|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
889-1969 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1483.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 889 TRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDL 968
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 969 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR 1048
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1049 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAK 1128
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1129 KEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQE 1208
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1209 LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAK 1288
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1289 SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE 1368
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1369 TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQK 1448
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1449 LEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALS 1528
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1529 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1608
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1609 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQL 1688
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1689 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAL 1768
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1769 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGS 1848
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1849 VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLE 1928
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 688558683 1929 EAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1969
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1420.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP----------------GELERQLLQANPILESFGNAKTVKNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14920 145 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14920 225 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14920 305 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14920 385 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespg 661
Cdd:cd14920 465 FQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD--------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 662 eVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 741
Cdd:cd14920 524 -VDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 602
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 742 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14920 603 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
102-812 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1302.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkavklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKK---------------KGTLEDQILQANPILEAFGNAKTVRNNNSSRF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYR-FLSNGNIPIPGQQ 340
Cdd:cd01377 146 GKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd01377 226 DAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd01377 306 KVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTH- 579
Cdd:cd01377 385 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKs 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 580 GKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQnfqrasfydvsslhes 659
Cdd:cd01377 463 KNFKKPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE---------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 660 pgevdrivgldqvagmnETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQ 739
Cdd:cd01377 527 -----------------SGGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQ 589
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558683 740 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd01377 590 LRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1231.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS------------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14932 149 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14932 229 KELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14932 309 VGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14932 389 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespg 661
Cdd:cd14932 469 FQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD--------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 662 eVDRIVGLDQVAGMNETAFGaAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 741
Cdd:cd14932 528 -VDRIVGLDKVAGMGESLHG-AFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLR 605
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 742 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14932 606 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1182.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------------------GELERQLLQANPILEAFGNAKTVKNDNSSRF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14919 142 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14919 222 KDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14919 302 VGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14919 382 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespg 661
Cdd:cd14919 462 FQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD--------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 662 eVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 741
Cdd:cd14919 521 -VDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 742 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14919 600 CNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1174.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkavklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----------------TGELEKQLLQANPILEAFGNAKTVKNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14921 145 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14921 225 DEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14921 305 VGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14921 385 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespg 661
Cdd:cd14921 465 FQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD--------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 662 eVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 741
Cdd:cd14921 524 -VDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLR 602
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 742 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14921 603 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-812 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1170.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN------------SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd15896 149 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd15896 229 KDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd15896 309 VGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd15896 389 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespg 661
Cdd:cd15896 469 FFKPKKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD--------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 662 eVDRIVGLDQVAGMNEtaFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 741
Cdd:cd15896 528 -VDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 604
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 742 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd15896 605 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1155.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPkavklqNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAV------NPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14911 154 GKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14911 234 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14911 314 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14911 394 LQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 582 FQKpRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydvsslhespg 661
Cdd:cd14911 471 FMK-TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDA-------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 662 evdRIVGLDQVAgMNETAFGAayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 741
Cdd:cd14911 530 ---EIVGMAQQA-LTDTQFGA--RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLR 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 742 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14911 604 CNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1128.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----------------GELERQLLQANPILEAFGNAKTVKNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQd 341
Cdd:cd14930 145 GKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14930 224 RELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14930 304 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14930 384 LQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhespg 661
Cdd:cd14930 464 FQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD--------------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 662 eVDRIVGLDQVAGMNETAFGAayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 741
Cdd:cd14930 523 -VEGIVGLEQVSSLGDGPPGG--RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLR 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 742 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14930 600 CNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
90-812 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1093.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 90 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 169
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 170 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkavklqngilfYGELERQLLQANPILESFGN 249
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------------------VGRLEEQILQSNPILEAFGN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 250 AKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL 329
Cdd:pfam00063 141 AKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 330 SNGN-IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNV 408
Cdd:pfam00063 221 SQSGcYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 409 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLN 488
Cdd:pfam00063 301 TELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 489 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTF 568
Cdd:pfam00063 381 SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 569 VDKLVQEQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqra 648
Cdd:pfam00063 458 LDKLYSTFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDY------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 649 sfydvsslhespgevdrivGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRA 728
Cdd:pfam00063 530 -------------------ETAESAAANESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRA 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 729 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSK 808
Cdd:pfam00063 591 GVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTK 670
|
....
gi 688558683 809 IFFR 812
Cdd:pfam00063 671 IFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
83-824 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 999.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 83 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 162
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 163 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnippespkavklqngilfyGELERQLLQANP 242
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV----------------------GSVEDQILESNP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 243 ILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEG 322
Cdd:smart00242 139 ILEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 323 FNSYRFLSNGN-IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENT-AAQKL 400
Cdd:smart00242 219 PEDYRYLNQGGcLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 401 CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIA 480
Cdd:smart00242 299 AELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 481 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWF 560
Cdd:smart00242 378 GFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 561 PKATDKTFVDKLVQEQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKD 640
Cdd:smart00242 455 PKGTDQTFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 641 EIQNfqrasfydvsslhespgevdrivgldqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCI 720
Cdd:smart00242 534 GVSN----------------------------------------AGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCI 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 721 IPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPN 800
Cdd:smart00242 574 KPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDED 653
|
730 740
....*....|....*....|....
gi 688558683 801 LYRIGQSKIFFRTGVLAHLEEERD 824
Cdd:smart00242 654 EYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
39-1385 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 903.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 39 VWVPSERHGFEAASIREERGEEVLVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 113
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 114 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 193
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 194 VIQYLAHVASSHkgrkdhniPPESpkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 273
Cdd:COG5022 172 IMQYLASVTSSS--------TVEI-------------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 274 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQETMEAM 352
Cdd:COG5022 231 EICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 353 HIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQT 432
Cdd:COG5022 311 KTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 433 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 512
Cdd:COG5022 390 LEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 513 LEQEEYQREGIEWSFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVDKLVQ--EQGTHGKFQKPRQLKD 590
Cdd:COG5022 469 LEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 591 KadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQnfqrasfydvsslhespgevdrivgld 670
Cdd:COG5022 547 K--FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------------------------- 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 671 qvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 750
Cdd:COG5022 598 --------------IESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIR 663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 751 ICRQGFPNRIVFQEFRQRYEILTPNA----IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRTGVLAHLEEERDLK 826
Cdd:COG5022 664 ISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAK 743
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 827 ITDIIIYFQSVCRGYLARKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVk 906
Cdd:COG5022 744 LDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL- 822
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 907 erQVKVENELVEMERKHQQLLEEKNILAEQlqaetelFAEAEEMRARLVAKKQelEEILHDLESRVEEEEERNQSLQNEK 986
Cdd:COG5022 823 --QKTIKREKKLRETEEVEFSLKAEVLIQK-------FGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDV 891
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 987 KKMQShiqdleeqldeeeAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEdrvgemTSQLaeEEEKAKNL 1066
Cdd:COG5022 892 KSISS-------------LKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLN------NIDL--EEGPSIEY 950
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1067 GKVKNKQEMMMVDleerlKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDElkiqLAKKEEELQAVlargdeevaq 1146
Cdd:COG5022 951 VKLPELNKLHEVE-----SKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKE----LAELSKQYGAL---------- 1011
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1147 kNNALKQLRELQAQLAELQEDLE------SEKAARNKAEKLKRD-------LSEELEALKTELEDTLDTTAAQQELRSKR 1213
Cdd:COG5022 1012 -QESTKQLKELPVEVAELQSASKiissesTELSILKPLQKLKGLlllennqLQARYKALKLRRENSLLDDKQLYQLESTE 1090
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1214 EQEVAELKKAIDDETRNHESQIQEMR-----QRHGTALEEISEQLEQA----KRVKGNLEKNKQTLESDNKELTNEVKSL 1284
Cdd:COG5022 1091 NLLKTINVKDLEVTNRNLVKPANVLQfivaqMIKLNLLQEISKFLSQLvntlEPVFQKLSVLQLELDGLFWEANLEALPS 1170
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1285 QQAKSESEHKRKKLEAQLQEV-MARFSEGEKVKGELADRTHKIQTElDNVSCLLEDAEKKGIKLT------KDVSSLESQ 1357
Cdd:COG5022 1171 PPPFAALSEKRLYQSALYDEKsKLSSSEVNDLKNELIALFSKIFSG-WPRGDKLKKLISEGWVPTeystslKGFNNLNKK 1249
|
1370 1380
....*....|....*....|....*...
