independently predict cardiovascular and all-cause mortality in chronic kidney disease (CKD) patients on hemodialysis. Increased synovial inflammatory cells infiltration in rheumatoid arthritis and ankylosing spondylitis is also associated with the elevated DcR3 expression. In cartilaginous fish, mRNA expression of DcR3 in the thymus and leydig, which are the representative lymphoid tissues of elasmobranchs, suggests that DcR3 may act as a modulator in the immune system. Interestingly, in banded dogfish (Triakis scyllia), DcR3 mRNA is strongly expressed in the gill, compared with human expression in the normal lung; both are respiratory organs, suggesting potential relevance of DcR3 to respiratory function.
Pssm-ID: 276901 [Multi-domain] Cd Length: 163 Bit Score: 42.39 E-value: 5.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66272331 721 CNQHGTCDPNTGICLCGHHTEGPSCERCMPGFYGNAFSGRaDDCQP-CPCPGQSACATIP--ESGDVVCTHC 789
Cdd:cd10575 93 CLRHSSCPPGEGVIKLGTPYSDTQCEPCPPGFFSASSSST-EPCQPhTNCTQGGLETNVPgnDYHDTLCTSC 163
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1409-1571 |
6.26e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1409 AELMSKDNAkLSRALLREGKQgyrhasRLASQTQATLRRaSRLLLTSEAHKQELEEAKQVTSGLSTVERQIRESRISLEK 1488
Cdd:pfam05557 30 IELEKKASA-LKRQLDRESDR------NQELQKRIRLLE-KREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1489 DTKVLSELLVKLGSLGVH-QAPAQTLNETQRALESLRLQLDshgALHHKLRQLEE----------ESARQELQI------ 1551
Cdd:pfam05557 102 AREVISCLKNELSELRRQiQRAELELQSTNSELEELQERLD---LLKAKASEAEQlrqnlekqqsSLAEAEQRIkelefe 178
|
170 180
....*....|....*....|.
gi 66272331 1552 -QSFEDDLAEIRADKHNLETI 1571
Cdd:pfam05557 179 iQSQEQDSEIVKNSKSELARI 199
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1174-1492 |
6.44e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1174 ARSHRDTATKIEATSERALLASNASYELLKLMEGRVASEAQQELEDRYQEVQAAQTAlgiavAEALPKAEKALATVKQVI 1253
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-----AEAKKKADEAKKAEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1254 GDaaphlgllvtpeamnfQARGLSWKVKALEQKLEQKEPEVGQSVGALQVEAGRALEKMEPFMQLRNKTTAAFTRASSAV 1333
Cdd:PTZ00121 1524 AD----------------EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1334 QAAKVTVIGAETLLADLEGMKLRSPLPKEQAALK----KKAGSIRTRL------LEDTKRKT----KQAERMLGNAASLS 1399
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeelKKAEEEKKKVeqlkkkEAEEKKKAeelkKAEEENKIKAAEEA 1667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1400 SSTKKKSKEAELMSK---DNAKLSRALLREGKQGyRHASRLASQTQATLRRASRLLLTSEAHKQELEEAKQVTsglSTVE 1476
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKaeeDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA---EEDK 1743
|
330
....*....|....*.
gi 66272331 1477 RQIRESRISLEKDTKV 1492
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKI 1759
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1430-1555 |
9.00e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1430 GYRHASRLASQTQATlrrasrllltSEAHKQELEEAkqvtsglstvERQIRESRISLEKDTKVLSELLVKLGSL-GVHQA 1508
Cdd:COG3096 971 SYEDAVGLLGENSDL----------NEKLRARLEQA----------EEARREAREQLRQAQAQYSQYNQVLASLkSSRDA 1030
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66272331 1509 PAQTLNETQRALESLRLQLDS-------------HGALHH---KLRQLEEESARQELQIQSFE 1555
Cdd:COG3096 1031 KQQTLQELEQELEELGVQADAeaeerarirrdelHEELSQnrsRRSQLEKQLTRCEAEMDSLQ 1093
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
767-819 |
9.41e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.49 E-value: 9.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 66272331 767 CPCPGQSACATIPESGDVVCtHCPPGQRGRRCESCEDGFFGDPlglSGAPQPC 819
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQC-LCKPGVTGRHCDRCKPGYYGLP---SDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1409-1570 |
1.04e-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: 43.21 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1409 AELMSKDNAKLSRAL--LREGKQGYRHASRLASQTQATLRRASRLLLTSEAHKQELE-EAKQVTSGLSTVERQIRESRIS 1485
Cdd:COG4942 19 ADAAAEAEAELEQLQqeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEqELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1486 LEKDTKVLSELLVKLGSLGVHQAP-----AQTLNETQRALESL----RLQLDSHGALHHKLRQLEEESARQELQIQSFED 1556
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLalllsPEDFLDAVRRLQYLkylaPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170
....*....|....
