|
Name |
Accession |
Description |
Interval |
E-value |
| C1Q |
smart00110 |
Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
1094-1228 |
6.27e-45 |
|
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.
Pssm-ID: 128420 Cd Length: 135 Bit Score: 158.62 E-value: 6.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 1094 SYRYAPMVAFFASHTygMTIPG---PILFNNLDVNYGASYTPRTGKFRIPYLGVYVFKYTIESFSAHISGFLVVDGIDKL 1170
Cdd:smart00110 1 NYKAQPRSAFSVIRS--NRPPPpgqPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVM 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 1171 afeSENINSEIHCDRVLTGDALLELNYGQEVWLRL--AKGTIPAKFPPVTTFSGYLLYRT 1228
Cdd:smart00110 79 ---STYDEYQKGLYDVASGGALLQLRQGDQVWLELpdEKNGLYAGEYVDSTFSGFLLFPD 135
|
|
| C1q |
pfam00386 |
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ... |
1102-1225 |
2.57e-35 |
|
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.
Pssm-ID: 395310 [Multi-domain] Cd Length: 126 Bit Score: 130.87 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 1102 AFFASHTYGMTIPG--PILFNNLDVNYGASYTPRTGKFRIPYLGVYVFKYTIES-FSAHISGFLVVDGIDKLAFESENIN 1178
Cdd:pfam00386 1 AFSAGRTTGLTAPNeqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTvDGKSLYVSLVKNGQEVVSFYDQPQK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 45269141 1179 SEihcDRVLTGDALLELNYGQEVWLRLA--KGTIPAKFPPVTTFSGYLL 1225
Cdd:pfam00386 81 GS---LDVASGSVVLELQRGDEVWLQLTgyNGLYYDGSDTDSTFSGFLL 126
|
|
| EMI |
pfam07546 |
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ... |
208-277 |
5.28e-15 |
|
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.
Pssm-ID: 462204 Cd Length: 69 Bit Score: 70.91 E-value: 5.28e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45269141 208 KNWCAYvhtRLSPTVILDNQVTYV----PGGKGPCGWTGgSCPQRsQKISNPVYRMQHKIVTSLDWRCCPGYSG 277
Cdd:pfam07546 1 RNVCAY---KVVSCVVVTGTESYVqpvyKPYLTWCAGHR-RCSTY-RTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
1045-1077 |
2.95e-11 |
|
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.
Pssm-ID: 238011 Cd Length: 38 Bit Score: 59.19 E-value: 2.95e-11
10 20 30
....*....|....*....|....*....|....
gi 45269141 1045 C-SRHPCQNGGTCINGRTSFTCACRHPFTGDNCT 1077
Cdd:cd00054 5 CaSGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
|
|
| EGF |
pfam00008 |
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
1045-1075 |
8.63e-10 |
|
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.
Pssm-ID: 394967 Cd Length: 31 Bit Score: 54.70 E-value: 8.63e-10
10 20 30
....*....|....*....|....*....|.
gi 45269141 1045 CSRHPCQNGGTCINGRTSFTCACRHPFTGDN 1075
Cdd:pfam00008 1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
1045-1077 |
1.73e-08 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 51.48 E-value: 1.73e-08
10 20 30
....*....|....*....|....*....|....*
gi 45269141 1045 C-SRHPCQNGGTCINGRTSFTCACRHPFT-GDNCT 1077
Cdd:smart00179 5 CaSGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
296-743 |
1.24e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 296 AESHTAVGRGVAEQQQQQGCGDPEVMQKMTDQVNYQAMKLTLlqKKIDNISLTVNDVRN--TYSSLEGKVsEDKSREFQ- 372
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL--EKEQNKRLWDRDTGNsiTIDHLRREL-DDRNMEVQr 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 373 --SLLKGLKSKSINVLIRDIVREQFKifqNDMQETVaqlfktvSSLSEDLESTRQIIQKVNESV----VSIAAQQKFV-- 444
Cdd:pfam15921 431 leALLKAMKSECQGQMERQMAAIQGK---NESLEKV-------SSLTAQLESTKEMLRKVVEELtakkMTLESSERTVsd 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 445 ----LVQENR---PTLTDIVELR-----------------NHIVNVRQE---MTLTCEKPIKELEVKQTHLEGALE--QE 495
Cdd:pfam15921 501 ltasLQEKERaieATNAEITKLRsrvdlklqelqhlknegDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQlvGQ 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 496 HSRSILYYESLNKTLSklKEVHEQLLSTEQ---VSDQKNAPAAE---SVSNNVTEYMSTLH---------ENIKKQSlmm 560
Cdd:pfam15921 581 HGRTAGAMQVEKAQLE--KEINDRRLELQEfkiLKDKKDAKIREleaRVSDLELEKVKLVNagserlravKDIKQER--- 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 561 LQMFEDLHIQESKINNLTVSLEMEKESLRGECEDMlSKCRNDFKFQLKDTEENLHVLNQTL----------AEVLFPMDN 630
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKMQLKSAQSELEQTRNTLksmegsdghaMKVAMGMQK 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 631 KMDKMSEQLNDLTYDMEILQPLLEQGASLRQTMTYEQPKEAivirkkiENLTSAVNSLNFIIKELtkrhNLLRNEvqgrd 710
Cdd:pfam15921 735 QITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS-------QELSTVATEKNKMAGEL----EVLRSQ----- 798
|
490 500 510
....*....|....*....|....*....|...