gi 688558683 1358 LQDTQELLQEETRQKLNLSSRIRQLEEE 1385
Cdd:COG5022 1250 FDTPASMSNEKLLSLLNSIDNLLSSYKL 1277
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
102-812 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 845.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-----------------ASSIEQQILQSNPILEAFGNAKTVRNDNSSR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL-----SNGNIP 335
Cdd:cd00124 144 FGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 336 IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNT--DQASMPENTAAQKLCHLLGMNVMEFTR 413
Cdd:cd00124 224 IDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFQLNSFEQ 492
Cdd:cd00124 304 ALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 493 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKL 572
Cdd:cd00124 384 LCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 573 VQEQGTHGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkdeiqnfqrasfyd 652
Cdd:cd00124 461 YSAHGSHPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 653 vsslhespgevdrivgldqvagmnetafgaayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLE 732
Cdd:cd00124 519 ---------------------------------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFD 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 733 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd00124 554 PELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 773.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKAvklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTG----------GTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQ 339
Cdd:cd14927 151 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14927 230 DDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14927 310 VKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 578
Cdd:cd14927 389 EKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 579 HGKFQKPR---QLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiQNFQRASFYDvss 655
Cdd:cd14927 466 SPNFQKPRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY----ENYVGSDSTE--- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 656 lhespgevdrivglDQVAGMNETafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHL 735
Cdd:cd14927 539 --------------DPKSGVKEK------RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFL 598
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 736 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14927 599 VLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
103-812 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 753.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASShkgrkdhnIPPESPKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT--------GDLAKKKDSKMK------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQ 340
Cdd:cd14913 148 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASID 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14913 227 DAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14913 307 KVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTH 579
Cdd:cd14913 386 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 580 GKFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrASFydvsslh 657
Cdd:cd14913 463 NNFQKPKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY---------ATF------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 658 espgevdrivgldqvAGMNETAFGAAYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLV 736
Cdd:cd14913 527 ---------------ATADADSGKKKVAKKKGSsFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLV 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 737 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14913 592 LHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 738.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKAvklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKT------DEAAKSK----------GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQ 340
Cdd:cd14909 145 GKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14909 225 DGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14909 305 KVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 579
Cdd:cd14909 384 KLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 580 GKFQKPRQLK---DKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydvssl 656
Cdd:cd14909 461 APFQKPKPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH--------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 657 hesPGEvdrivgldqvAGMNETAFGAAYKtKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLV 736
Cdd:cd14909 526 ---AGQ----------SGGGEQAKGGRGK-KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLV 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 737 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14909 592 MHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 716.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK------------------GSLEDQIIQANPVLEAFGNAKTTRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHL-RSDLLLEGFNSYRFLSNGNIPIPGQQ 340
Cdd:cd14934 143 GKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14934 223 DGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14934 303 KVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 579
Cdd:cd14934 382 KLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 580 GKFQKPRQLKDK---ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdKFVAELWKDEiqnfqrasfydvssl 656
Cdd:cd14934 459 SNFLKPKGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFKE--------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 657 hespgevdrivgldqvagmnETAFGAAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHL 735
Cdd:cd14934 523 --------------------EEAPAGSKKQKRGsSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHL 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 736 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14934 583 IMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
103-812 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 707.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippESpkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET--------------QVEEKVLASNPIMEAFGNAKTTRNDNSSRF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQ 340
Cdd:cd01380 140 GKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd01380 220 DAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd01380 300 VTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYAN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTH 579
Cdd:cd01380 380 EKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 580 GK--FQKPRQLKDKadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLhqstdkfvaelwkdeiqnfqRASfydvsslh 657
Cdd:cd01380 456 PNkhFKKPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVL--------------------KAS-------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 658 espgevdrivgldqvagmnetafgaayKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 737
Cdd:cd01380 506 ---------------------------KNRK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVV 555
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 738 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd01380 556 QQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
102-812 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 695.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkavKLqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKK------------KL-------GALEDQIMQANPVLEAFGNAKTLRNDNSSRF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhLRsDLLLEGFN--SYRFLSNGNIPIPGQ 339
Cdd:cd14929 142 GKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE-LR-DLLLVSANpsDFHFCSCGAVAVESL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14929 220 DDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14929 300 IKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 578
Cdd:cd14929 379 EKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 579 HGKFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIqnfqrasfydvssl 656
Cdd:cd14929 456 SVHFQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYI-------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 657 hespgevdrivgldqVAGmNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLV 736
Cdd:cd14929 522 ---------------STD-SAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLV 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 737 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14929 586 LQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
103-812 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 694.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippESPKAvklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPGK----------GTLEDQIIQANPALEAFGNAKTVRNDNSSRF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQ 339
Cdd:cd14917 147 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELL-DMLLITNNpyDYAFISQGETTVASI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14917 226 DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14917 306 VKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 578
Cdd:cd14917 385 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 579 HGKFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvssl 656
Cdd:cd14917 462 SNNFQKPRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 657 hespgevdrivgldqVAGMNETAFGAAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHL 735
Cdd:cd14917 526 ---------------YAGADAPIEKGKGKAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPL 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 736 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14917 591 VMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
104-812 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 678.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 183
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 184 GAGKTENTKKVIQYLAHVASSHKGRKDhnippespKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFGK 263
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKE--------ESGKMQ------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 264 FIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLE-GFNSYRFLSNGNIPIPGQQDK 342
Cdd:cd14918 149 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 343 DNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKV 422
Cdd:cd14918 229 EELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 423 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 502
Cdd:cd14918 309 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 503 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGK 581
Cdd:cd14918 388 QQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSAN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 582 FQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqraSFYdvsslheS 659
Cdd:cd14918 465 FQKPKVVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF----------STY-------A 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 660 PGEVDrivgldqvagmneTAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQ 739
Cdd:cd14918 528 SAEAD-------------SGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQ 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558683 740 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14918 595 LRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
103-812 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 676.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEITSGKMQ------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14912 150 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14912 230 QEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14912 310 VGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHG 580
Cdd:cd14912 389 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 581 KFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfydvSSLHE 658
Cdd:cd14912 466 NFQKPKVVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF---------------SGAQT 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 659 SPGEvdrivgldqVAGMNETAFGaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 738
Cdd:cd14912 531 AEGA---------SAGGGAKKGG---KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLH 598
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 739 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14912 599 QLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
103-812 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 674.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippespkavklqNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKE--------------NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQ 339
Cdd:cd14916 148 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELL-DMLLVTNNpyDYAFVSQGEVSVASI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14916 227 DDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14916 307 VKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 578
Cdd:cd14916 386 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 579 HGKFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydvssl 656
Cdd:cd14916 463 SNNFQKPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY--------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 657 hespgevdrivgldQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLV 736
Cdd:cd14916 528 --------------ASADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLV 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 737 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14916 594 MHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
103-812 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 671.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEATSGKMQ------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLE-GFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14910 150 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14910 230 QEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14910 310 VGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHG 580
Cdd:cd14910 389 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 581 KFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvsslhe 658
Cdd:cd14910 466 NFQKPKPAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG------------------ 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 659 spgevdrivgldQVAGMNETAFGAAYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 737
Cdd:cd14910 528 ------------AAAAEAEEGGGKKGGKKKGSsFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVL 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 738 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14910 596 HQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-812 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 670.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQ------GTLEDQIIQANPLLEAFGNAKTVRNDNSSRFG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQ 340
Cdd:cd14923 149 KFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASID 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14923 228 DSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14923 308 KVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTH 579
Cdd:cd14923 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 580 GKFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfYDVSSLH 657
Cdd:cd14923 464 NNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSN----------YAGAEAG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 658 ESPGEvdrivgldqvagmnetafGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 737
Cdd:cd14923 534 DSGGS------------------KKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVM 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 738 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14923 596 HQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-812 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 664.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEAASGKMQ------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYRF--LSNGNIPIPGQQ 340
Cdd:cd14915 150 KFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14915 229 DQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14915 309 KVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 579
Cdd:cd14915 388 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 580 GKFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfydvsslh 657
Cdd:cd14915 465 NNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLF------------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 658 eSPGEvdrivgldqvAGMNETAFGAAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLV 736
Cdd:cd14915 526 -SGGQ----------TAEAEGGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELV 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 737 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14915 595 LHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
103-812 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 634.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--HLRSDLLLEGFNSYRFLS-NGNIPIPGQ 339
Cdd:cd14883 137 KFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK-LCHLLGMNVMEFTRAILSP 418
Cdd:cd14883 217 NDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKiVAKLLGVDPDKLKKALTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 419 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYT 498
Cdd:cd14883 297 QINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 499 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 578
Cdd:cd14883 376 NEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 579 HGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdeiqnfqrasfydvsslhe 658
Cdd:cd14883 453 HPYYEKPDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFT------------------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 659 sPGEVDRIVGLDQVAGMNETAFGaaykTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 738
Cdd:cd14883 514 -YPDLLALTGLSISLGGDTTSRG----TSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLA 587
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558683 739 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14883 588 QLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
103-812 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 631.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqngilfygeLERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-------------------------IENEILQTNPILEAFGNAKTLRNDNSSRFG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQD 341
Cdd:cd01383 135 KLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd01383 215 AKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd01383 295 AGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANER 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd01383 375 LQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSC 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 582 FQKPRqlkDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQNFQRASfydvsslhespg 661
Cdd:cd01383 452 FKGER---GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKAL------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 662 evdrivgldqvagMNETAFGAAyktkkGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 741
Cdd:cd01383 516 -------------PLTKASGSD-----SQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLR 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 742 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd01383 578 CCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
103-812 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 625.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkaVKlqngilfygeleRQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VK------------DMLLASNPLLEAFGNAKTLRNDNSSRFG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQD 341
Cdd:cd01378 141 KYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd01378 221 AADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 422 VG---RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYT 498
Cdd:cd01378 300 TGgggRSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 499 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVDKLVQEQG 577
Cdd:cd01378 380 NEKLQQIFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 578 THGKFQKPRQLKD--KADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQnfqrasfydvss 655
Cdd:cd01378 457 NHPHFECPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 656 lhespgevdrivgldqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHL 735
Cdd:cd01378 525 -----------------------------LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEEL 575
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 736 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd01378 576 VLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
102-812 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 603.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAHVAsshkGRKDHNIPPespkavklqngilfygeLERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEGRS-----------------VEQQVLESNPLLEAFGNAKTVRNNNSSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQ 339
Cdd:cd01384 140 FGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAIL 416
Cdd:cd01384 220 DDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALC 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 417 SpRIKVGRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCI 495
Cdd:cd01384 300 K-RVIVTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 496 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQE 575
Cdd:cd01384 378 NLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQT 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 576 QGTHGKFQKPRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfydvss 655
Cdd:cd01384 455 LKDHKRFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF----------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 656 lHESPGEvdrivgldqvagmnetafgaayKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPH 734
Cdd:cd01384 516 -PPLPRE----------------------GTSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENA 572
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 735 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 812
Cdd:cd01384 573 NVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
102-812 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 598.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------------------WIEQQILEANPILEAFGNAKTIRNDNSSRF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQ 340
Cdd:cd01381 136 GKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKK--ERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSP 418
Cdd:cd01381 216 DAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 419 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFQLNSFEQLCIN 496
Cdd:cd01381 296 TIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCIN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 497 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVDKLVQE 575
Cdd:cd01381 376 FANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHST 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 576 QGTHGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIqnfqrasfydvss 655
Cdd:cd01381 452 HGNNKNYLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 656 lheSPGEVDRivgldqvagmnetafgaayktKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHL 735
Cdd:cd01381 518 ---SMGSETR---------------------KKSP--TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDREL 571
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 736 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd01381 572 CVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
102-812 |
6.63e-180 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 561.10 E-value: 6.63e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG------------------------PIEQRILEANPLLEAFGNAKTVRNNNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLegfnsyrflsngnipIPGQQ 340
Cdd:cd01382 137 FGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNT-------DQASMPENTAAQKlchLLGMNVMEF-- 411
Cdd:cd01382 202 DVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrv 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 412 ---TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFQLN 488
Cdd:cd01382 279 sltTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 489 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTF 568
Cdd:cd01382 357 SFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHF 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 569 VDKLVQEQGTHGKFQKPRQ--------LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkd 640
Cdd:cd01382 434 TSAVHQKHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSL--- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 641 eiqnFQRASFYDVSSLHespgevdrivgldqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCI 720
Cdd:cd01382 511 ----FESSTNNNKDSKQ---------------------------KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCI 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 721 IPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPN 800
Cdd:cd01382 560 KPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNEN 637
|
730
....*....|..
