|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
6-820 |
0e+00 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 804.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 6 MHIPIQPSPESTQSTNTTDNIDYFDISDESNYyLISQLRPHFSNIYFFDEFKRYA-SYHTEIKRYEDIHKTKVNSLLNEA 84
Cdd:PTZ00440 77 KRSLLQLSPSLVTLNNSNDNLDYIDVSDDNGN-LISSVYPHYVNIYYFKEMIHYAtSYYDDLKKYSDKINEDVEPLNEEI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 85 SRAIGICNRAKNTVKGLINILENPQKFKTQRESYDVKLRQYEEKKEAFRGCLLNKNRKNLDQIKKINNEIRDLLEKLKCS 164
Cdd:PTZ00440 156 IKNIEQCLGNKNDLDNLIIVLENPEKYNVRKTLYDEKFNEYKNKKEAFYNCLKNKKEDYDKKIKKINNEIRKLLKNIKCT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 165 -QDCQTNVYFDMIKIYLVDFKKMPYENYDTFIKQYKNSYLSGVDMIRKIEKQIDNPVTINAIKFTQKEMGYIIDRFEYHL 243
Cdd:PTZ00440 236 gNMCKTDTYVDMVELYLLRVNEVPSNNYDNYLNRAKELLESGSDLINKIKKELGDNKTIYSINFIQEEIGDIIKRYNFHL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 244 QKVKHSIDQVTALSDGVKPKQVTKNRLKEYYFNIGNYYSIFKFGKDSLNMLNKALIHKEKIVHNLLGELFGHLEERISKL 323
Cdd:PTZ00440 316 KKIEKGKEYIKRIQNNNIPPQVKKDELKKKYFESAKHYASFKFSLEMLSMLDSLLIKKEKILNNLFNKLFGDLKEKIETL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 324 IDSEYFITESNNIISQSEETLKLAEDVYDKNTKLIEDLTLYPHLEINEFKKDYDNNVEDLRESIIYIQSYVSSIKSAYRY 403
Cdd:PTZ00440 396 LDSEYFISKYTNIISLSEHTLKAAEDVLKENSQKIADYALYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMKSFYDL 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 404 NVLEKDSVESKQKNIPANSNAQKKVDELLSIIDSISYSNFSVAENFQKMKDYYKEIEKLKIKILQLIEAIKKYQQHVEEL 483
Cdd:PTZ00440 476 IISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETL 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 484 INKEKAVAILKEDINKIIEYIKGIIEKLKQLISANKDFDKIFQQVEQLINEALFNKDQFEHNKNDLHTKMKEIMHTFHER 563
Cdd:PTZ00440 556 IKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKG 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 564 DLQQFLDNMSKFLKDQEASYQNADSKEKLDQLLTTVKAKQDELKEMKCDDIPDIIDNLKKESQNVLNLKDEVINKQFENM 643
Cdd:PTZ00440 636 DLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKKQLNNI 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 644 RTEMSSSLDQMTKEYNALKSSIEEYEAEKKGIENHKQNIIKRKNTFIVAEHENDEDVPEGKNTYNEFISNKDTILQKESA 723
Cdd:PTZ00440 716 EQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENK 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 724 ISNQMNTLEEKKRNRKTTLQTYGDAIQKLETYTEKKDEETKVLLDKFNTEVENFKLDEDEKSFNDAKSIVSNTINEVENE 803
Cdd:PTZ00440 796 ISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENM 875
|
810
....*....|....*..