gi 45269141 711 dalERRINEYALEMEDGLNKTMTIINNAIDFIQ 743
Cdd:pfam15921 799 ---ERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
339-744 |
1.95e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 339 QKKIDNISLTVNDVRNTYSSLEGKVSEDKSREFQSLLKGLKS------KSINVLIRDIVREQFKIfqNDMQETVAQLFKT 412
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSelknqeKKLEEIQNQISQNNKII--SQLNEQISQLKKE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 413 VSSL-SEDLESTRQIIQKVNESVVSIAAQQKFVlvQENRPTLTDIVELRNHIVNVRQEMTLTCEKpikeLEVKQTHLEgA 491
Cdd:TIGR04523 351 LTNSeSENSEKQRELEEKQNEIEKLKKENQSYK--QEIKNLESQINDLESKIQNQEKLNQQKDEQ----IKKLQQEKE-L 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 492 LEQEHSRSILYYESLNKTLSKLKE-------VHEQLLSTEQVSDQKnapaAESVSNNVTEYMSTLhENIKKQSLMMLQMF 564
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQ----LKVLSRSINKIKQNL-EQKQKELKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 565 EDLHIQESKINNLTVSLEMEKESLRgECEDMLSKCRNDFKFQLKDTEENLHVLNQTLA-----EVLFPMDNKMDKMSEQL 639
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLK-EKIEKLESEKKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQ 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 640 NDLTYDMEILQPLLEQgaslrqtmtYEQPKEAIviRKKIENLTSAVNSLNFIIKELTKRHNLLRNEVQGRDDALErRINE 719
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQ---------KEKEKKDL--IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN-KLKQ 645
|
410 420
....*....|....*....|....*
gi 45269141 720 YALEMEDGLNKTMTIINNAIDFIQD 744
Cdd:TIGR04523 646 EVKQIKETIKEIRNKWPEIIKKIKE 670
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
340-761 |
3.12e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.67 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 340 KKIDNISLTVNDVRNTYSSLEGKvsedKSREFQSLLKGLKSKSINV--LIRDIVREQFKIFQNDMQETVAQLFKTVSSLS 417
Cdd:PTZ00440 659 KSKEDLQTLLNTSKNEYEKLEFM----KSDNIDNIIKNLKKELQNLlsLKENIIKKQLNNIEQDISNSLNQYTIKYNDLK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 418 EDLES-----------TRQIIQKVNESVVSIAAQQKFVLVQENrpTLTDIVELRNHIVNVRQEMT---LTCEKPIKELEV 483
Cdd:PTZ00440 735 SSIEEykeeeeklevyKHQIINRKNEFILHLYENDKDLPDGKN--TYEEFLQYKDTILNKENKISndiNILKENKKNNQD 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 484 KQTHLEGALEQEHSRSILYYESLNKTLSKLKEVHEQLLSTEQVSDQKNAPAAESVSNNVTEYMSTLHENIKKQslmmlqm 563
Cdd:PTZ00440 813 LLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTL------- 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 564 feDLHIQESKINNLTV-SLEMEKESLRGECEDMLSKCRNDFKFQLKDTEENLHVLNQTLAEVLFPMDN-KMDKMSEQLND 641
Cdd:PTZ00440 886 --NIAINRSNSNKQLVeHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKIEKQLSDtKINNLKMQIEK 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 642 LTYDMEILQPLLEQGASLRQTMTYEQPKEAIVIRKKIENLTSAVNSLN-----FIIKELTKRHNLLRNEVQGRDDALERR 716
Cdd:PTZ00440 964 TLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNILNkkiddLIKKQHDDIIELIDKLIKEKGKEIEEK 1043
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 45269141 717 INEYALEMEDGLNKTMTI-INNAIDFIQDNyALKETLSTIKDNSEI 761
Cdd:PTZ00440 1044 VDQYISLLEKMKTKLSSFhFNIDIKKYKNP-KIKEEIKLLEEKVEA 1088
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
676-873 |
6.14e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 676 KKIENLTSAVNSLNFIIKELTKRHNLLRNEVQGRDDALERRINEYALEmEDGLNKTMTIINN---------AIDFIQD-- 744
Cdd:TIGR01612 730 KKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKE-KDELNKYKSKISEiknhyndqiNIDNIKDed 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 745 ---NY-ALKETLSTIKDNSEIHHKCTSDM----ETILTFIPQFHRLNDSIQTLVNDNQRyNFVLQVAKTLAGIpRDEKLN 816
Cdd:TIGR01612 809 akqNYdKSKEYIKTISIKEDEIFKIINEMkfmkDDFLNKVDKFINFENNCKEKIDSEHE-QFAELTNKIKAEI-SDDKLN 886
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45269141 817 --QSNFQKMYQMFNETTSQVRKYQQNMSHLEE-----KLLLTTKIS-KNFETRLQDIESKVTQTL 873
Cdd:TIGR01612 887 dyEKKFNDSKSLINEINKSIEEEYQNINTLKKvdeyiKICENTKESiEKFHNKQNILKEILNKNI 951
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| C1Q |
smart00110 |
Complement component C1q domain; Globular domain found in many collagens and eponymously in ... |
1094-1228 |
6.27e-45 |
|
Complement component C1q domain; Globular domain found in many collagens and eponymously in complement C1q. When part of full length proteins these domains form a 'bouquet' due to the multimerization of heterotrimers. The C1q fold is similar to that of tumour necrosis factor.