gi 688558683 801 LYRIGQSKIFFR 812
Cdd:cd01382 638 DFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
102-812 |
7.01e-179 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 558.24 E-value: 7.01e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqngilfygeLERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------------VEQRVLLANPILEAFGNAKTLRNNNSSRF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGfnSYRFLSNGN-IPIPGQQ 340
Cdd:cd14872 136 GKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA--AYGYLSLSGcIEVEGVD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCH---LLGMNVMEFTRAILS 417
Cdd:cd14872 214 DVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 418 PRIKV-GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCIN 496
Cdd:cd14872 294 RLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCIN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 497 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQ 576
Cdd:cd14872 374 FTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 577 GTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdeiqnfqrasfydvssl 656
Cdd:cd14872 451 AAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP----------------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 657 hesPGEVDRivgldqvagmnetafgaayKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLV 736
Cdd:cd14872 514 ---PSEGDQ-------------------KTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMS 568
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 737 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtPNAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14872 569 LEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
102-812 |
7.75e-173 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 542.44 E-value: 7.75e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 176
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 177 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhniPPESPKAvkLQNGILFYGELERQLLQANPILESFGNAKTVKND 256
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGA----SGEGEAA--SEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 257 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPI 336
Cdd:cd14890 155 NSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 337 PGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKErntDQASMPEN-TAAQKLCH---LLGMNVMEFT 412
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE---NDTTVLEDaTTLQSLKLaaeLLGVNEDALE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 413 RAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQ 492
Cdd:cd14890 312 KALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 493 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFV 569
Cdd:cd14890 391 LCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 570 DKLVQEQGT-------------HGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvae 636
Cdd:cd14890 469 SQLHASFGRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 637 lwkdeiqnfqrasfydvSSLHESpgevdrivgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNF 716
Cdd:cd14890 542 -----------------RSIREV---------------------------------SVGAQFRTQLQELMAKISLTNPRY 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 717 VRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALE 796
Cdd:cd14890 572 VRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLG 646
|
730
....*....|....*.
gi 688558683 797 LDPNLYRIGQSKIFFR 812
Cdd:cd14890 647 LGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
102-812 |
9.02e-170 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 533.95 E-value: 9.02e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnippESPKAVKLQngilfygelerQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-------------QRRNNLVTE-----------QILEATPLLEAFGNAKTVRNDNSSRF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG-NIPIPGQQ 340
Cdd:cd01387 137 GKYLEVFFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ---ASMPENTAAQKLCHLLGMNVMEFTRAILS 417
Cdd:cd01387 216 DADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 418 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINY 497
Cdd:cd01387 296 KVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 498 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQG 577
Cdd:cd01387 375 ANENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 578 THGKFQKPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQNFQRASfydvsslh 657
Cdd:cd01387 452 LNELYSKPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAP-------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 658 espgevdrivgldqVAGMNetafgAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 737
Cdd:cd01387 522 --------------PRLGK-----GRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVM 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 738 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 812
Cdd:cd01387 583 AQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-812 |
5.82e-166 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 525.02 E-value: 5.82e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLahVASSHKGrkdhnippespkavklqngilfYGE-LERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG----------------------YGSgVEQTILGAGPVLEAFGNAKTAHNNNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQ 339
Cdd:cd01385 137 FGKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKER-NTDQASMPENTAAQKL-CHLLGMNVMEFTRAILS 417
Cdd:cd01385 217 DEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 418 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFQLNSFEQL 493
Cdd:cd01385 297 KKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 494 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLV 573
Cdd:cd01385 376 CINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 574 QEQGTHGKFQKPrQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAEL----------Wkdeiq 643
Cdd:cd01385 453 QQHKDNKYYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrW----- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 644 NFQRASFYDVSSLHESPGEVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPN 723
Cdd:cd01385 526 AVLRAFFRAMAAFREAGRRRAQRTAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSN 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 724 HEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYR 803
Cdd:cd01385 606 AEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQ 681
|
....*....
gi 688558683 804 IGQSKIFFR 812
Cdd:cd01385 682 IGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
102-812 |
1.16e-164 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 520.10 E-value: 1.16e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIppespkavklqngilfygeleRQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI---------------------KKIIEVNPLLESFGNAKTVRNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsdLLLEGFNSYRFL-SNGNIPIPGQ 339
Cdd:cd14903 137 FGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGM 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASM--PENTAAQKLCHLLGMNVMEFTRAILS 417
Cdd:cd14903 215 SDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 418 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINY 497
Cdd:cd14903 295 RTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 498 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVqeqG 577
Cdd:cd14903 374 ANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---S 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 578 THGKFQK----PRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdeiqnfQRASFYDV 653
Cdd:cd14903 447 IHKDEQDviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK------EKVESPAA 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 654 SSlhespgevdrivgldqvagMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEP 733
Cdd:cd14903 519 AS-------------------TSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDH 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 734 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 812
Cdd:cd14903 580 LMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
103-812 |
2.82e-158 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 501.81 E-value: 2.82e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVAsshkgrkdhnippespKAVklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG----------------KAN--------NRTLEEKILQVNPLMEAFGNARTVINDNSSRFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGagehLRSDLLLEGFNS-------YRFLSNGNIP 335
Cdd:cd01379 138 KYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKLpenkpprYLQNDGLTVQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 336 IPGQQD--KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENTAA-QKLCHLLGMNVM 409
Cdd:cd01379 214 DIVNNSgnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEAD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 410 EFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFQL 487
Cdd:cd01379 294 ELQEALTSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 488 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDK 566
Cdd:cd01379 374 NSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 567 TFVDKLvqEQGTHGKFQKpRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdeiqnfq 646
Cdd:cd01379 450 TLVEKF--HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ---------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 647 rasfydvsslhespgevdrivgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEK 726
Cdd:cd01379 517 ----------------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSR 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 727 RAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQ 806
Cdd:cd01379 551 QAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGK 627
|
....*.
gi 688558683 807 SKIFFR 812
Cdd:cd01379 628 TKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
102-810 |
5.36e-158 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 501.63 E-value: 5.36e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 173
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 174 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKGRKDHNIPPESpkavklqngilfygeLERQLLQANPILESFGNAK 251
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNATEREN---------------VRDRVLESNPILEAFGNAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 252 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL-- 329
Cdd:cd14901 145 TNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLns 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 330 SNGNIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-KKERNTDQASMPENTAAQKLCHLLGMNV 408
Cdd:cd14901 225 SQCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDM 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 409 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFQL 487
Cdd:cd14901 305 DVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFAT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 488 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKA 563
Cdd:cd14901 385 NSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 564 TDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdeiq 643
Cdd:cd14901 458 NDEKLANKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 644 nfqrasfydvsslhespgevdrivgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPN 723
Cdd:cd14901 531 -------------------------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPN 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 724 HEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LEL 797
Cdd:cd14901 562 DVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEH 641
|
730
....*....|...