6D05_E 804 NKNIDSIKKVNIAMKRS 820
Cdd:PTZ00440 876 NKNINIIKTLNIAINRS 892
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
371-818 |
7.49e-15 |
|
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: 79.33 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 371 EFKKDYDNNVED---LRESIIYIQSYVSSIKSAYRYnvlEKDSVESKqkNIPANSNAQKKVDELLSIIDSISYSNFSVAE 447
Cdd:TIGR01612 480 DIKKDIDENSKQdntVKLILMRMKDFKDIIDFMELY---KPDEVPSK--NIIGFDIDQNIKAKLYKEIEAGLKESYELAK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 448 NFQKMK-DYYKEIEKLKIKILQLIEAIK----KYQQHVEELINKEKAVAILKEDINKII---EYIKGIIEkLKQLISANK 519
Cdd:TIGR01612 555 NWKKLIhEIKKELEEENEDSIHLEKEIKdlfdKYLEIDDEIIYINKLKLELKEKIKNISdknEYIKKAID-LKKIIENNN 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 520 DFdkifqqVEQLINEALFNKDQFEHNKNDLHTKMKEIMHTFHERDLQQFLDNMSKFLkdQEASYQNADSKEKLDQLLTTV 599
Cdd:TIGR01612 634 AY------IDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIV--KENAIDNTEDKAKLDDLKSKI 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 600 KAKQDELKEMKCDDIPDIIDNLKKESQNVLNLKDEVINKQFENMRTEMSSSLDQMTKEYNALKSSIEEYEAEKKGIENHK 679
Cdd:TIGR01612 706 DKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYK 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 680 QNIIKRKNTFIVAEHENDEDVPEGKNTYNEFISNKDTILQKESAISNQMNTLEEKKRNRKTTLQTYGDAIQKLETYTEKK 759
Cdd:TIGR01612 786 SKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSE 865
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
6D05_E 760 DEETKVLLDKFNTEVENFKLDEDEKSFNDAKSIVSNTINEVENENKNIDSIKKVNIAMK 818
Cdd:TIGR01612 866 HEQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIK 924
|
|
| Rh5 |
pfam18515 |
Rh5 coiled-coil domain; This is a helical coiled-coil domain found in reticulocyte-binding ... |
74-327 |
1.37e-13 |
|
Rh5 coiled-coil domain; This is a helical coiled-coil domain found in reticulocyte-binding protein homolog 5 (RH5), a Plasmodium falciparum protein essential for erythrocyte invasion.
Pssm-ID: 436554 [Multi-domain] Cd Length: 255 Bit Score: 71.63 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 74 KTKVNSLLNEASRAIGICNRAKNTVKGLINILENPQKFKTQRESYDVKlRQYEEKKEAFRGCLLNKNRKNLDQIKKINNE 153
Cdd:pfam18515 2 WPKIDKVSKDIIKNKEECEPKKKELINEVDNLENPEYNFYNRPYSNDY-NSYKKSKTNFVNCLLPKFKKLYKKINYIISY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 154 IRDLLEKLKCSQD-CQTNVYFDMIKIYLVDFKKMPYENYDTFIKQYKNSYLSGVDMIRKIEKQIDNPVTINAIKFTQKEM 232
Cdd:pfam18515 81 IKYLYKIYCYNENkCSDKIYKKRLKIVKNEINNFLSKIKKWAINKDKEVIPFINSLITILKSENEPKNLSDKLDFIKKQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 233 GYIIDRFEYHLQKVKHSIDQVTALSDGVKPKQVTKNRLKEYYFNIGNYYSIFKFGKDSLNMLNKALIHKEKIVHNLLGEL 312
Cdd:pfam18515 161 EDIIKKSNKHLEKCKCASDYVKKIQKEKKPNKYYKYELFNEIKKLATHYSIFKYNYEHLINLESVYKTKKEILNNFFNKL 240
|
250
....*....|....*
6D05_E 313 FGHLEERISKLIDSE 327
Cdd:pfam18515 241 GKLLINKVDPDINSI 255
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
475-671 |
1.23e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.97 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 475 KYQQHVEELIN--KEKAVAILKEDINKIIEYIKGIIEKLKQL---ISANKD-FDKIFQQVEQLINEALFNKDQFEHNKND 548
Cdd:cd00176 4 QFLRDADELEAwlSEKEELLSSTDYGDDLESVEALLKKHEALeaeLAAHEErVEALNELGEQLIEEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 549 LHTKMKEIMHTFHER--------DLQQFLDNMSKFLKDQEASYQNADSkEKLDQLLTTVKAKQDELKEMKcddipDIIDN 620
Cdd:cd00176 84 LNQRWEELRELAEERrqrleealDLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELE-----EELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
6D05_E 621 LKKESQNVLNLKDEVINKQFENMRTEMSSSLDQMTKEYNALKSSIEEYEAE 671
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
450-687 |
2.98e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 450 QKMKDYYKEIEKLKIKILQLIEAIKKYQQHVEELINKEKAvaiLKEDINKIIEYIKGIIEKLKQLISANKDFDKIFQQVE 529
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---LREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 530 QLINEALFNKDQFEHNKNDLHTKMKEI-----------MHTFHERDLQQFLDNMSKFLKDQEASyqnADSKEKLDQLLTT 598
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIerlewrqqtevLSPEEEKELVEKIKELEKELEKAKKA---LEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 599 VKAKQDELKEmkcddIPDIIDNLKKESQNVLNLKDEVINK---------QFENMRTEMSSSLDQMTKEYNALKSSIEEYE 669
Cdd:COG1340 169 LKELRKEAEE-----IHKKIKELAEEAQELHEEMIELYKEadelrkeadELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250
....*....|....*...