Pssm-ID: 128420 Cd Length: 135 Bit Score: 158.62 E-value: 6.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 1094 SYRYAPMVAFFASHTygMTIPG---PILFNNLDVNYGASYTPRTGKFRIPYLGVYVFKYTIESFSAHISGFLVVDGIDKL 1170
Cdd:smart00110 1 NYKAQPRSAFSVIRS--NRPPPpgqPIRFDKVLYNQQGHYDPRTGKFTCPVPGVYYFSYHVESKGRNVKVSLMKNGIQVM 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 1171 afeSENINSEIHCDRVLTGDALLELNYGQEVWLRL--AKGTIPAKFPPVTTFSGYLLYRT 1228
Cdd:smart00110 79 ---STYDEYQKGLYDVASGGALLQLRQGDQVWLELpdEKNGLYAGEYVDSTFSGFLLFPD 135
|
|
| C1q |
pfam00386 |
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement ... |
1102-1225 |
2.57e-35 |
|
C1q domain; C1q is a subunit of the C1 enzyme complex that activates the serum complement system.
Pssm-ID: 395310 [Multi-domain] Cd Length: 126 Bit Score: 130.87 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 1102 AFFASHTYGMTIPG--PILFNNLDVNYGASYTPRTGKFRIPYLGVYVFKYTIES-FSAHISGFLVVDGIDKLAFESENIN 1178
Cdd:pfam00386 1 AFSAGRTTGLTAPNeqPVRFDKVLTNIGGHYDPATGKFTCPVPGVYYFSYHITTvDGKSLYVSLVKNGQEVVSFYDQPQK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 45269141 1179 SEihcDRVLTGDALLELNYGQEVWLRLA--KGTIPAKFPPVTTFSGYLL 1225
Cdd:pfam00386 81 GS---LDVASGSVVLELQRGDEVWLQLTgyNGLYYDGSDTDSTFSGFLL 126
|
|
| EMI |
pfam07546 |
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ... |
208-277 |
5.28e-15 |
|
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.
Pssm-ID: 462204 Cd Length: 69 Bit Score: 70.91 E-value: 5.28e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45269141 208 KNWCAYvhtRLSPTVILDNQVTYV----PGGKGPCGWTGgSCPQRsQKISNPVYRMQHKIVTSLDWRCCPGYSG 277
Cdd:pfam07546 1 RNVCAY---KVVSCVVVTGTESYVqpvyKPYLTWCAGHR-RCSTY-RTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
1045-1077 |
2.95e-11 |
|
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.
Pssm-ID: 238011 Cd Length: 38 Bit Score: 59.19 E-value: 2.95e-11
10 20 30
....*....|....*....|....*....|....
gi 45269141 1045 C-SRHPCQNGGTCINGRTSFTCACRHPFTGDNCT 1077
Cdd:cd00054 5 CaSGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
|
|
| EGF |
pfam00008 |
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
1045-1075 |
8.63e-10 |
|
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.
Pssm-ID: 394967 Cd Length: 31 Bit Score: 54.70 E-value: 8.63e-10
10 20 30
....*....|....*....|....*....|.
gi 45269141 1045 CSRHPCQNGGTCINGRTSFTCACRHPFTGDN 1075
Cdd:pfam00008 1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
|
|
| EGF |
cd00053 |
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
1045-1077 |
5.68e-09 |
|
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.
Pssm-ID: 238010 Cd Length: 36 Bit Score: 52.48 E-value: 5.68e-09
10 20 30
....*....|....*....|....*....|....*
gi 45269141 1045 CSR-HPCQNGGTCINGRTSFTCACRHPFTGD-NCT 1077
Cdd:cd00053 2 CAAsNPCSNGGTCVNTPGSYRCVCPPGYTGDrSCE 36
|
|
| EGF_CA |
smart00179 |
Calcium-binding EGF-like domain; |
1045-1077 |
1.73e-08 |
|
Calcium-binding EGF-like domain;
Pssm-ID: 214542 [Multi-domain] Cd Length: 39 Bit Score: 51.48 E-value: 1.73e-08
10 20 30
....*....|....*....|....*....|....*
gi 45269141 1045 C-SRHPCQNGGTCINGRTSFTCACRHPFT-GDNCT 1077
Cdd:smart00179 5 CaSGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
296-743 |
1.24e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 296 AESHTAVGRGVAEQQQQQGCGDPEVMQKMTDQVNYQAMKLTLlqKKIDNISLTVNDVRN--TYSSLEGKVsEDKSREFQ- 372
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL--EKEQNKRLWDRDTGNsiTIDHLRREL-DDRNMEVQr 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 373 --SLLKGLKSKSINVLIRDIVREQFKifqNDMQETVaqlfktvSSLSEDLESTRQIIQKVNESV----VSIAAQQKFV-- 444
Cdd:pfam15921 431 leALLKAMKSECQGQMERQMAAIQGK---NESLEKV-------SSLTAQLESTKEMLRKVVEELtakkMTLESSERTVsd 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 445 ----LVQENR---PTLTDIVELR-----------------NHIVNVRQE---MTLTCEKPIKELEVKQTHLEGALE--QE 495
Cdd:pfam15921 501 ltasLQEKERaieATNAEITKLRsrvdlklqelqhlknegDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQlvGQ 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 496 HSRSILYYESLNKTLSklKEVHEQLLSTEQ---VSDQKNAPAAE---SVSNNVTEYMSTLH---------ENIKKQSlmm 560
Cdd:pfam15921 581 HGRTAGAMQVEKAQLE--KEINDRRLELQEfkiLKDKKDAKIREleaRVSDLELEKVKLVNagserlravKDIKQER--- 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 561 LQMFEDLHIQESKINNLTVSLEMEKESLRGECEDMlSKCRNDFKFQLKDTEENLHVLNQTL----------AEVLFPMDN 630
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKMQLKSAQSELEQTRNTLksmegsdghaMKVAMGMQK 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 631 KMDKMSEQLNDLTYDMEILQPLLEQGASLRQTMTYEQPKEAivirkkiENLTSAVNSLNFIIKELtkrhNLLRNEvqgrd 710
Cdd:pfam15921 735 QITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS-------QELSTVATEKNKMAGEL----EVLRSQ----- 798
|
490 500 510
....*....|....*....|....*....|...