gi 688558683 798 DPNLYrIGQSKIF 810
Cdd:cd14901 642 LPPFQ-VGKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
102-812 |
6.62e-158 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 501.25 E-value: 6.62e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAHVAsshkgrkdhNIPPESPKAVKLQNgilfygeLERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVIS---------QQSLELSLKEKTSC-------VEQAILESSPIMEAFGNAKTVYNNNSSR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQ 339
Cdd:cd14873 145 FGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKkerNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14873 225 SDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYT 498
Cdd:cd14873 302 MFLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 499 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGT 578
Cdd:cd14873 379 NEKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHAN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 579 HGKFQKPRQLKDkaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdeiqnfqrasFYDVSSLHe 658
Cdd:cd14873 455 NHFYVKPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDL------------FEHVSSRN- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 659 spgevdrivgldqvagmNETAFGAAYKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 738
Cdd:cd14873 520 -----------------NQDTLKCGSKHRRP---TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLN 579
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558683 739 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14873 580 QLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
102-774 |
3.44e-157 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 499.99 E-value: 3.44e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------------------LVEAQVLESNPLLEAFGNARTLRNDNSSR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVT---------GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN 331
Cdd:cd14888 139 FGKFIELQFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 332 GNIP------------------------IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD 387
Cdd:cd14888 219 DAKPisidmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 388 QASMPENTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD 464
Cdd:cd14888 299 EGAVVSASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 465 RTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErp 544
Cdd:cd14888 379 YSKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ-- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 545 ANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVAT 624
Cdd:cd14888 456 EKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 625 LLHQSTDKFVAELWKDEIqnfqrasfydvsslhespgevDRIVGLdqvagmnetafgaayKTKKGMFRTVGQLYKESLTK 704
Cdd:cd14888 534 VIKNSKNPFISNLFSAYL---------------------RRGTDG---------------NTKKKKFVTVSSEFRNQLDV 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 705 LMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 774
Cdd:cd14888 578 LMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
102-812 |
4.89e-156 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 496.20 E-value: 4.89e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 174
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 175 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKAVKLQNGIlfygelERQLLQANPILESFGNAKTVK 254
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKGAANAHESI------EECVLLSNLILEAFGNAKTIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 255 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN- 333
Cdd:cd14892 149 NDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNc 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 334 IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQ----ASMPENTAAQKLCHLLGMNVM 409
Cdd:cd14892 229 VEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 410 EFTRAILSPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDI 479
Cdd:cd14892 307 ELMFKLVTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 480 AGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECW 559
Cdd:cd14892 387 FGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQML 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 560 FP-KATDKTFVDKLVQEQ-GTHGKFQKPRQLKDkaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvael 637
Cdd:cd14892 464 LKrKTTDKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 638 wkdeiqnfqrasfydvsslhespgevdrivgldqvagmnetafgaayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFV 717
Cdd:cd14892 536 -----------------------------------------------------FRT-------QLAELMEVLWSTTPSYI 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 718 RCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM----- 791
Cdd:cd14892 556 KCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkcee 635
|
730 740
....*....|....*....|.
gi 688558683 792 IRALELDPNLYRIGQSKIFFR 812
Cdd:cd14892 636 IVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-812 |
9.95e-154 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 489.20 E-value: 9.95e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAHVASShkgrkDHnippespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS-----DD-------------------SDLLDKIVQINPLLEAFGNASTVMNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQ 340
Cdd:cd14897 137 FGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 D-------KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTR 413
Cdd:cd14897 217 DseeleyyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFQLNS 489
Cdd:cd14897 297 ALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 490 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFV 569
Cdd:cd14897 377 FDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 570 DKLVQEQGTHGKFQKPrqLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeIQNFQRas 649
Cdd:cd14897 454 QKLNKYCGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---TSYFKR-- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 650 fydvsslhespgevdrivgldqvagmnetafgaayktkkgmfrtvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAG 729
Cdd:cd14897 527 ---------------------------------------------------SLSDLMTKLNSADPLFVRCIKPNNFLRPN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 730 KLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKI 809
Cdd:cd14897 556 KFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKV 632
|
...
gi 688558683 810 FFR 812
Cdd:cd14897 633 FLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
103-772 |
6.53e-141 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 453.22 E-value: 6.53e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 168
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 169 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASshkgrkdhnipPESPKAVKLQNGILfygELERQLLQANPILES 246
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGD-----------NNLAASVSMGKSTS---GIAAKVLQTNILLES 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 247 FGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhlrsdlllegfnsy 326
Cdd:cd14900 148 FGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 327 rflsngnipipGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPENTAAQKL----- 400
Cdd:cd14900 214 -----------AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrda 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 401 -CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIG 475
Cdd:cd14900 283 aATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 476 ILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLD 555
Cdd:cd14900 363 ILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLID 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 556 EECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDplndnvatLLHQSTdkfva 635
Cdd:cd14900 440 EECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 636 elwkdeiqnfqrasfydvsslhespgeVDrivgldqvagmnetafgaayktkkgMFRTVGQlYKESLTKLMATLRNTNPN 715
Cdd:cd14900 507 ---------------------------VD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPH 533
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 716 FVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 772
Cdd:cd14900 534 YVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-775 |
4.53e-140 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 452.56 E-value: 4.53e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 172
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 173 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKAV-KLQNGIlfygelERQLLQANPILESFGNAK 251
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATsKSTKSI------EQKILSCNPILEAFGNAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 252 TVKNDNSSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLE----GFNSY 326
Cdd:cd14907 155 TVRNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 327 RFLSNGNIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK-KERNTDQASMPENTAA-QKLCHLL 404
Cdd:cd14907 235 YLKKSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 405 GMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGIL 477
Cdd:cd14907 315 GIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 478 DIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WSFIDFgLDLQPCIDLIERPanPPGVLALLD 555
Cdd:cd14907 395 DIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLD 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 556 EECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVA 635
Cdd:cd14907 472 DSCKLATGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIIS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 636 ELWKDEIQNFQRASFYDVSSlhespgevdrivgldqvagmnetafgaaYKTKKgmfrTVGQLYKESLTKLMATLRNTNPN 715
Cdd:cd14907 551 SIFSGEDGSQQQNQSKQKKS----------------------------QKKDK----FLGSKFRNQMKQLMNELMQCDVH 598
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 716 FVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 775
Cdd:cd14907 599 FIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
104-812 |
3.41e-139 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 449.74 E-value: 3.41e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 179
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 180 TGESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSS 259
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS-------------------------QLEQQILQVNPLLEAFGNAQTVMNDNSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 260 RFGKFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN--GNIPIP 337
Cdd:cd14889 138 RFGKYIQLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNgaGCKREV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 338 gQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQASMPENTAAQKL---CHLLGMNVMEFTRA 414
Cdd:cd14889 217 -QYWKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 415 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFQLNSFEQ 492
Cdd:cd14889 294 LTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 493 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPKATDKTFVDKL 572
Cdd:cd14889 374 ACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 573 VQEQGTHGKFQKPRQLKDKadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfyd 652
Cdd:cd14889 451 NIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF-------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 653 VSSLHESPGEVDRIVGLDQvagmNETAFGAAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLE 732
Cdd:cd14889 515 TATRSRTGTLMPRAKLPQA----GSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLD 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 733 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIF 810
Cdd:cd14889 585 SKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLF 657
|
..
gi 688558683 811 FR 812
Cdd:cd14889 658 FK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
102-812 |
4.33e-136 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 440.63 E-value: 4.33e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 174
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 175 QSILCTGESGAGKTENTKKVIQYLAHvaSSHKGRKDHNIPPESPKAVKLQNGIlfygELERQLLQANPILESFGNAKTVK 254
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTT--RAVGGKKASGQDIEQSSKKRKLSVT----SLDERLMDTNPILESFGNAKTLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 255 NDNSSRFGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN 333
Cdd:cd14891 150 NHNSSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 334 -IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK----LCHLLGMNV 408
Cdd:cd14891 230 cVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEalatAAELLGVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 409 MEFTRAILSPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFQL 487
Cdd:cd14891 310 EALEKVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFET 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 488 -NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE-----WSfidfglDLQPCIDLIErpANPPGVLALLDEECWFP 561
Cdd:cd14891 388 kNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLIA--SKPNGILPLLDNEARNP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 562 KATDKTFVDKLVQEQGTHGKFQKPRQlKDKAD-FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQStdkfvaelwkd 640
Cdd:cd14891 460 NPSDAKLNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 641 eiqnfqrASFydvsslhespgevdrivgLDQVAGMNEtafgaayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCI 720
Cdd:cd14891 528 -------AKF------------------SDQMQELVD------------------------------TLEATRCNFIRCI 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 721 IPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDP 799
Cdd:cd14891 553 KPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPS 632
|
730
....*....|...