6D05_E 670 AEKKGIENHKQNIIKRKN 687
Cdd:COG1340 244 KELKKLRKKQRALKREKE 261
|
|
| CAS_csx29_CRASP |
NF041237 |
type III-E CRISPR-associated TPR-CHAT protein Csx29; Csx29, the protease subunit of the ... |
380-513 |
4.15e-03 |
|
type III-E CRISPR-associated TPR-CHAT protein Csx29; Csx29, the protease subunit of the craspase complex, is a TPR-CHAP family protein of type III-E CRISPR/Cas systems. Craspase is guided by crRNA, but cleaves protein, not nucleotide, and therefore is highly interesting for potential technological applications.
Pssm-ID: 469139 [Multi-domain] Cd Length: 669 Bit Score: 40.81 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 380 VEDLRESIIYIQSYV-SSIKSAYRYNVLEKDSVEskQKNIPANSNAQKKVDELLsiIDSISYSNFSVAENFQKMKDY--Y 456
Cdd:NF041237 54 KEALKKALRLAEKAIdNKEKNLEALRLKAQALLE--LERINKDEDSEKTLKELL--EEAVQNGCNDFIAELEDIEIFlrY 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
6D05_E 457 KEIEKLKIKILQLIEAIKKYQQHVEELINKEKAVAILKEDINKIIEYIKGIIEKLKQ 513
Cdd:NF041237 130 SERDKLLDKIEYLLQIIGSWLSNNDELLLKAKLAAILNKANDDVDKYLNKAIEKAPK 186
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
6-820 |
0e+00 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 804.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 6 MHIPIQPSPESTQSTNTTDNIDYFDISDESNYyLISQLRPHFSNIYFFDEFKRYA-SYHTEIKRYEDIHKTKVNSLLNEA 84
Cdd:PTZ00440 77 KRSLLQLSPSLVTLNNSNDNLDYIDVSDDNGN-LISSVYPHYVNIYYFKEMIHYAtSYYDDLKKYSDKINEDVEPLNEEI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 85 SRAIGICNRAKNTVKGLINILENPQKFKTQRESYDVKLRQYEEKKEAFRGCLLNKNRKNLDQIKKINNEIRDLLEKLKCS 164
Cdd:PTZ00440 156 IKNIEQCLGNKNDLDNLIIVLENPEKYNVRKTLYDEKFNEYKNKKEAFYNCLKNKKEDYDKKIKKINNEIRKLLKNIKCT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 165 -QDCQTNVYFDMIKIYLVDFKKMPYENYDTFIKQYKNSYLSGVDMIRKIEKQIDNPVTINAIKFTQKEMGYIIDRFEYHL 243
Cdd:PTZ00440 236 gNMCKTDTYVDMVELYLLRVNEVPSNNYDNYLNRAKELLESGSDLINKIKKELGDNKTIYSINFIQEEIGDIIKRYNFHL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 244 QKVKHSIDQVTALSDGVKPKQVTKNRLKEYYFNIGNYYSIFKFGKDSLNMLNKALIHKEKIVHNLLGELFGHLEERISKL 323
Cdd:PTZ00440 316 KKIEKGKEYIKRIQNNNIPPQVKKDELKKKYFESAKHYASFKFSLEMLSMLDSLLIKKEKILNNLFNKLFGDLKEKIETL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 324 IDSEYFITESNNIISQSEETLKLAEDVYDKNTKLIEDLTLYPHLEINEFKKDYDNNVEDLRESIIYIQSYVSSIKSAYRY 403
Cdd:PTZ00440 396 LDSEYFISKYTNIISLSEHTLKAAEDVLKENSQKIADYALYSNLEIIEIKKKYDEKINELKKSINQLKTLISIMKSFYDL 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 404 NVLEKDSVESKQKNIPANSNAQKKVDELLSIIDSISYSNFSVAENFQKMKDYYKEIEKLKIKILQLIEAIKKYQQHVEEL 483
Cdd:PTZ00440 476 IISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETL 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 484 INKEKAVAILKEDINKIIEYIKGIIEKLKQLISANKDFDKIFQQVEQLINEALFNKDQFEHNKNDLHTKMKEIMHTFHER 563
Cdd:PTZ00440 556 IKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKG 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 564 DLQQFLDNMSKFLKDQEASYQNADSKEKLDQLLTTVKAKQDELKEMKCDDIPDIIDNLKKESQNVLNLKDEVINKQFENM 643
Cdd:PTZ00440 636 DLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKKQLNNI 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 644 RTEMSSSLDQMTKEYNALKSSIEEYEAEKKGIENHKQNIIKRKNTFIVAEHENDEDVPEGKNTYNEFISNKDTILQKESA 723
Cdd:PTZ00440 716 EQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENK 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 724 ISNQMNTLEEKKRNRKTTLQTYGDAIQKLETYTEKKDEETKVLLDKFNTEVENFKLDEDEKSFNDAKSIVSNTINEVENE 803
Cdd:PTZ00440 796 ISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENM 875
|
810
....*....|....*..