gi 45269141 711 dalERRINEYALEMEDGLNKTMTIINNAIDFIQ 743
Cdd:pfam15921 799 ---ERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
416-897 |
4.52e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 54.34 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 416 LSEDLESTRQIIQKVNESVVSIAAQQKFVLVQ----ENR-PTLTDIVELRNHIVNVRQEMTLTCEKPIKELEVKQTHLEG 490
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQitekENKmKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 491 ALEQehsrsilYYESLNKTLSKLKEVHEQL-LSTE---QVSDQKNAPAAESVSNNVTEYMSTLHENIKKQSLMMLQMFED 566
Cdd:pfam05483 297 ELED-------IKMSLQRSMSTQKALEEDLqIATKticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 567 LHIQESKINNLTVSLEMEKESlrGECEDMlSKCRNDFKFQLKDteenlhvLNQTLAE--VLFPMDNKMDKMSEQLNDLTY 644
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKS--SELEEM-TKFKNNKEVELEE-------LKKILAEdeKLLDEKKQFEKIAEELKGKEQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 645 DMEILQPLLEQ-----GASLRQTMTYEQ--PKEAIVIRKKIEN-------LTSAVNSLNFIIKELTKRHNLLRNEVQGRD 710
Cdd:pfam05483 440 ELIFLLQAREKeihdlEIQLTAIKTSEEhyLKEVEDLKTELEKeklknieLTAHCDKLLLENKELTQEASDMTLELKKHQ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 711 DALE--RRINEYALEMEDGLNKTMTIINNAIDFIQDNYalketlstIKDNSEIhhKCTSDMETILTFIPQFHRLNDSIQT 788
Cdd:pfam05483 520 EDIIncKKQEERMLKQIENLEEKEMNLRDELESVREEF--------IQKGDEV--KCKLDKSEENARSIEYEVLKKEKQM 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 789 LVNDNQRYNFVLQVAKTLAGIprdEKLNQSNfQKMYQMFNETTSQVRKYQQNMSHLEEKLLLTTK----ISKNFETRLQD 864
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNI---EELHQEN-KALKKKGSAENKQLNAYEIKVNKLELELASAKQkfeeIIDNYQKEIED 665
|
490 500 510
....*....|....*....|....*....|...
gi 45269141 865 ieSKVTQTLIpyYISVKKGSVVTnerDQALQLQ 897
Cdd:pfam05483 666 --KKISEEKL--LEEVEKAKAIA---DEAVKLQ 691
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
339-744 |
1.95e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 339 QKKIDNISLTVNDVRNTYSSLEGKVSEDKSREFQSLLKGLKS------KSINVLIRDIVREQFKIfqNDMQETVAQLFKT 412
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSelknqeKKLEEIQNQISQNNKII--SQLNEQISQLKKE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 413 VSSL-SEDLESTRQIIQKVNESVVSIAAQQKFVlvQENRPTLTDIVELRNHIVNVRQEMTLTCEKpikeLEVKQTHLEgA 491
Cdd:TIGR04523 351 LTNSeSENSEKQRELEEKQNEIEKLKKENQSYK--QEIKNLESQINDLESKIQNQEKLNQQKDEQ----IKKLQQEKE-L 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 492 LEQEHSRSILYYESLNKTLSKLKE-------VHEQLLSTEQVSDQKnapaAESVSNNVTEYMSTLhENIKKQSLMMLQMF 564
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQ----LKVLSRSINKIKQNL-EQKQKELKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 565 EDLHIQESKINNLTVSLEMEKESLRgECEDMLSKCRNDFKFQLKDTEENLHVLNQTLA-----EVLFPMDNKMDKMSEQL 639
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLK-EKIEKLESEKKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQ 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 640 NDLTYDMEILQPLLEQgaslrqtmtYEQPKEAIviRKKIENLTSAVNSLNFIIKELTKRHNLLRNEVQGRDDALErRINE 719
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQ---------KEKEKKDL--IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN-KLKQ 645
|
410 420
....*....|....*....|....*
gi 45269141 720 YALEMEDGLNKTMTIINNAIDFIQD 744
Cdd:TIGR04523 646 EVKQIKETIKEIRNKWPEIIKKIKE 670
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
338-821 |
4.26e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 338 LQKKIDNISLTVNDVRNTYSSLEG----------KVSEDKSREFQSLLKGLKSKSINVL--------IRDIVR-EQFKIF 398
Cdd:pfam05483 294 LTKELEDIKMSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKAAHSFVVTefeattcsLEELLRtEQQRLE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 399 QNDMQETV--AQLFKTVSSLSEDLESTRQIIQKVNESVVSIAAQQKfvLVQENRptltDIVELRNHIVNVRQEMTL---T 473
Cdd:pfam05483 374 KNEDQLKIitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEK--LLDEKK----QFEKIAEELKGKEQELIFllqA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 474 CEKPIKELEVKQTHLEGAlEQEHSRSIlyyESLNKTLSKLKEVHEQLLSTEQVSDQKNAPAAESVSNNVTEYMSTLHE-- 551
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTS-EEHYLKEV---EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDii 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 552 NIKKQSLMMLQMFEDLHIQESKINNltvslemEKESLRGEcedmLSKCRNDFKFQLKDTEENlhvlNQTLAEVLFPMDNK 631
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLRD-------ELESVREE----FIQKGDEVKCKLDKSEEN----ARSIEYEVLKKEKQ 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 632 MDKMSEQLNDLtydmeilqplleqgaslrqtmtyeqpkeaiviRKKIENLTSAVNSLNFIIKELTKRHNLLRNEVqgrdD 711
Cdd:pfam05483 589 MKILENKCNNL--------------------------------KKQIENKNKNIEELHQENKALKKKGSAENKQL----N 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 712 ALERRINEYALEMEDGLNKTMTIINNAIDFIQDNYALKETL------------STIKDNSEIHHKCTsdmetiltfipqf 779
Cdd:pfam05483 633 AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLleevekakaiadEAVKLQKEIDKRCQ------------- 699
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 45269141 780 HRLNDSIQTLVNDNQRYNFVLQVAKTLAGIPRDEKLNQSNFQ 821
Cdd:pfam05483 700 HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAK 741
|
|
| EGF |
smart00181 |
Epidermal growth factor-like domain; |
1045-1076 |
7.18e-06 |
|
Epidermal growth factor-like domain;
Pssm-ID: 214544 Cd Length: 35 Bit Score: 44.04 E-value: 7.18e-06
10 20 30
....*....|....*....|....*....|....