gi 688558683 800 NLYRIGQSKIFFR 812
Cdd:cd14891 633 DAYRLGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
102-812 |
3.34e-132 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 429.59 E-value: 3.34e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIppespkavklqngilfygeleRQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL---------------------RQPEDVLPILESFGHAKTILNANASRF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI-PIPGQQ 340
Cdd:cd14896 137 GQVLRLHLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ--ASMPENTAAQKLCHLLGMNVMEFTRAILSP 418
Cdd:cd14896 216 DAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 419 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINY 497
Cdd:cd14896 296 VTETPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 498 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQG 577
Cdd:cd14896 376 ASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 578 THGKFQKPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdeiqnFQRASfydvsslh 657
Cdd:cd14896 453 DHPSYAKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSL-------FQEAE-------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 658 espgevdrivgldqvagmnetafgAAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 737
Cdd:cd14896 516 ------------------------PQYGLGQGK-PTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVT 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 738 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd14896 571 EQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
102-812 |
8.59e-131 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 425.90 E-value: 8.59e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPpespkavklqngilfygelerQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA---------------------KVIDVNPLLESFGNAKTTRNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL--SNGNIPIPG 338
Cdd:cd14904 137 FGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 339 QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASmpenTAAQKLCHLLGMNVMEFTR--AIL 416
Cdd:cd14904 217 LDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRI----SNGSQLSQVAKMLGLPTTRieEAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 417 SPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCI 495
Cdd:cd14904 293 CNRSVVTRnESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 496 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKL--- 572
Cdd:cd14904 373 NYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtn 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 573 VQEQGTHGKFQKPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdeiqnfqrasfyd 652
Cdd:cd14904 449 HQTKKDNESIDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF-------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 653 vsslhespgevdrivglDQVAGMNETAFGAAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLE 732
Cdd:cd14904 513 -----------------GSSEAPSETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFD 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 733 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFF 811
Cdd:cd14904 575 KRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYF 652
|
.
gi 688558683 812 R 812
Cdd:cd14904 653 K 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
102-812 |
1.01e-129 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 423.94 E-value: 1.01e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 171
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 172 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkaVKLQNGILFYGELERQLLQANPILESFGNAK 251
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEG-------------APNEGEELGKLSIMDRVLQSNPILEAFGNAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 252 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--------HLRSDLLLEGF 323
Cdd:cd14908 148 TLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 324 NSYRFLSNGNIPIPGQ-QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPE---NTAAQK 399
Cdd:cd14908 228 NEFHYTGQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLAR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 400 LCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGIL 477
Cdd:cd14908 308 VAKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 478 DIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEE 557
Cdd:cd14908 387 DIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 558 CWFP-KATDKTFVDKLV--------QEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLM-KNmdplndnvatllh 627
Cdd:cd14908 464 CRLGiRGSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKN------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 628 qstdkfvaelwKDEIQNfqrasfydvsslhespgevdrivgldqvagmnetafgaaykTKKGMFRTvGQLYKESLTKLMA 707
Cdd:cd14908 531 -----------KDEIPL-----------------------------------------TADSLFES-GQQFKAQLHSLIE 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 708 TLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-------- 779
Cdd:cd14908 558 MIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsme 636
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 688558683 780 ---------GFMDGKQACERMIRALELDPNL----YRIGQSKIFFR 812
Cdd:cd14908 637 rldpqklcvKKMCKDLVKGVLSPAMVSMKNIpedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
102-774 |
7.85e-129 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 422.76 E-value: 7.85e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 171
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 172 REDQSILCTGESGAGKTENTKKVIQYLAHVasshkGRKDHNIPPESPKAVKLQngilfygeleRQLLQANPILESFGNAK 251
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSV-----GRDQSSTEQEGSDAVEIG----------KRILQTNPILESFGNAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 252 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN 331
Cdd:cd14902 146 TIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 332 ---GNIPIPGQQDKDN--FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKE-RNTDQASMPENTAAQ--KLCHL 403
Cdd:cd14902 226 ygpSFARKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 404 LGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIG 475
Cdd:cd14902 306 MGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 476 ILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLD 555
Cdd:cd14902 386 ILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 556 EECWFPKATDKTFVDKLVQEQGTHGKFqkprqlkdkadfCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVA 635
Cdd:cd14902 463 QECLMPKGSNQALSTKFYRYHGGLGQF------------VVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 636 ELWKDEIQNfqrasfydvsslheSPGEVDrivgldqvagmnetafGAAYKTKKGMFRT--VGQLYKESLTKLMATLRNTN 713
Cdd:cd14902 531 AIGADENRD--------------SPGADN----------------GAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTE 580
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 714 PNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 774
Cdd:cd14902 581 AHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
100-865 |
2.10e-123 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 410.58 E-value: 2.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 100 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 179 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkavklQNGILfygelerqllQANPILESFGNAKTVKNDNS 258
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----------QNAIM----------AANPVLEAFGNAKTIRNNNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 259 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPG 338
Cdd:PTZ00014 245 SRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 339 QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASM--PENTAA-QKLCHLLGMNVMEFTR 413
Cdd:PTZ00014 325 IDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFQLNSFEQL 493
Cdd:PTZ00014 405 ELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 494 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLV 573
Cdd:PTZ00014 484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCN 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 574 QEQGTHGKFQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqrasfydv 653
Cdd:PTZ00014 561 TNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGV------------ 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 654 sslhespgEVDRivgldqvagmnetafgaaYKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEP 733
Cdd:PTZ00014 628 --------EVEK------------------GKLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNS 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 734 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFF-R 812
Cdd:PTZ00014 680 SKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkK 759
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 813 TGV--LAHLEEERDLKITDIIIYFQSVCRGYLARKAFAKKqqqlsaLKVLQRNCA 865
Cdd:PTZ00014 760 DAAkeLTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-812 |
1.25e-122 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 404.00 E-value: 1.25e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnIPPEspkavKLQngilfygelerqllQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVE-----KLN--------------AALTVLEAFGNVRTALNGNATRF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSyrflSNGNIPIPGQQD 341
Cdd:cd01386 138 SQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KD------NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAI 415
Cdd:cd01386 214 EDkqkaaaAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 416 ------------LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGfe 483
Cdd:cd01386 294 fkhhlsggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG-- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 484 iFQLN---------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERP---ANPP--- 548
Cdd:cd01386 371 -FQNPahsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdl 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 549 ------GVLALLDEECWFPKATDKTFVDKLVQEQG--THGKFQKPRQLKDKA-DFCIIHYAGR--VDYKADEWLMK-NMD 616
Cdd:cd01386 450 rdedrrGLLWLLDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKEN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 617 PLNDNVATLLHQSTDKFvaelwkdeiqnfqrasfydvsslhespgevdrivgldqvagmnetafgAAYKtKKGMFRTVgq 696
Cdd:cd01386 530 PSAQNATQLLQESQKET------------------------------------------------AAVK-RKSPCLQI-- 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 697 lyKESLTKLMATLRNTNPNFVRCIIPNHEkrAGKLEPH--------------LVLDQLRCNGVLEGIRICRQGFPNRIVF 762
Cdd:cd01386 559 --KFQVDALIDTLRRTGLHFVHCLLPQHN--AGKDERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPL 634
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 763 QEFRQRYEILTPNAIPKGF-----MDGKQACERMIRALELDPNLYRIGQSKIFFR 812
Cdd:cd01386 635 GEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
103-773 |
5.05e-122 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 402.79 E-value: 5.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 170
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 171 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPPEspkavklqngilfygelerQLLQANPIL 244
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS-------------------ELLSANPIL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 245 ESFGNAKTVKNDNSSRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLL 319
Cdd:cd14895 136 ESFGNARTLRNDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 320 LEGFNS--YRFLSNGNIPI--PGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-------- 387
Cdd:cd14895 216 LELLSAqeFQYISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaa 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 388 -------QASMPENTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVH 457
Cdd:cd14895 296 sapcrlaSASPSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 458 RINKALDRTK----------RQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSF 527
Cdd:cd14895 376 KVNSASPQRQfalnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 528 IDFGLDlQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlKDKAD--FCIIHYAGRVDY 605
Cdd:cd14895 456 VDYEDN-SVCLEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRY 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 606 KADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdeiqnfqrasFYDVSSLHE----SPGEVDRIVGLDQVAgmnetafg 681
Cdd:cd14895 531 QAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFE----------FFKASESAElslgQPKLRRRSSVLSSVG-------- 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 682 aayktkkgmfrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 761
Cdd:cd14895 593 ------------IGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMK 660
|
730
....*....|..