gi 66272331 1557 DLAEIRADKHNLET 1570
Cdd:COG4942 179 LLAELEEERAALEA 192
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1439-1564 |
1.06e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1439 SQTQATLRRASRLLLTSEAHKQELeeakqvTSGLSTV----ERQIRESRISLEKDTKVLSELLVKlgSLGVH----QAPA 1510
Cdd:pfam00038 145 RELQAQVSDTQVNVEMDAARKLDL------TSALAEIraqyEEIAAKNREEAEEWYQSKLEELQQ--AAARNgdalRSAK 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66272331 1511 QTLNETQRALESLRLQLDSH----GALHHKLRQLEE--ESARQELQ--IQSFEDDLAEIRAD 1564
Cdd:pfam00038 217 EEITELRRTIQSLEIELQSLkkqkASLERQLAETEEryELQLADYQelISELEAELQETRQE 278
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1115-1488 |
1.31e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1115 AQAGAQKTCIQLAELEETLQSSEEEvlraasalsfLASLQKGSSTptnwshlASEAQILARSHRDTATKIEATSERALLA 1194
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEK----------IAELEKALAE-------LRKELEELEEELEQLRKELEELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1195 SNASYELLKLMEGRVASEAQQELEDRyQEVQAAQTALgiavAEALPKAEKALATVKQVIGDaaphlgllVTPEAMNFQAR 1274
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKEL-TELEAEIEEL----EERLEEAEEELAEAEAEIEE--------LEAQIEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1275 glswkVKALEQKLEQKEPEVGQsvgaLQVEAGRALEKMEpfmQLRNKTTAAFTRASSAVQAAKVTVIGAETLLADLEgmK 1354
Cdd:TIGR02168 798 -----LKALREALDELRAELTL----LNEEAANLRERLE---SLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--E 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1355 LRSPLPKEQAALKKKagsirtrlledTKRKTKQAERMlgnaaslssstKKKSKEAELMSKDNAKLSRAL-----LREGKQ 1429
Cdd:TIGR02168 864 LEELIEELESELEAL-----------LNERASLEEAL-----------ALLRSELEELSEELRELESKRselrrELEELR 921
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 66272331 1430 GYRHASRLAsQTQATLRRASRLLLTSEAHKQELEEAKQVTSGLSTVERQIRESRISLEK 1488
Cdd:TIGR02168 922 EKLAQLELR-LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| TNFRSF5 |
cd13407 |
Tumor necrosis factor receptor superfamily member 5 (TNFRSF5), also known as CD40; TNFRSF5 ... |
721-832 |
1.33e-03 |
|
Tumor necrosis factor receptor superfamily member 5 (TNFRSF5), also known as CD40; TNFRSF5 (commonly known as CD40 and also as CDW40, p50, Bp50) is widely expressed in diverse cell types including B lymphocytes, dendritic cells, platelets, monocytes, endothelial cells, and fibroblasts. It is essential in mediating a wide variety of immune and inflammatory responses, including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation. Its natural immunomodulating ligand is CD40L, and a primary defect in the CD40/CD40L system is associated with X-linked hyper-IgM (XHIM) syndrome. It is also involved in tumorigenesis; CD40 expression is significantly higher in gastric carcinomas and it is associated with the lymphatic metastasis of cancer cells and their tumor node metastasis (TNM) classification. Upregulated levels of CD40/CD40L on B cells and T cells may play an important role in the immune pathogenesis of breast cancer. Consequently, the CD40/CD40L system serves as a link between tumorigenesis, atherosclerosis, and the immune system, and offers a potential target for drug therapy for related diseases, such as cancer, atherosclerosis, diabetes mellitus, and immunological rejection.