gi 45269141 1045 CS-RHPCQNGgTCINGRTSFTCACRHPFTGD-NC 1076
Cdd:smart00181 2 CAsGGPCSNG-TCINTPGSYTCSCPPGYTGDkRC 34
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
340-761 |
3.12e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.67 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 340 KKIDNISLTVNDVRNTYSSLEGKvsedKSREFQSLLKGLKSKSINV--LIRDIVREQFKIFQNDMQETVAQLFKTVSSLS 417
Cdd:PTZ00440 659 KSKEDLQTLLNTSKNEYEKLEFM----KSDNIDNIIKNLKKELQNLlsLKENIIKKQLNNIEQDISNSLNQYTIKYNDLK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 418 EDLES-----------TRQIIQKVNESVVSIAAQQKFVLVQENrpTLTDIVELRNHIVNVRQEMT---LTCEKPIKELEV 483
Cdd:PTZ00440 735 SSIEEykeeeeklevyKHQIINRKNEFILHLYENDKDLPDGKN--TYEEFLQYKDTILNKENKISndiNILKENKKNNQD 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 484 KQTHLEGALEQEHSRSILYYESLNKTLSKLKEVHEQLLSTEQVSDQKNAPAAESVSNNVTEYMSTLHENIKKQslmmlqm 563
Cdd:PTZ00440 813 LLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKTL------- 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 564 feDLHIQESKINNLTV-SLEMEKESLRGECEDMLSKCRNDFKFQLKDTEENLHVLNQTLAEVLFPMDN-KMDKMSEQLND 641
Cdd:PTZ00440 886 --NIAINRSNSNKQLVeHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKIEKQLSDtKINNLKMQIEK 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 642 LTYDMEILQPLLEQGASLRQTMTYEQPKEAIVIRKKIENLTSAVNSLN-----FIIKELTKRHNLLRNEVQGRDDALERR 716
Cdd:PTZ00440 964 TLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNILNkkiddLIKKQHDDIIELIDKLIKEKGKEIEEK 1043
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 45269141 717 INEYALEMEDGLNKTMTI-INNAIDFIQDNyALKETLSTIKDNSEI 761
Cdd:PTZ00440 1044 VDQYISLLEKMKTKLSSFhFNIDIKKYKNP-KIKEEIKLLEEKVEA 1088
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
458-736 |
1.65e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 458 ELRNHIVNVRQEMTLTcEKPIKELEVKQTHLEGALEQEHSRsilyYESLNKTLSKLKEVHEQLLSTEqvsdqKNAPAAES 537
Cdd:PRK03918 190 NIEELIKEKEKELEEV-LREINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLE-----GSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 538 VSNNVTEYMSTLHENIKKQslmmlqmfedlhiqESKINNLTVSLEMEKESLRgecedmLSKCRNDFKFQLKDTEENLHVL 617
Cdd:PRK03918 260 KIRELEERIEELKKEIEEL--------------EEKVKELKELKEKAEEYIK------LSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 618 NQTLAEV------LFPMDNKMDKMSEQLNDLTYDMEILQP----------LLEQGASLRQTMTYEQPKEAIV-------- 673
Cdd:PRK03918 320 EEEINGIeerikeLEEKEERLEELKKKLKELEKRLEELEErhelyeeakaKKEELERLKKRLTGLTPEKLEKeleeleka 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45269141 674 ---IRKKIENLTSAVNSLNFIIKELTKRHNLLRNE-----VQGR---DDALERRINEYALEMEDGLNKTMTIIN 736
Cdd:PRK03918 400 keeIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGReltEEHRKELLEEYTAELKRIEKELKEIEE 473
|
|
| hEGF |
pfam12661 |
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ... |
1050-1067 |
3.30e-04 |
|
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.