6D05_E 804 NKNIDSIKKVNIAMKRS 820
Cdd:PTZ00440 876 NKNINIIKTLNIAINRS 892
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
371-818 |
7.49e-15 |
|
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: 79.33 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 371 EFKKDYDNNVED---LRESIIYIQSYVSSIKSAYRYnvlEKDSVESKqkNIPANSNAQKKVDELLSIIDSISYSNFSVAE 447
Cdd:TIGR01612 480 DIKKDIDENSKQdntVKLILMRMKDFKDIIDFMELY---KPDEVPSK--NIIGFDIDQNIKAKLYKEIEAGLKESYELAK 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 448 NFQKMK-DYYKEIEKLKIKILQLIEAIK----KYQQHVEELINKEKAVAILKEDINKII---EYIKGIIEkLKQLISANK 519
Cdd:TIGR01612 555 NWKKLIhEIKKELEEENEDSIHLEKEIKdlfdKYLEIDDEIIYINKLKLELKEKIKNISdknEYIKKAID-LKKIIENNN 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 520 DFdkifqqVEQLINEALFNKDQFEHNKNDLHTKMKEIMHTFHERDLQQFLDNMSKFLkdQEASYQNADSKEKLDQLLTTV 599
Cdd:TIGR01612 634 AY------IDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIV--KENAIDNTEDKAKLDDLKSKI 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 600 KAKQDELKEMKCDDIPDIIDNLKKESQNVLNLKDEVINKQFENMRTEMSSSLDQMTKEYNALKSSIEEYEAEKKGIENHK 679
Cdd:TIGR01612 706 DKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYK 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 680 QNIIKRKNTFIVAEHENDEDVPEGKNTYNEFISNKDTILQKESAISNQMNTLEEKKRNRKTTLQTYGDAIQKLETYTEKK 759
Cdd:TIGR01612 786 SKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSE 865
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
6D05_E 760 DEETKVLLDKFNTEVENFKLDEDEKSFNDAKSIVSNTINEVENENKNIDSIKKVNIAMK 818
Cdd:TIGR01612 866 HEQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIK 924
|
|
| Rh5 |
pfam18515 |
Rh5 coiled-coil domain; This is a helical coiled-coil domain found in reticulocyte-binding ... |
74-327 |
1.37e-13 |
|
Rh5 coiled-coil domain; This is a helical coiled-coil domain found in reticulocyte-binding protein homolog 5 (RH5), a Plasmodium falciparum protein essential for erythrocyte invasion.
Pssm-ID: 436554 [Multi-domain] Cd Length: 255 Bit Score: 71.63 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 74 KTKVNSLLNEASRAIGICNRAKNTVKGLINILENPQKFKTQRESYDVKlRQYEEKKEAFRGCLLNKNRKNLDQIKKINNE 153
Cdd:pfam18515 2 WPKIDKVSKDIIKNKEECEPKKKELINEVDNLENPEYNFYNRPYSNDY-NSYKKSKTNFVNCLLPKFKKLYKKINYIISY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 154 IRDLLEKLKCSQD-CQTNVYFDMIKIYLVDFKKMPYENYDTFIKQYKNSYLSGVDMIRKIEKQIDNPVTINAIKFTQKEM 232
Cdd:pfam18515 81 IKYLYKIYCYNENkCSDKIYKKRLKIVKNEINNFLSKIKKWAINKDKEVIPFINSLITILKSENEPKNLSDKLDFIKKQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 233 GYIIDRFEYHLQKVKHSIDQVTALSDGVKPKQVTKNRLKEYYFNIGNYYSIFKFGKDSLNMLNKALIHKEKIVHNLLGEL 312
Cdd:pfam18515 161 EDIIKKSNKHLEKCKCASDYVKKIQKEKKPNKYYKYELFNEIKKLATHYSIFKYNYEHLINLESVYKTKKEILNNFFNKL 240
|
250
....*....|....*
6D05_E 313 FGHLEERISKLIDSE 327
Cdd:pfam18515 241 GKLLINKVDPDINSI 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
446-764 |
1.10e-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: 58.91 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 446 AENFQKMKDYYKEIEKLKIKILqlieaIKKYQQHVEELINKEKAVAILKEDINKIIEYIKGIIEKLKQLISAnkdfdkiF 525