Pssm-ID: 276912 [Multi-domain] Cd Length: 161 Bit Score: 41.23 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 721 CNQHGTCDPNTG-------------ICLC--GHHTEGPSCERCMPGfygnafsgraddcQPCPcPGQSACATIPESGDVV 785
Cdd:cd13407 52 CHQHRYCDPNLGlrvqtegtaetdtTCTCqeGQHCTSEACETCALH-------------TSCK-PGFGVKQIATGVSDTI 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 66272331 786 CTHCPpgqrgrrcesceDGFFGDplgLSGAPQPCR---RCQCSGNVDLNA 832
Cdd:cd13407 118 CEPCP------------VGFFSN---VSSAFEKCHpwtSCETKGLVELQA 152
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1439-1578 |
1.53e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1439 SQTQATLRRASRLLLTSEAHKQELEEAkqvtsgLSTVERQIRESRISLEKDTKVLSELLVKL----GSLGVHQAPAQTLN 1514
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEK------LEELRLEVSELEEEIEELQKELYALANEIsrleQQKQILRERLANLE 315
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66272331 1515 ETQRALESLRLQLDSH-GALHHKLRQLEEESARQELQIQSFEDDLAEIRADKHNLETILSSLPEN 1578
Cdd:TIGR02168 316 RQLEELEAQLEELESKlDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
280-317 |
1.59e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 1.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 66272331 280 CKCN--GHASE-CEPNAaGQlaCRCQHNTTGVDCERCLPFF 317
Cdd:smart00180 1 CDCDpgGSASGtCDPDT-GQ--CECKPNVTGRRCDRCAPGY 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1080-1294 |
1.79e-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: 42.44 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1080 LQETRGTFLQQMVGLEDSVKATWEQLQVLRGHVHCAQAGAQKTCIQLAELEETLQSSEE---EVLRAA------SALSFL 1150
Cdd:COG4942 46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaELLRALyrlgrqPPLALL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1151 ASlqkgsstPTNWSHLASEAQILARSHRDTATKIEA-TSERALLASNAsyellklmegRVASEAQQELEDRYQEVQAAQT 1229
Cdd:COG4942 126 LS-------PEDFLDAVRRLQYLKYLAPARREQAEElRADLAELAALR----------AELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66272331 1230 ALGIAVAEalpkAEKALATVKQVIGDAAPHLgllvtpEAMNFQARGLSWKVKALEQKLEQKEPEV 1294
Cdd:COG4942 189 ALEALKAE----RQKLLARLEKELAELAAEL------AELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1417-1578 |
2.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1417 AKLSRALLREgkqgyrHASRLASQTQATLRRASRLLLTSEAHKQELEEAKQVTSG-----LSTVERQIRESRISLEKDTK 1491
Cdd:COG4913 286 AQRRLELLEA------ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrLEQLEREIERLERELEERER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1492 VLSELLVKLGSLGVhQAP--AQTLNETQRALESLRLQLDSHgalhhkLRQLEEESARQELQIQSFEDDLAEIRADKHNLE 1569
Cdd:COG4913 360 RRARLEALLAALGL-PLPasAEEFAALRAEAAALLEALEEE------LEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
....*....