Pssm-ID: 463660 Cd Length: 22 Bit Score: 38.85 E-value: 3.30e-04
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
387-650 |
9.79e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 387 IRDIVREQFKIFQNDMQETVAQLFKTVSSLSE-----DLESTRQIIQKVNESV--------VSIAAQQKfvlVQENRPTL 453
Cdd:pfam06160 220 YREMEEEGYALEHLNVDKEIQQLEEQLEENLAllenlELDEAEEALEEIEERIdqlydlleKEVDAKKY---VEKNLPEI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 454 TDIVElrnHIVNVRQEMTLtcekpikELE-VKQTHLEGALEQEHSRSilyyesLNKTLSKLKEVHEQLlstEQVSDQKNA 532
Cdd:pfam06160 297 EDYLE---HAEEQNKELKE-------ELErVQQSYTLNENELERVRG------LEKQLEELEKRYDEI---VERLEEKEV 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 533 PAAEsVSNNVTEYMSTLhENIKKQSLMMLQMFEDLHIQESKINN---------LTVSLEMEKESLRGecedmLSkcrNDF 603
Cdd:pfam06160 358 AYSE-LQEELEEILEQL-EEIEEEQEEFKESLQSLRKDELEAREkldefklelREIKRLVEKSNLPG-----LP---ESY 427
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 45269141 604 KFQLKDTEENLHVLNQTLAEVlfPMDnkMDKMSEQLNDLTYDMEILQ 650
Cdd:pfam06160 428 LDYFFDVSDEIEDLADELNEV--PLN--MDEVNRLLDEAQDDVDTLY 470
|
|
| EGF_3 |
pfam12947 |
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ... |
1045-1076 |
1.04e-03 |
|
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.
Pssm-ID: 463759 [Multi-domain] Cd Length: 36 Bit Score: 37.58 E-value: 1.04e-03
10 20 30
....*....|....*....|....*....|....*.
gi 45269141 1045 CSR--HPCQNGGTCINGRTSFTCACRHPFTGD--NC 1076
Cdd:pfam12947 1 CSDnnGGCHPNATCTNTGGSFTCTCNDGYTGDgvTC 36
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
334-1027 |
1.57e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 334 KLTLLQKKIDNISLTVNDVRNTYSSLE-GKVSEDKSREFQSLLKGLKSKSINVL-IRDIVREQFKIFQNDMQEtVAQLFK 411
Cdd:PTZ00440 451 KINELKKSINQLKTLISIMKSFYDLIIsEKDSMDSKEKKESSDSNYQEKVDELLqIINSIKEKNNIVNNNFKN-IEDYYI 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 412 TVSSLSEDLESTRQIIQKVNESVVSIAAQQKfvlvqENRPTLTDIvelRNHIVNVRQEMtltceKPIKELEvkqthlega 491
Cdd:PTZ00440 530 TIEGLKNEIEGLIELIKYYLQSIETLIKDEK-----LKRSMKNDI---KNKIKYIEENV-----DHIKDII--------- 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 492 leqehsrsilyyeSLNKTLSKLKEVHEQLLSTEQVSDQKNAPAAESVSNNVTEYMSTLHENIKKQSLMMLQMFEDLH--- 568
Cdd:PTZ00440 588 -------------SLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQELLDELSHFLDDHkyl 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 569 IQESKINNLTVSLEMEKESLRGECEDMLSKCRNDFKFQLKDTEENLHVLNQTLAEVLF-----PMDNKMDKMSEQLNDLT 643
Cdd:PTZ00440 655 YHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKKQLnnieqDISNSLNQYTIKYNDLK 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 644 YDMEilqplleqgaslrqtmTYEQPKEAIVIRKK--IENLTSAVNSLNFIIKELTKRHNLLRNEVQGRDDALERrineya 721
Cdd:PTZ00440 735 SSIE----------------EYKEEEEKLEVYKHqiINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNK------ 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 722 lemEDGLNKTMTIINNAIDFIQDNYALKETLS-TIKDNSEIHhkcTSDMETILTFIP-------------QFHRLNDSIQ 787
Cdd:PTZ00440 793 ---ENKISNDINILKENKKNNQDLLNSYNILIqKLEAHTEKN---DEELKQLLQKFPtedenlnlkelekEFNENNQIVD 866
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 788 TLVNDNQRYNFVLQVAKTLA-GIPRDEKLNQS------NFQKMYQMFNETTSQVRKYqqNMSHLEEKLLLTTKISK---N 857
Cdd:PTZ00440 867 NIIKDIENMNKNINIIKTLNiAINRSNSNKQLvehllnNKIDLKNKLEQHMKIINTD--NIIQKNEKLNLLNNLNKekeK 944
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 858 FETRLQDI-----ESKVTQTLIPYYISvkKGSVVTNERDQALQLQVLNSRFKALEAKSIHLSINFFSLNKTLHEVLTMCH 932
Cdd:PTZ00440 945 IEKQLSDTkinnlKMQIEKTLEYYDKS--KENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDLIKKQH 1022
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 933 NastsvselnatipKWIKHSLPDIQLLQKGLTEFVEPIIQI--KTQAALSNLTCCIDRSL---PGSLANVVKSQKQVKSL 1007
Cdd:PTZ00440 1023 D-------------DIIELIDKLIKEKGKEIEEKVDQYISLleKMKTKLSSFHFNIDIKKyknPKIKEEIKLLEEKVEAL 1089
|
730 740
....*....|....*....|
gi 45269141 1008 PKKINALKKPTVNLTTVLIG 1027
Cdd:PTZ00440 1090 LKKIDENKNKLIEIKNKSHE 1109
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
340-719 |
3.84e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 340 KKIDNISLTVNDVRNTYSSLEGKVS--EDKSREFQSLLKGLKSKsINVLiRDIVREQFKI------------FQNDMQET 405
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRklEEKIRELEERIEELKKE-IEEL-EEKVKELKELkekaeeyiklseFYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 406 VAQLFKTVSSLSEDLESTRQIIQKVNESVVSIAA--------QQKFVLVQENRPTLTDIVELRNHIVNVRQEMT-LTCEK 476
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkklkelEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 477 PIKELE-VKQTHLEgaLEQEHSRSILYYESLNKTLSKLKEVHEQLLSTEQVSDQKNAPAAESVSNNVTEYMSTLHENIKK 555
Cdd:PRK03918 389 LEKELEeLEKAKEE--IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 556 QslmmLQMFEDlhiQESKINNLTVSLEMEkesLRGECEdmLSKCRNDFKfQLKDTEENLHVLNqtlAEVLFPMDNKMDKM 635
Cdd:PRK03918 467 E----LKEIEE---KERKLRKELRELEKV---LKKESE--LIKLKELAE-QLKELEEKLKKYN---LEELEKKAEEYEKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 636 SEQLNDLTYDMEILQPLLEQGASLRqtmtyeqpKEAIVIRKKIENLTsavnslnfiiKELTKRHNLLRNEVQGRDDALER 715
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELK--------KKLAELEKKLDELE----------EELAELLKELEELGFESVEELEE 592
|
....