gi 688558683 762 FQEFRQRYEILT 773
Cdd:cd14895 661 HADFVKQYRLLV 672
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
102-810 |
5.39e-121 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 397.82 E-value: 5.39e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkavklQNGILfygelerqllQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----------QTAIM----------AANPVLEAFGNAKTIRNNNSSR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQ 340
Cdd:cd14876 138 FGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGID 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAI 415
Cdd:cd14876 218 DVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKREL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 416 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFQLNSFEQLC 494
Cdd:cd14876 298 TVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 495 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQ 574
Cdd:cd14876 376 INITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 575 EQGTHGKFqKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIqnfqrasfydvs 654
Cdd:cd14876 453 KLKSNGKF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVV------------ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 655 slhespgevdrivgldQVAGmnetafgaayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPH 734
Cdd:cd14876 520 ----------------VEKG----------KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSS 571
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 735 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 810
Cdd:cd14876 572 KVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-774 |
8.25e-115 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 380.35 E-value: 8.25e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 177
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 178 LCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnipPESPKAVKLQNGIlfygelERQLLQANPILESFGNAKTVKNDN 257
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAS----------PTSWESHKIAERI------EQRILNSNPVMEAFGNACTLRNNN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 258 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIp 337
Cdd:cd14880 145 SSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 338 gqqDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTA---AQKLCHLLGMNVMEFTRA 414
Cdd:cd14880 224 ---EEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 415 ILSPRIKVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQ 492
Cdd:cd14880 301 LQIRTIRAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 493 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKL 572
Cdd:cd14880 381 LCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 573 VQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQNfqrasfyd 652
Cdd:cd14880 458 IESALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEE-------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 653 vsSLHESPGEVDRIVGLdqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLE 732
Cdd:cd14880 530 --KTQEEPSGQSRAPVL-----------------------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFL 584
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 688558683 733 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 774
Cdd:cd14880 585 QEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-775 |
5.18e-114 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 380.09 E-value: 5.18e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 179
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 180 TGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklQNGilfYGELERQLLQANPILESFGNAKTVKNDNSS 259
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNN-----------NNN---NNSIEKDILTSNPILEAFGNSRTTKNHNSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 260 RFGKFIRINFDVTGYIV-GANIETYLLEKSR-AIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEG-FNSYRFL------- 329
Cdd:cd14906 147 RFGKFLKIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvi 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 330 -------SNGNIPIPGQQDKD-NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQAS--MPENTAA-Q 398
Cdd:cd14906 227 ssfksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 399 KLCHLLGMNVMEFTRAILSPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------T 466
Cdd:cd14906 307 SVSKLLGYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 467 KRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAN 546
Cdd:cd14906 387 NKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 547 ppGVLALLDEECWFPKATDKTFVDKLVQE-QGTHGKFQkpRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATL 625
Cdd:cd14906 466 --GILSLLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 626 LHQSTdkfvaelwkdeiqNFQRASFYDVSSLHESpgevdrivgldqvagmNETafgaaykTKKGMFRTVGQLYKESLTKL 705
Cdd:cd14906 541 LLASS-------------NFLKKSLFQQQITSTT----------------NTT-------KKQTQSNTVSGQFLEQLNQL 584
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 706 MATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 775
Cdd:cd14906 585 IQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
102-812 |
2.81e-108 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 361.51 E-value: 2.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 176 SILCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnippespKAVKLQNGILfygelerqllQANPILESFGNAKTVKN 255
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST--------------SSTDVQSLIL----------GSNPLLESFGNAKTLRN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 256 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI- 334
Cdd:cd14886 137 NNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCy 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 335 PIPGQQDKDNFQETMEAMHIMsFNHEEILSMLKVVSAVLQFGNIVFKKERN--TDQASMPENTAA-QKLCHLLGMNVMEF 411
Cdd:cd14886 217 DAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 412 TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFQLN 488
Cdd:cd14886 296 AQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 489 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTF 568
Cdd:cd14886 372 TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKF 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 569 VdklvqeQGTHGKFQKPRQLKDKA---DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVaelwkdeiqnf 645
Cdd:cd14886 449 T------SSCKSKIKNNSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV----------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 646 qRASFYDVSslhespgevdrivgldqvagmNETAfgaaykTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHE 725
Cdd:cd14886 512 -NKAFSDIP---------------------NEDG------NMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQD 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 726 KRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYR 803
Cdd:cd14886 562 KVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYR 641
|
....*....
gi 688558683 804 IGQSKIFFR 812
Cdd:cd14886 642 IGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-812 |
3.26e-108 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 361.43 E-value: 3.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 178
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 179 CTGESGAGKTENTKKVIQYLAHVASSHKGRkdhniPPESPKAVKLQNgilfygelerQLLQANPILESFGNAKTVKNDNS 258
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSN-----TSQRSIADKIDE----------NLKWSNPVMESFGNARTVRNDNS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 259 SRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDL-LLEGFNSYRFLSNGNI-- 334
Cdd:cd14875 146 SRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfv 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 335 --PIPGQ--QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVME 410
Cdd:cd14875 226 rrGVDGKtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 411 FTRAILsprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFQLNS 489
Cdd:cd14875 305 LRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 490 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFV 569
Cdd:cd14875 382 FEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFT 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 570 DKLVQEQGTHGK-FQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfqra 648
Cdd:cd14875 459 TNLWDQWANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 649 sfydvsslhesPGEVDRIvgldqvagmnetafgaayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRA 728
Cdd:cd14875 531 -----------KGLARRK-------------------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASP 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 729 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNl 801
Cdd:cd14875 575 SFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN- 653
|
730
....*....|.
gi 688558683 802 YRIGQSKIFFR 812
Cdd:cd14875 654 YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
102-769 |
7.58e-104 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 350.55 E-value: 7.58e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 170
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 171 DREDQSILCTGESGAGKTENTKKVIQYLA---HVASSHKGRKDHNIPPESPKAVKLqngilfygelERQLLQANPILESF 247
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcGTGNNNLTNSESISPPASPSRTTI----------EEQVLQSNPILEAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 248 GNAKTVKNDNSSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-----AGEHLRSDLLLE 321
Cdd:cd14899 151 GNARTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 322 GFNSYRFLSNG--NIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-----KKERNT--DQASMP 392
Cdd:cd14899 231 GPQSFRLLNQSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 393 ENTAA-----QKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT- 466
Cdd:cd14899 311 SSTTGafdhfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQa 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 467 -------------KRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlD 533
Cdd:cd14899 391 sapwgadesdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-N 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 534 LQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKL---VQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEW 610
Cdd:cd14899 470 NRACLELFEH--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 611 LMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvSSLHESPGEVDRIVGLDQVAGMNETAFGAAyktkkgm 690
Cdd:cd14899 548 LAKNKDSFCESAAQLLAGSSNPLIQALAAG-------------SNDEDANGDSELDGFGGRTRRRAKSAIAAV------- 607
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 691 frTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 769
Cdd:cd14899 608 --SVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
102-812 |
1.91e-92 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 317.75 E-value: 1.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 173
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 174 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqngilfygeLERQLLQANPILESFGNAKTV 253
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG--------------------LEARLLQSGPVLEAFGNAHTV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 254 KNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFnsyrflsng 332
Cdd:cd14887 141 LNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGD--------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 333 nipiPGQQDKDNFQETMEAMHIMSFNHEEIlsmLKVVSAVLQFGNIVFKKERNTDQASMPENTA--------AQKLCHLL 404
Cdd:cd14887 212 ----PESTDLRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 405 -------GMNVMEFTRAILS--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVH 457
Cdd:cd14887 285 evkclssGLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 458 RINKALDRTKR-------------QGASFIGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQRE 521
Cdd:cd14887 365 RINAGLQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 522 G--IEWSFIDFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVDKL 572
Cdd:cd14887 445 GvfQNQDCSAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKL 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 573 VQ--EQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLlhqstdkfvaelwkdeiqnFQRASF 650
Cdd:cd14887 525 NKniINSAKYKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERL-------------------FLACST 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 651 YdvsslhespgevDRIVGLDQVAGMNetafgaAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGK 730
Cdd:cd14887 586 Y------------TRLVGSKKNSGVR------AISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGI 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 731 LEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIF 810
Cdd:cd14887 645 FEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIF 723
|
..
gi 688558683 811 FR 812
Cdd:cd14887 724 FR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
103-776 |
1.04e-91 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 310.68 E-value: 1.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 182
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT-------------------------SIEKLITAANLILEAFGNAKTQLNDNSSRFG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDvtGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLlegfNSYRFLSNGNIPIPGQQDK 342
Cdd:cd14898 133 KRIKLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 343 DNFQETMEAMHIMSFNHEEILSMlkvvsAVLQFGNIVFKKERNTDQASmpeNTAAQKLCHLLGMNVMEFTRAILSPRIKV 422
Cdd:cd14898 207 KMTCSAMKSLGIANFKSIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 423 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 502
Cdd:cd14898 279 KGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 503 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLvqeqgthGKF 582
Cdd:cd14898 356 QNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKY 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 583 QKPRqLKDKADFCII--HYAGRVDYKADEWLMKNmdplndnvatllhqsTDKFVAELWKDeiqnfqrasfydvsslhesP 660
Cdd:cd14898 425 LNGF-INTKARDKIKvsHYAGDVEYDLRDFLDKN---------------REKGQLLIFKN-------------------L 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 661 GEVDrivgldqvagmnetafgaayktkKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQL 740
Cdd:cd14898 470 LIND-----------------------EGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQL 526
|
650 660 670
....*....|....*....|....*....|....*.