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALL-----VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE-------V 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 526 QQVEQLINEAlfNKDQFEHNkNDLHTKMKEIMHtfherdLQQFLDNMSKFLKDQEASYQNADSK-EKLDQLLTTVKAKQD 604
Cdd:TIGR02168 277 SELEEEIEEL--QKELYALA-NEISRLEQQKQI------LRERLANLERQLEELEAQLEELESKlDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 605 ELKEmKCDDIPDIIDNLKKESQNVLNLKDEViNKQFENMRTEmsssLDQMTKEYNALKSSIEEYEAEKKGIENHKQNIIK 684
Cdd:TIGR02168 348 ELKE-ELESLEAELEELEAELEELESRLEEL-EEQLETLRSK----VAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 685 RKNTFIVAEHEND-----EDVPEGKNTYNEFISNKDTILQKESAISNQMNTLEEKKRNRKTTLQTYGDAIQKLETYTEKK 759
Cdd:TIGR02168 422 EIEELLKKLEEAElkelqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
....*
6D05_E 760 DEETK 764
Cdd:TIGR02168 502 EGFSE 506
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
445-819 |
2.43e-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: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 445 VAENFQKMKDYYKEIEKLKIKILQLIEAIKKYQQHVEELINKEKAVAILKEDINKiieyikgiieKLKQLISANKDFDKI 524
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKM----------SLQRSMSTQKALEED 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 525 FQQVEQLINEALFNKDQFEHNKNDLHTKmkeimHTFHERDLQQFLDNMSKFLKDQEASYQNADSKEKLdqLLTTVKAKQD 604
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAA-----HSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI--ITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 605 ELKEM-KCDDIPDI-IDNLKKESQNVLNLKDEviNKQFENMRTEMSSSLDQMTKEYNALKSSIEEYEAEKKGIENHKQNI 682
Cdd:pfam05483 392 ELEEMtKFKNNKEVeLEELKKILAEDEKLLDE--KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 683 IKR-------------KNTFIVAEH-----ENDEDVPEGKNTYNEFISNKDTIL---QKESAISNQMNTLEEKKRNRKTT 741
Cdd:pfam05483 470 LKEvedlktelekeklKNIELTAHCdklllENKELTQEASDMTLELKKHQEDIInckKQEERMLKQIENLEEKEMNLRDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 742 LQTYGDAIQKletytekKDEETKVLLDKF--NTEVENFKLDEDEKSFNDAKSIVSNTINEVENENKNIDSIKKVNIAMKR 819
Cdd:pfam05483 550 LESVREEFIQ-------KGDEVKCKLDKSeeNARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
437-769 |
4.87e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 437 SISYSNFSVAENFQKMKDYYKEIEKLKIKI---LQLIEAIKKYQQHVEELINKEKAVAILKEDINKIIEYIKGIIEKLKQ 513
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATNAEITKLRSRVdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 514 LISANKDFDKIFQ----QVEQLINEALFNKDQFEHNKNDLHTKMKEIMHTFHERDLQQ--FLDNMSKFLKDQEasyqnaD 587
Cdd:pfam15921 577 LVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvkLVNAGSERLRAVK------D 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 588 SKEKLDQLLTTVKAKQDELkemkcddipdiidnlkkesqNVLNLKDEVINKQFENMRTEMSSSLDQMTKEYNALKSSIEE 667
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNEL--------------------NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 668 YEAEKKGIE---NHKQNIIKRKNTFIVAEHENDEDVPEGKNTYNEFISN----KDTILQKESAISNQMNTLEEKKRNRKT 740
Cdd:pfam15921 711 TRNTLKSMEgsdGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNankeKHFLKEEKNKLSQELSTVATEKNKMAG 790
|
330 340
....*....|....*....|....*....