gi 45269141 716 RINE 719
Cdd:PRK03918 593 RLKE 596
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
482-866 |
5.26e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 482 EVKQTHLEGALEQEhsrsilyYESLNK-----TLSKLKEVHEQLLSTEQVSDQKNAPAAESVSNNVTEYMSTLHENIKKq 556
Cdd:PRK04778 52 KVKKLNLTGQSEEK-------FEEWRQkwdeiVTNSLPDIEEQLFEAEELNDKFRFRKAKHEINEIESLLDLIEEDIEQ- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 557 slmMLQMFEDLHIQESKINNLTVSLEMEKESLRgecEDMLSkcrNDFKF---------QLKDTEENLH---VLNQ----- 619
Cdd:PRK04778 124 ---ILEELQELLESEEKNREEVEQLKDLYRELR---KSLLA---NRFSFgpaldelekQLENLEEEFSqfvELTEsgdyv 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 620 TLAEVLfpmdnkmDKMSEQLNDLTYDMEILQPLL--------EQGASLRQtmTYEQ-------------PKEAIVIRKKI 678
Cdd:PRK04778 195 EAREIL-------DQLEEELAALEQIMEEIPELLkelqtelpDQLQELKA--GYRElveegyhldhldiEKEIQDLKEQI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 679 ENLTSAVNSLNF-----IIKELTKR----HNLLRNEVQGRDDALER--RINEYALEMEDGLNKTMTiinnAIDFIQDNY- 746
Cdd:PRK04778 266 DENLALLEELDLdeaeeKNEEIQERidqlYDILEREVKARKYVEKNsdTLPDFLEHAKEQNKELKE----EIDRVKQSYt 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 747 ----------ALKETLSTIKDNSEIHHKCTSD-----------METILTFIPQFH----RLNDSIQTLVNDNQRYN-FVL 800
Cdd:PRK04778 342 lneselesvrQLEKQLESLEKQYDEITERIAEqeiayselqeeLEEILKQLEEIEkeqeKLSEMLQGLRKDELEAReKLE 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 801 QVAKTLAGIPRdeKLNQSNF----QKMYQMFNETTSQVrkyQQNMSHLEEKLLLTTKISKNFETRLQDIE 866
Cdd:PRK04778 422 RYRNKLHEIKR--YLEKSNLpglpEDYLEMFFEVSDEI---EALAEELEEKPINMEAVNRLLEEATEDVE 486
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
676-873 |
6.14e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 676 KKIENLTSAVNSLNFIIKELTKRHNLLRNEVQGRDDALERRINEYALEmEDGLNKTMTIINN---------AIDFIQD-- 744
Cdd:TIGR01612 730 KKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKE-KDELNKYKSKISEiknhyndqiNIDNIKDed 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 745 ---NY-ALKETLSTIKDNSEIHHKCTSDM----ETILTFIPQFHRLNDSIQTLVNDNQRyNFVLQVAKTLAGIpRDEKLN 816
Cdd:TIGR01612 809 akqNYdKSKEYIKTISIKEDEIFKIINEMkfmkDDFLNKVDKFINFENNCKEKIDSEHE-QFAELTNKIKAEI-SDDKLN 886
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45269141 817 --QSNFQKMYQMFNETTSQVRKYQQNMSHLEE-----KLLLTTKIS-KNFETRLQDIESKVTQTL 873
Cdd:TIGR01612 887 dyEKKFNDSKSLINEINKSIEEEYQNINTLKKvdeyiKICENTKESiEKFHNKQNILKEILNKNI 951
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
455-761 |
6.65e-03 |
|
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: 40.82 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 455 DIVELRNHIVNVRQEMTlTCEKPIKELEVKQTHLEGALEQEHSRsilyyeslnktlskLKEVHEQLLSTEQvsdqknapa 534
Cdd:TIGR02169 696 ELRRIENRLDELSQELS-DASRKIGEIEKEIEQLEQEEEKLKER--------------LEELEEDLSSLEQ--------- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 535 aesvsnNVTEYMSTLHENIKKQSlmmlQMFEDLHIQESKINNLTVSLEMEK-ESLRGECEDMlskcrndfKFQLKDTEEN 613
Cdd:TIGR02169 752 ------EIENVKSELKELEARIE----ELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKL--------EEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 614 LHVLNQtlaevlfpmdnkmdkmseQLNDLTYDMEILQPLLeQGASLRQTMTYEQPKEaivIRKKIENLTSAVNSLNFIIK 693
Cdd:TIGR02169 814 LREIEQ------------------KLNRLTLEKEYLEKEI-QELQEQRIDLKEQIKS---IEKEIENLNGKKEELEEELE 871
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45269141 694 ELTKRHNLLRNEVQGRDDALERRINEYAlEMEDGLNKTMTIINNAIDFIQDnyaLKETLSTIKDN-SEI 761
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLR-ELERKIEELEAQIEKKRKRLSE---LKAKLEALEEElSEI 936
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
282-679 |