gi 688558683 741 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 776
Cdd:cd14898 527 AECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
99-811 |
2.42e-91 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 311.79 E-value: 2.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 99 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 168
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 169 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnippeSPKAVKLQNgilfygelerQLLQANPILESFG 248
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTKLSS----------QISAAEFVLDSFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 249 NAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRF 328
Cdd:cd14879 137 NAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 329 LSNGN----IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMpENTAA-QKLC 401
Cdd:cd14879 217 LASYGchplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 402 HLLGMNVMEFtRAILSPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGI 476
Cdd:cd14879 296 AFLGVSPEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 477 LDIAGfeiFQL------NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGV 550
Cdd:cd14879 371 LDFPG---FQNrsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 551 LALLDEEC-WFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD---FCIIHYAGRVDYKADEWLMKNMDPLndnvatll 626
Cdd:cd14879 445 LGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL-------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 627 hqSTDkFVAelwkdeiqnfqrasfydvsslhespgevdrivgldqvagmnetafgaayktkkgMFRTVGQLyKESLTKLM 706
Cdd:cd14879 517 --SPD-FVN------------------------------------------------------LLRGATQL-NAALSELL 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 707 ATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQ 786
Cdd:cd14879 539 DTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAER 612
|
730 740
....*....|....*....|....*
gi 688558683 787 ACERMIRALELDPNLYRIGQSKIFF 811
Cdd:cd14879 613 IRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
102-812 |
3.33e-87 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 300.19 E-value: 3.33e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 179 CTGESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNS 258
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSR------------------------TTFDSRFKHVNCILEAFGHAKTTLNDLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 259 SRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG----N 333
Cdd:cd14878 137 SCFIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 334 IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTR 413
Cdd:cd14878 217 STAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFQLNSF 490
Cdd:cd14878 297 ALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 491 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIewsfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECW 559
Cdd:cd14878 377 EQLCVNMTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 560 FPKATDKTFVDKL---VQEQGTHGKFQKPRQ------LKDK-ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQS 629
Cdd:cd14878 444 MIWSVEPNLPKKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 630 TDKFVAELWKDEIQnfqrasfydvsslhespgevdrivgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATL 709
Cdd:cd14878 524 ENVVINHLFQSKLV-------------------------------------------------TIASQLRKSLADIIGKL 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 710 RNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACE 789
Cdd:cd14878 555 QKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAE 631
|
730 740
....*....|....*....|....*
gi 688558683 790 RMIRALELDPNL--YRIGQSKIFFR 812
Cdd:cd14878 632 ERCRLVLQQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-812 |
1.50e-84 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 291.92 E-value: 1.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAhvasshKGRKDHNippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN-------------------EISNTLWDSNFILEAFGNAKTLKNNNSSRY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14937 132 GKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFnHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENT--AAQKLCHLLGMNVMEFTRAIL 416
Cdd:cd14937 212 AKDFGNLMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 417 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFQLNSFEQLCIN 496
Cdd:cd14937 291 FTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLIN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 497 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVDKLVQEQ 576
Cdd:cd14937 370 IANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 577 GTHGKFQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDeiqnfqrasfydvSSL 656
Cdd:cd14937 446 SKHEKYASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-------------VEV 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 657 HESPGEVDRIvgldqvagmnetafgaAYKtkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLV 736
Cdd:cd14937 512 SESLGRKNLI----------------TFK------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKV 563
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 737 LDQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 812
Cdd:cd14937 564 FPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
102-764 |
3.70e-76 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 268.70 E-value: 3.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 173
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 174 DQSILCTGESGAGKTENTKKVIQYLAHVasshkgrkdhnippespkavklqNGILFYGELERQLLQANPILESFGNAKTV 253
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI-----------------------QTDSQMTERIDKLIYINNILESMSNATTI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 254 KNDNSSRFGKFIRINFD---------VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-AGEHLRSDLLLEGF 323
Cdd:cd14884 138 KNNNSSRCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNC 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 324 NSYRFLSN----------GNIPIPG----------QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKe 383
Cdd:cd14884 218 GVYGLLNPdeshqkrsvkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 384 rntdqasmpentaaqkLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL 463
Cdd:cd14884 297 ----------------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 464 DRTKRQGA-----------SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGl 532
Cdd:cd14884 361 LKCKEKDEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 533 DLQPCIDLIERpanppgVLALLDE-----ECWFPKATDKTFVD-------KLVQEQGTHGK-------FQKPRQLKDKAD 593
Cdd:cd14884 440 SYSDTLIFIAK------IFRRLDDitklkNQGQKKTDDHFFRYllnnerqQQLEGKVSYGFvlnhdadGTAKKQNIKKNI 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 594 FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdeiqnfqrasfydvsslhespgevdrivgldqva 673
Cdd:cd14884 514 FFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE------------------------------------- 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 674 gmnetafgAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICR 753
Cdd:cd14884 557 --------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILN 628
|
730
....*....|.
gi 688558683 754 QGFPNRIVFQE 764
Cdd:cd14884 629 RGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
103-799 |
3.50e-72 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 255.42 E-value: 3.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 176 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipPESpkavklqngilfygELERQLLQANPILESFGNAKTVKN 255
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGGG---------PET--------------DAFKHLAAAFTVLRSLGSAKTATN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 256 DNSSRFGKFIRINFdVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFN--SYRFLSNGN 333
Cdd:cd14881 127 SESSRIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 334 IPIPGQQDKDNFQETMEAMHIMSFnheEILSMLKVVSAVLQFGNIVFkKERNTDQASMPENTAAQKLCHLLGMNVMEFTR 413
Cdd:cd14881 206 TRQNEAEDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIF 485
Cdd:cd14881 282 GLTTRTHNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 486 QLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKAT 564
Cdd:cd14881 358 KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGT 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 565 DKTFVDKLVQEQGTHGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvaelwkdeiqn 644
Cdd:cd14881 434 AESYVAKIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 645 fqrasfydvsslhespgevdrivgldqvagmneTAFGaayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNH 724
Cdd:cd14881 499 ---------------------------------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNT 536
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 725 EKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 799
Cdd:cd14881 537 TETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
103-812 |
1.28e-70 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 251.94 E-value: 1.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnippespkavklqngilfygelerqLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY-------------------------ILESGIILESFGHASTDSNHNSSR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN-GNIPIPGQ 339
Cdd:cd14905 135 WGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtdQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14905 215 DDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 420 IKVGRDYVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14905 293 SMPVNEAVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 500 EKLQQLFNHTMFILEQEEYQREGIEW-SFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVDKLVQEQGT 578
Cdd:cd14905 361 ERLQQIYLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSR 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 579 HGKF-QKPRQlkdkadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVaeLWKDEIQNFQRA-----SFYD 652
Cdd:cd14905 434 HHLFgKKPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL--FSRDGVFNINATvaelnQMFD 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 653 V-SSLHESPGEVDRIV------GLDQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPN 723
Cdd:cd14905 506 AkNTAKKSPLSIVKVLlscgsnNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPN 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 724 HEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLY 802
Cdd:cd14905 586 SKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPI 663
|
730
....*....|
gi 688558683 803 RIGQSKIFFR 812
Cdd:cd14905 664 QVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
105-811 |
8.05e-69 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 248.35 E-value: 8.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 105 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 174
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 175 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDhnipPESpkavklQNGILFygELERQLLQANPILESFGNAKTVK 254
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD----SEG------ASGVLH--PIGQQILHAFTILEAFGNAATRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 255 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgEH---LRSDLLL-EGFNSYRFLS 330
Cdd:cd14893 152 NRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 331 N-----GNIPIpgqqDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF------KKERN-------TDQASMP 392
Cdd:cd14893 231 QadplaTNFAL----DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGgansttvSDAQSCA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 393 ENTAAQKL--CHLLGMNVMEF-----TRAILSpriKVGRDYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL 463
Cdd:cd14893 307 LKDPAQILlaAKLLEVEPVVLdnyfrTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGIL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 464 ----DRTKRQG----ASFIGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWS 526
Cdd:cd14893 384 ggifDRYEKSNivinSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 527 FIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD------------F 594
Cdd:cd14893 464 NVDITSEQEKCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllF 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 595 CIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQStdkfvaelwkdeiqnfQRASFYDVSSLHESPGEVDRIVGLDQVAG 674
Cdd:cd14893 542 IVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSS----------------KNAVLHAVGAAQMAAASSEKAAKQTEERG 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 675 MNETAFG----AAYKTKKGMFRTVGQLYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 750
Cdd:cd14893 606 STSSKFRksasSARESKNITDSAATDVYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQ 684
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 751 ICRQGFPNRIVFQEFRQRYeiltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 811
Cdd:cd14893 685 ASRSIFTVHLTYGHFFRRY---------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
102-777 |
2.15e-67 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 241.31 E-value: 2.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 180
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 181 GESGAGKTENTKKVIQYLAHvasshkgrkdhniPPESPKAVKLQNGILFygelerqllqanpILESFGNAKTVKNDNSSR 260
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS-------------QPKSKVTTKHSSAIES-------------VFKSFGCAKTLKNDEATR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 261 FGKFIRINFDvTGYIVGANIE-TYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQ 339
Cdd:cd14874 125 FGCSIDLLYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPE--NTAAQKLCHLLGMNVMEFTRAIL 416
Cdd:cd14874 204 SDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 417 SPRIKVGrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFQLNSFEQLCIN 496
Cdd:cd14874 284 LPKSEDG-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLIN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 497 YTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDF----GLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKL 572
Cdd:cd14874 357 SVNERIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHC 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 573 VQEQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEIQNFQrasfyd 652
Cdd:cd14874 432 NLNHTDRSSYGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTS------ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 653 vsslhespgevDRIVgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLE 732
Cdd:cd14874 505 -----------DMIV-------------------------SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFD 548
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 688558683 733 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 777
Cdd:cd14874 549 IPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
103-772 |
1.46e-59 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 218.46 E-value: 1.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 183 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespKAVKLQNGIlfygelerqllqanPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRG-----------ATGRVESSI--------------KAILALVNAGTPLNADSTRCI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHLRSDLLLEGFNsYRFL--SNGNIPIPG 338
Cdd:cd14882 137 LQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEVPPSKL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 339 QQDKDN-------FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKerNTDQASMPENTAAQKLCHLLGMNVMEF 411
Cdd:cd14882 216 KYRRDDpegnverYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 412 TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFQ 486
Cdd:cd14882 294 MWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFH 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 487 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECwfPKATDK 566
Cdd:cd14882 371 RNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 567 TFVDKLVQEQgtHGKFQKPrqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnfq 646
Cdd:cd14882 446 NYIMDRIKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNS----- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 647 rasfydvsslhespgevdrivgldQVAGMnetafgaayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPN 723
Cdd:cd14882 516 ------------------------QVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSD 556
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558683 724 HEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 772
Cdd:cd14882 557 LEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
103-810 |
8.68e-59 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 217.78 E-value: 8.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 182 ESGAGKTENTKKVIQYLAHVASSHKgRKDHNIPPESPKAVKLQNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSR-RLPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 262 GKFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14938 161 SKFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNI-----VFKKE---------------------RNTDQASMPENT 395
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 396 AAQKL-CHLLGMNVMEFTRAILSPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGAS 472
Cdd:cd14938 320 KNLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 473 FIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANppGVLA 552
Cdd:cd14938 399 YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 553 LLDEECWFPKATDKT-FVDKLVQEQGTHGKF-QKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQST 630
Cdd:cd14938 477 SLLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 631 DKFVAELwkdeiqnfqrASFYDVSSLHESPGEVDRIvgldqVAGMNETAFGAAYKTKKGMFRTvgqLYKESLTKLMATLR 710
Cdd:cd14938 557 NEYMRQF----------CMFYNYDNSGNIVEEKRRY-----SIQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQE 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 711 NTNPNFVRCIIPNHEKRA-GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACE 789
Cdd:cd14938 619 TTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVE 690
|
730 740
....*....|....*....|.