gi 66272331 1570 TILSSLPEN 1578
Cdd:COG4913 433 RRKSNIPAR 441
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
335-385 |
3.47e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 3.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 66272331 335 PCNCSGH-SEECTFDrelyrstghGGHCQrCRDHTTGPHCERCEKNYYRWSP 385
Cdd:smart00180 2 DCDPGGSaSGTCDPD---------TGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1094-1497 |
4.03e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1094 LEDSVKATWEQLQVLRghvhcAQAgaqktciQLAELEETLQSSEEEVLRAASALSFLASLQKgsstptnWSHLASEAQIL 1173
Cdd:TIGR02168 191 LEDILNELERQLKSLE-----RQA-------EKAERYKELKAELRELELALLVLRLEELREE-------LEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1174 ARSHRDTATKIEATSErallasnaSYELLKLmegrvaseAQQELEDRYQEVQAAQTALGIAVAEAlpKAEKALAtvkqvi 1253
Cdd:TIGR02168 252 EEELEELTAELQELEE--------KLEELRL--------EVSELEEEIEELQKELYALANEISRL--EQQKQIL------ 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1254 gdaaphlgllvtpeamNFQARGLSWKVKALE---QKLEQKEPEVGQSVGALQVEAGRALEKMEpfmQLRNKttaaFTRAS 1330
Cdd:TIGR02168 308 ----------------RERLANLERQLEELEaqlEELESKLDELAEELAELEEKLEELKEELE---SLEAE----LEELE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1331 SAVQAAKVTVIGAETLLADLEgmklrsplpKEQAALKKKAGSIRTRLLEDTKRKTkQAERMLGNAASLSSSTKKKSKEAE 1410
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLR---------SKVAQLELQIASLNNEIERLEARLE-RLEDRRERLQQEIEELLKKLEEAE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1411 L--MSKDNAKLSRALLREGKQGYRHASRLASQTQ--ATLRRASRLLLTSEAHKQE----LEEAKQVTSGLSTVERQIRES 1482
Cdd:TIGR02168 435 LkeLQAELEELEEELEELQEELERLEEALEELREelEEAEQALDAAERELAQLQArldsLERLQENLEGFSEGVKALLKN 514
|
410
....*....|....*
gi 66272331 1483 RISLEKDTKVLSELL 1497
Cdd:TIGR02168 515 QSGLSGILGVLSELI 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1408-1581 |
9.07e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1408 EAEL-MSKDNAKLSR--ALLREGKQGYRHASRLASQTQ------ATLRRASRLLLTS--EAHKQELEEAKQVtsgLSTVE 1476
Cdd:TIGR02168 176 ETERkLERTRENLDRleDILNELERQLKSLERQAEKAErykelkAELRELELALLVLrlEELREELEELQEE---LKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1477 RQIRESRISLEKDTKVLSELLVKLGSLGVHQAPAQ-TLNETQRALESLRLQLDSHGAlhhKLRQLEEESARQELQIQSFE 1555
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQkELYALANEISRLEQQKQILRE---RLANLERQLEELEAQLEELE 329
|
170 180
....*....|....*....|....*.
gi 66272331 1556 DDLAEIRADKHNLETILSSLPENCAS 1581
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELES 355
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1125-1291 |
9.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1125 QLAELEETLQSSEEEVLRAASALSFLASLQKGSSTP-TNWSHLA--SEAQILARSHRDTATKIEATSERALLASNAsyel 1201
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrEALQRLAeySWDEIDVASAEREIAELEAELERLDASSDD---- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1202 LKLMEGRV--ASEAQQELEDRYQEVQAAQTALGIAVAEALPKAEKALATVKQVIG--------DAAPHLGLLVTPEAMNF 1271
Cdd:COG4913 687 LAALEEQLeeLEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelraLLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|
gi 66272331 1272 QARGLSWKVKALEQKLEQKE 1291
Cdd:COG4913 767 LRENLEERIDALRARLNRAE 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1210-1392 |
9.82e-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: 40.13 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1210 ASEAQQELEDRYQEVQAAQTALG------IAVAEALPKAEKALATVKQVIGDAAPHLgllvtpEAMNFQARGLSWKVKAL 1283
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAalkkeeKALLKQLAALERRIAALARRIRALEQEL------AALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66272331 1284 EQKLEQKEPEVGQSVGALQ-----------------VEAGRALEKMEPFMQLRNKTTAAFTRASSAVQAAKVTvigAETL 1346
Cdd:COG4942 96 RAELEAQKEELAELLRALYrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE---LEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 66272331 1347 LADLEgmKLRSPLPKEQAALKKKAgSIRTRLLEDTKRKTKQAERML 1392
Cdd:COG4942 173 RAELE--ALLAELEEERAALEALK-AERQKLLARLEKELAELAAEL 215
|
|
| |