8.36e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 282 LRAQEQQSLIHTNQAEshtavgrgVAEQQQQQGCGDPEVmQKMTDQVNYQAMKLTLLQKKIDNISLTVNDVrntysslEG 361
Cdd:pfam10174 352 LRLEEKESFLNKKTKQ--------LQDLTEEKSTLAGEI-RDLKDMLDVKERKINVLQKKIENLQEQLRDK-------DK 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 362 KVSEDKSRefqslLKGLKSKSIN-----VLIRDIVREQFKIFQNdMQEtvaQLFKTVSSLSEDLESTRQIIQKVNESVvs 436
Cdd:pfam10174 416 QLAGLKER-----VKSLQTDSSNtdtalTTLEEALSEKERIIER-LKE---QREREDRERLEELESLKKENKDLKEKV-- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 437 iAAQQKFVLVQEnrptlTDIVELRNHIVNVRQEMTLtcekpiKELEVKQthLEGALEQEhsrsilyYESLNKTLSKLKEV 516
Cdd:pfam10174 485 -SALQPELTEKE-----SSLIDLKEHASSLASSGLK------KDSKLKS--LEIAVEQK-------KEECSKLENQLKKA 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 517 HEQllsteQVSDQKNAPAAESVSNNVTEYMSTLHENIKKQS----LM--MLQMFEDLHIQESKINnltvslEMEKESLRg 590
Cdd:pfam10174 544 HNA-----EEAVRTNPEINDRIRLLEQEVARYKEESGKAQAeverLLgiLREVENEKNDKDKKIA------ELESLTLR- 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 591 ECEDMLSKCRNDFKFQLKDTEENLhvlnQTLAEVLFPMDNKMDKMSE-QLNDLTYDME-ILQPLLEQGASLRQTMTYEQP 668
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQEMKKKGA----QLLEEARRREDNLADNSQQlQLEELMGALEkTRQELDATKARLSSTQQSLAE 687
|
410
....*....|.
gi 45269141 669 KEAIVIRKKIE 679
Cdd:pfam10174 688 KDGHLTNLRAE 698
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
321-947 |
8.46e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 321 MQKMTDQVNYQAMK-LTLLQKKIDNISLTVNDVRNtysslegkvSEDKSREFqSLLKGLKSKSINvlirdIVREQFKIFQ 399
Cdd:TIGR01612 1826 FKKKLDHVNDKFTKeYSKINEGFDDISKSIENVKN---------STDENLLF-DILNKTKDAYAG-----IIGKKYYSYK 1890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 400 NDMQETVAQLFKTVSSLSEDLESTRQI--IQKVNESVVSIAAQQ-----KFVLVQENRP-TLTDIVELRNHIVNVRQEMT 471
Cdd:TIGR01612 1891 DEAEKIFINISKLANSINIQIQNNSGIdlFDNINIAILSSLDSEkedtlKFIPSPEKEPeIYTKIRDSYDTLLDIFKKSQ 1970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 472 LTCEKPIKELEVKQTHlegaleQEHSRSILYYESLNKTLSKLKEVHEQLLSTEQV----SDQKNAPAAESvSNNVTEYMS 547
Cdd:TIGR01612 1971 DLHKKEQDTLNIIFEN------QQLYEKIQASNELKDTLSDLKYKKEKILNDVKLllhkFDELNKLSCDS-QNYDTILEL 2043
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 548 TLHENIK------KQSLMMLQMFEDLHIQESKINNLTVSLEmekeslrgecedmlsKCRNDFKFQLKDTEENLHVLNQTL 621
Cdd:TIGR01612 2044 SKQDKIKekidnyEKEKEKFGIDFDVKAMEEKFDNDIKDIE---------------KFENNYKHSEKDNHDFSEEKDNII 2108
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 622 AEvlfpmDNKMDKMSEQLNdlTYDMEILQPLLEQGASLRQTMtyEQPKEAIVIRKK--IENLTSAVNSLNFIIKELTKrh 699
Cdd:TIGR01612 2109 QS-----KKKLKELTEAFN--TEIKIIEDKIIEKNDLIDKLI--EMRKECLLFSYAtlVETLKSKVINHSEFITSAAK-- 2177
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 700 nllrnevqgrddalerrineYALEMEDGLNKTMTIINNAIDFIQDNYALKET--------LSTIKDNSEIHHKCTSDMET 771
Cdd:TIGR01612 2178 --------------------FSKDFFEFIEDISDSLNDDIDALQIKYNLNQTkkhmisilADATKDHNNLIEKEKEATKI 2237
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 772 I--LTFIPQFHRLNDSIQTLVNDN-QRYNFVLQVAKTLAGIprdeklnqsnfQKMYQmfnettsQVRKYQ-QNMSHLEEK 847
Cdd:TIGR01612 2238 InnLTELFTIDFNNADADILHNNKiQIIYFNSELHKSIESI-----------KKLYK-------KINAFKlLNISHINEK 2299
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45269141 848 LlltTKISKNFETRLQDIESKVTQTL-----IPYYISVKKGSVVtnerdQALQlQVLNSRFKALeaKSIHLSInfFSLNK 922
Cdd:TIGR01612 2300 Y---FDISKEFDNIIQLQKHKLTENLndlkeIDQYISDKKNIFL-----HALN-ENTNFNFNAL--KEIYDDI--INREN 2366
|
650 660
....*....|....*....|....*
gi 45269141 923 TLHEVLTMCHNASTSVSELNATIPK 947
Cdd:TIGR01612 2367 KADEIENINNKENENIMQYIDTITK 2391
|
|
|