6D05_E 741 TLQTygdaIQKLETYTEKKDEETKVLLDK 769
Cdd:pfam15921 791 ELEV----LRSQERRLKEKVANMEVALDK 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
423-778 |
1.48e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 423 NAQKKVDELLSIIDSISYSNFSVAENFQKMKDYYKEIEKLKIKILQLIEAIKK-YQQHVEELINKEKAVAILKEDINKII 501
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 502 EYIKGIIEKLKQLISANKDFDKIFQQVEQLINEALFNKDQFEHNKNDLHTKMKEIMHTFHerDLQQFLDNMSKFLKDQEA 581
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 582 SYQN-ADSKEKLDQLLTTVKAKQDELKEmKCDDIPDIIDNLKKEsQNVLNLKDEVINKQFENMRT---EMSSSLDQMTKE 657
Cdd:TIGR02168 839 RLEDlEEQIEELSEDIESLAAEIEELEE-LIEELESELEALLNE-RASLEEALALLRSELEELSEelrELESKRSELRRE 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 658 YNALKSSIEEYEAEKKGIENHKQNIIKRkntfIVAEHENDEDVPEGKNTYNEFISNK--DTILQKESAISN----QMNTL 731
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQER----LSEEYSLTLEEAEALENKIEDDEEEarRRLKRLENKIKElgpvNLAAI 992
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
6D05_E 732 EE--KKRNRKTTLQTYGD----AIQKLETYTEKKDEETKV-LLDKFNTEVENFK 778
Cdd:TIGR02168 993 EEyeELKERYDFLTAQKEdlteAKETLEEAIEEIDREARErFKDTFDQVNENFQ 1046
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
184-811 |
3.28e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 184 KKMPYENYDTFIKQYKNSYLSGVDMIRKIEKQIDNPV--TINAIKFTQKEMGYIIDRFEYHLQKVKHSIDQVTALSD--G 259
Cdd:TIGR01612 1091 EKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIdhHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDpeE 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 260 VKPKQ---VTKNRLKEY-YFNIGNYYS-IFKFGKD--SLNMLNKALIHKEKIVHNLLGELFGHLEERISKLIDS-EYFIT 331
Cdd:TIGR01612 1171 IEKKIeniVTKIDKKKNiYDEIKKLLNeIAEIEKDktSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAmEAYIE 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 332 ESNNIISQSEETLKLAEDVYDKNTKL-IEDLTLYPHLEINEFKKDYDNNVEDLRESII------YIQSYVSSIKSAYRYN 404
Cdd:TIGR01612 1251 DLDEIKEKSPEIENEMGIEMDIKAEMeTFNISHDDDKDHHIISKKHDENISDIREKSLkiiedfSEESDINDIKKELQKN 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 405 VLEkdsvesKQKNipaNSNAQKKVDELLSIIDSISYSNfsVAENFQKMKDYYKEIEKLKIKILQLIEAIKKYQQHVEELI 484
Cdd:TIGR01612 1331 LLD------AQKH---NSDINLYLNEIANIYNILKLNK--IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDI 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 485 NKEKAVAILKE--DINKIIEYIKGIIEKLKQLISANKDFDKIFQQVEQLINEAL--FNKDQFEHNKNDLHTKMKEIMHTF 560
Cdd:TIGR01612 1400 NLEECKSKIEStlDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLllFKNIEMADNKSQHILKIKKDNATN 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 561 -HERDLQQFLDNMSKFLKDQEASYQNADSKEKLDQLLTTVKAKQDE-LKEMKCDDIPDIIDNLKKESQNVLNLKDEVINK 638
Cdd:TIGR01612 1480 dHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTElLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKK 1559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 639 qfenmrtemsSSLDQMTKEYNALKSSIEEYEAEKKGIENHKQNIIKRKNTFIVAEHEND-EDVPEGKNTYNEFISNKDTI 717
Cdd:TIGR01612 1560 ----------FILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKfLKISDIKKKINDCLKETESI 1629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 718 LQKESAIS-NQMNTLEEKKRNRKTTLQTYGDAIQKletyTEKKDEETKVLLDKFNTEVENFKLDEDEKSFNDAKSIVSNt 796
Cdd:TIGR01612 1630 EKKISSFSiDSQDTELKENGDNLNSLQEFLESLKD----QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEK- 1704
|
650
....*....|....*.
6D05_E 797 INEVENENKN-IDSIK 811
Cdd:TIGR01612 1705 IKEIAIANKEeIESIK 1720
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-737 |
1.09e-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: 45.83 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 367 LEINEFKKDYDNNVEDLRESIIYIQSYVSSIKSAYRynvLEKDSVESKQKNIPA-NSNAQKKVDELLSIIDSISYSNFSV 445
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELS---DASRKIGEIEKEIEQlEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 446 AENFQKMKDYYKEIEKLKIKILQLIEAIKKYQQHVEELINKEkaVAILKEDINKIIEYIKGIIEKLKQLISAnKDFDKif 525
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPE--IQAELSKLEEEVSRIEARLREIEQKLNR-LTLEK-- 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 526 QQVEQLINEALFNKDQFEHNKNDLHTKMKEImhTFHERDLQQFLDNMSKFLKDQEASYQNADSK-EKLDQLLTTVKAKQD 604
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENL--NGKKEELEEELEELEAALRDLESRLGDLKKErDELEAQLRELERKIE 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 605 ELKEMKcddipdiidNLKKESQNVLNLKDEVINKQFenmrtemsssldqmtKEYNALKSSIEEYEAEKKGIENHKQNIIK 684
Cdd:TIGR02169 907 ELEAQI---------EKKRKRLSELKAKLEALEEEL---------------SEIEDPKGEDEEIPEEELSLEDVQAELQR 962
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
6D05_E 685 RKNTFIVAEHEND---EDVPEGKNTYNEFISNKDTILQKESAISNQMNTLEEKKRN 737
Cdd:TIGR02169 963 VEEEIRALEPVNMlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
475-671 |
1.23e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.97 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 475 KYQQHVEELIN--KEKAVAILKEDINKIIEYIKGIIEKLKQL---ISANKD-FDKIFQQVEQLINEALFNKDQFEHNKND 548
Cdd:cd00176 4 QFLRDADELEAwlSEKEELLSSTDYGDDLESVEALLKKHEALeaeLAAHEErVEALNELGEQLIEEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 549 LHTKMKEIMHTFHER--------DLQQFLDNMSKFLKDQEASYQNADSkEKLDQLLTTVKAKQDELKEMKcddipDIIDN 620
Cdd:cd00176 84 LNQRWEELRELAEERrqrleealDLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELE-----EELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
6D05_E 621 LKKESQNVLNLKDEVINKQFENMRTEMSSSLDQMTKEYNALKSSIEEYEAE 671
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
450-687 |
2.98e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 450 QKMKDYYKEIEKLKIKILQLIEAIKKYQQHVEELINKEKAvaiLKEDINKIIEYIKGIIEKLKQLISANKDFDKIFQQVE 529
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---LREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 530 QLINEALFNKDQFEHNKNDLHTKMKEI-----------MHTFHERDLQQFLDNMSKFLKDQEASyqnADSKEKLDQLLTT 598
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIerlewrqqtevLSPEEEKELVEKIKELEKELEKAKKA---LEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 599 VKAKQDELKEmkcddIPDIIDNLKKESQNVLNLKDEVINK---------QFENMRTEMSSSLDQMTKEYNALKSSIEEYE 669
Cdd:COG1340 169 LKELRKEAEE-----IHKKIKELAEEAQELHEEMIELYKEadelrkeadELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250
....*....|....*...
6D05_E 670 AEKKGIENHKQNIIKRKN 687
Cdd:COG1340 244 KELKKLRKKQRALKREKE 261
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
436-680 |
3.75e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 436 DSISYSNFSVAENFQKMKDYYKEIEKLKikiLQLIEAIKKYQQHVEELINKEKAVAILKEDINKIIEYIKGIIEKLKQLI 515
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQ---AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 516 SANkdfdkifQQVEQLIN--EALFNKDqfehnkndlhtkmkeimhtfherDLQQFLDNMSKFlkDQEASYQNadskekld 593
Cdd:COG3883 93 RAL-------YRSGGSVSylDVLLGSE-----------------------SFSDFLDRLSAL--SKIADADA-------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 594 QLLTTVKAKQDELKEMKcddipdiiDNLKKESQNVLNLKDEVinkqfENMRTEMSSSLDQMTKEYNALKSSIEEYEAEKK 673
Cdd:COG3883 133 DLLEELKADKAELEAKK--------AELEAKLAELEALKAEL-----EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
....*..
6D05_E 674 GIENHKQ 680
Cdd:COG3883 200 ELEAELA 206
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
476-682 |
4.22e-04 |
|
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: 43.95 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 476 YQQHVEELinkEKAVAILKEDINKIIEYIKGIIEKL-KQLISANKDfdkifqqveqlINEALFNKDQFEHNKNDLHTKMK 554
Cdd:pfam15921 315 YMRQLSDL---ESTVSQLRSELREAKRMYEDKIEELeKQLVLANSE-----------LTEARTERDQFSQESGNLDDQLQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 555 EIMHTFHERDLQQFLDnmskflKDQEASYQNADSKEKLdqlltTVKAKQDEL--KEMKCDDIPDIIDNLKKESQNVLNLK 632
Cdd:pfam15921 381 KLLADLHKREKELSLE------KEQNKRLWDRDTGNSI-----TIDHLRRELddRNMEVQRLEALLKAMKSECQGQMERQ 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
6D05_E 633 DEVINKQFENMRtEMSSSLDQMTKEYNALKSSIEEYEAEKKGIENHKQNI 682
Cdd:pfam15921 450 MAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
320-812 |
7.83e-04 |
|
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: 43.50 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 320 ISKLIDSEYFITESNNIISQSEETLKLAEDVYDKNTKLIEDLTLYPHLEINEFK-------KDYDNNVEDLRESIIYIQS 392
Cdd:TIGR01612 1354 ILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKiestlddKDIDECIKKIKELKNHILS 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 393 YVSSIKSAYRYNVLEKDSVESKQKNIPANSNAQKKV--DELLSIIDSISYSNFSVAENFQKMKDYYKEIEKLKIKILQLI 470
Cdd:TIGR01612 1434 EESNIDTYFKNADENNENVLLLFKNIEMADNKSQHIlkIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNK 1513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 471 EAIKKYQQHVEELINKEKAVAIlKEDINKIIEYIKGIIEKLKQlisANKDFDKIFQQVEQLINEALFNKDQFEHNKNDLH 550
Cdd:TIGR01612 1514 ELFEQYKKDVTELLNKYSALAI-KNKFAKTKKDSEIIIKEIKD---AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKND 1589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 551 TKMKEIMhtfherDLQQFLDNM-SKFLKDQEASYQNAD---SKEKLDQLLTT--VKAKQDELKEM--KCDDIPDIIDNLK 622
Cdd:TIGR01612 1590 KSNKAAI------DIQLSLENFeNKFLKISDIKKKINDclkETESIEKKISSfsIDSQDTELKENgdNLNSLQEFLESLK 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 623 KESQNVLNLKDEVINKQFENMRTEMssSLDQMTKEY---------NALKSSIEEYEAEKKGIENHKQNIIKRKNTFIVAE 693
Cdd:TIGR01612 1664 DQKKNIEDKKKELDELDSEIEKIEI--DVDQHKKNYeigiiekikEIAIANKEEIESIKELIEPTIENLISSFNTNDLEG 1741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 694 HENDEDV----PEGKNTYNEFISNKDTILQKESAISNQMNTLEEKKRNRKTTLQTYGDAIQkletyTEKkdeetkvlldK 769
Cdd:TIGR01612 1742 IDPNEKLeeynTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRINAQNEFLKIIE-----IEK----------K 1806
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
6D05_E 770 FNTEVENFKLDEDEKSFNDAKSIVSNT----INEVENENKNIDSIKK 812
Cdd:TIGR01612 1807 SKSYLDDIEAKEFDRIINHFKKKLDHVndkfTKEYSKINEGFDDISK 1853
|
|
| CAS_csx29_CRASP |
NF041237 |
type III-E CRISPR-associated TPR-CHAT protein Csx29; Csx29, the protease subunit of the ... |
380-513 |
4.15e-03 |
|
type III-E CRISPR-associated TPR-CHAT protein Csx29; Csx29, the protease subunit of the craspase complex, is a TPR-CHAP family protein of type III-E CRISPR/Cas systems. Craspase is guided by crRNA, but cleaves protein, not nucleotide, and therefore is highly interesting for potential technological applications.
Pssm-ID: 469139 [Multi-domain] Cd Length: 669 Bit Score: 40.81 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 380 VEDLRESIIYIQSYV-SSIKSAYRYNVLEKDSVEskQKNIPANSNAQKKVDELLsiIDSISYSNFSVAENFQKMKDY--Y 456
Cdd:NF041237 54 KEALKKALRLAEKAIdNKEKNLEALRLKAQALLE--LERINKDEDSEKTLKELL--EEAVQNGCNDFIAELEDIEIFlrY 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
6D05_E 457 KEIEKLKIKILQLIEAIKKYQQHVEELINKEKAVAILKEDINKIIEYIKGIIEKLKQ 513
Cdd:NF041237 130 SERDKLLDKIEYLLQIIGSWLSNNDELLLKAKLAAILNKANDDVDKYLNKAIEKAPK 186
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
457-819 |
4.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 457 KEIEKLKIKILQLIEAIKKYQQHVEELINKEKA---VAILKEDINKIIEYIKGI-IEKLKQLIsanKDFDKIFQQVEQLI 532
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELyeeAKAKKEELERLKKRLTGLtPEKLEKEL---EELEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 533 NEALFNKDQFEHNKNDLHTKMKEIMHT----------FHERDLQQFLDNMSKFLKDQEASYQNADSKE-KLDQLLTTV-K 600
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKErKLRKELRELeK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 601 AKQDELKEMKCDDIPDIIDNLKKESQNVLNLKDEVINKQFENMRTEMS------SSLDQMTKEYNALKSSIEEYEAEKKG 674
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkgeiKSLKKELEKLEELKKKLAELEKKLDE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 675 IENHKQNIIKR-KNTFIVAEHENDEDVPEGKNTYNEFISNKDTILQKESaisnqmntLEEKKRNRKTTLQTYGDAIQKLE 753
Cdd:PRK03918 568 LEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKDAEKELER--------EEKELKKLEEELDKAFEELAETE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6D05_E 754 TYTEKKDEETKVLLDKFNTE-------------VENFKLDEDEKSFNDAKSIVSNTINEVENENKNIDS----IKKVNIA 816
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEeyeelreeylelsRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKakkeLEKLEKA 719
|
...
6D05_E 817 MKR 819
Cdd:PRK03918 720 LER 722
|
|
| |