gi 688558683 790 RMIRALELDPNLYRIGQSKIF 810
Cdd:cd14938 691 ALIKSYQISNYEWMIGNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
124-274 |
3.47e-58 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 198.72 E-value: 3.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 124 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 202
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558683 203 SSHKGRKDHNIPPESPKAvklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 274
Cdd:cd01363 81 FNGINKGETEGWVYLTEI---------TVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1116-1975 |
2.93e-35 |
|
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: 147.51 E-value: 2.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1116 QAQIDELkiqLAKKEEELQAVLargdEEVA-------QKNNALKQLRELQAQLA-------ELQEDLESEKAARNKAEKL 1181
Cdd:TIGR02168 143 QGKISEI---IEAKPEERRAIF----EEAAgiskykeRRKETERKLERTRENLDrledilnELERQLKSLERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1182 KrDLSEELEALKTELEdTLDTTAAQQELRSKREQEvaelkkaiddetrnheSQIQEMRQRHGTALEEISEQLEQAKRVKG 1261
Cdd:TIGR02168 216 K-ELKAELRELELALL-VLRLEELREELEELQEEL----------------KEAEEELEELTAELQELEEKLEELRLEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1262 NLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1341
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1342 KKGIKLTKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEeknnlleqqeeeeesrknlekQLATLQAQLVETKKKL 1421
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLET-------LRSKVAQLEL---------------------QIASLNNEIERLEARL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1422 EDDVGALEGLEEVKRKLQKDMEvtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQivsNLEKKQKKFDQMLAEE 1501
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAEREL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1502 KTISAR-YAEERDRAEAEAREKDTKALSMARA--------LDEALEAKEEFER-LNKQLRAEMEDLI-SSKDDVGKNVHE 1570
Cdd:TIGR02168 485 AQLQARlDSLERLQENLEGFSEGVKALLKNQSglsgilgvLSELISVDEGYEAaIEAALGGRLQAVVvENLNAAKKAIAF 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1571 LEKSK--------------RTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF---DRDLQARDEQNEEKKR 1633
Cdd:TIGR02168 565 LKQNElgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPG 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1634 ALV-----KQVREMEAELEDERKQRALAVAAK---KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1705
Cdd:TIGR02168 645 YRIvtldgDLVRPGGVITGGSAKTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1706 RTsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQleee 1785
Cdd:TIGR02168 725 SR-------QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---- 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1786 leeEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSkFKASIAALEAKIL 1865
Cdd:TIGR02168 794 ---LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIE 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1866 QLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAS-RRKL 1944
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEY 949
|
890 900 910
....*....|....*....|....*....|....*...
gi 688558683 1945 QRELDDA-------TEASEGLSREVNTLKNRLRRGGPV 1975
Cdd:TIGR02168 950 SLTLEEAealenkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
902-1779 |
8.47e-35 |
|
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: 145.97 E-value: 8.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 902 LIKVKERQVKVENELVEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARL-VAKKQELEEILHDLESRVEEEEERNQ 980
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 981 SLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEE 1060
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1061 EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG 1140
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1141 DEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEvael 1220
Cdd:TIGR02168 417 ERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQALDAAEREL---- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1221 kkaidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNK-ELTNEV---KSLQQAKSESEHKRK 1296
Cdd:TIGR02168 485 -----AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEAalgGRLQAVVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1297 K-LEAQLQEVMAR--FSEGEKVKG-ELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQE-ETRQ 1371
Cdd:TIGR02168 560 KaIAFLKQNELGRvtFLPLDSIKGtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAlELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1372 KLNLSSRIRQLEEEK-----------NNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1440
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1441 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERDRAEAEAR 1520
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE-----------------AEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1521 EKDTKALSMARALDEALEAKEEFERLNKQ---LRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ 1597
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1598 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEkKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEaa 1677
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSE-LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-- 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1678 nkardeaikqlRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQE-DLASSERARRhAEQERDELAD 1756
Cdd:TIGR02168 940 -----------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvNLAAIEEYEE-LKERYDFLTA 1007
|
890 900
....*....|....*....|...
gi 688558683 1757 EISNSASGKAALLDEKRRLEARI 1779
Cdd:TIGR02168 1008 QKEDLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1045-1845 |
1.42e-33 |
|
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: 142.12 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1045 LEDRVGEMTSQL------AEEEEKAKNLGK-VKNKQ-EMMMVDLEERLKKEEKTRQELEKAKRKLDAettdLQDQIAELQ 1116
Cdd:TIGR02168 191 LEDILNELERQLkslerqAEKAERYKELKAeLRELElALLVLRLEELREELEELQEELKEAEEELEE----LTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1117 AQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTEL 1196
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1197 EdtldttaaqqELRSKREQEVAELKKAiDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE 1276
Cdd:TIGR02168 347 E----------ELKEELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1277 LTNEVKSLqqakseSEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1356
Cdd:TIGR02168 416 RERLQQEI------EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1357 QLQDTQELLQEetrqKLNLSSRIRQLEEEKNNLLEQQEEEEES---RKNLEKQLAT-----LQAQLVETKKKLEDDVGAL 1428
Cdd:TIGR02168 490 RLDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSELisvDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1429 EGLEEVK-----------RKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLmvdLDHQRqIVSNLE-----KKQK 1492
Cdd:TIGR02168 566 KQNELGRvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYL---LGGVL-VVDDLDnalelAKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1493 KFDQML--AEEKTISARYAEERdraeaEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHE 1570
Cdd:TIGR02168 642 RPGYRIvtLDGDLVRPGGVITG-----GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1571 LEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRAlvkqvremEAELEDER 1650
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA--------EAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1651 KQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTsrdeiftQSKENEKKLKSLEAEI 1730
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE-------QIEELSEDIESLAAEI 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1731 LQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTL 1810
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 688558683 1811 NTELAGERSA--------AQKSENARQQLERQNKDLKSKLQEL 1845
Cdd:TIGR02168 942 QERLSEEYSLtleeaealENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1018-1899 |
1.66e-31 |
|
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: 135.20 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1018 EAKIKKMEEDIllleDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKtrQELEKA 1097
Cdd:TIGR02169 169 DRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR----EYEGYELLKEK--EALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1098 KRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLRELQAQLAELQEDLESEKAARN 1176
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1177 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaidDETRNHESQIQEMRQRHGTALEEIS---EQL 1253
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK----EELEDLRAELEEVDKEFAETRDELKdyrEKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1254 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1333
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1334 SCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRI-------RQLEEEKNNLLEQQEEEEESRknlekq 1406
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNR------ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1407 latLQAQLVEtkkkleDDVGALEGLEEVKRK-----------LQKDMEVTSQKLEEKA--------IAFDklEKTKNRLQ 1467
Cdd:TIGR02169 549 ---LNNVVVE------DDAVAKEAIELLKRRkagratflplnKMRDERRDLSILSEDGvigfavdlVEFD--PKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1468 QELDDLMV--DLDHQRQIVSN----------LEKKQKKFDQMLAEEKTISaRYAEERDRAEAEAREKDtkalSMARALDE 1535
Cdd:TIGR02169 618 YVFGDTLVveDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1536 ALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1615
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1616 QFDrdlQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQM 1695
Cdd:TIGR02169 773 DLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1696 KDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRL 1775
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1776 EARIAQLEEELEEEQSNMELLNDrFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfka 1855
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLE--------- 999
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 688558683 1856 siaaleakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQV 1899
Cdd:TIGR02169 1000 --------------------EERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1042-1781 |
1.95e-31 |
|
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: 135.20 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1042 KKLLEDRVGemTSQLAEEEEKAKN-LGKVKNKQEMMMVDLEERLKKEEKTRQELEKA-------KRKLDAETTDLQDQIA 1113
Cdd:TIGR02169 156 RKIIDEIAG--VAEFDRKKEKALEeLEEVEENIERLDLIIDEKRQQLERLRREREKAeryqallKEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1114 ELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnkaekLKRDLsEELEALK 1193
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKL----TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-----VKEKI-GELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1194 TELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESD 1273
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1274 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMarfSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvss 1353
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQ---EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1354 lESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE 1433
Cdd:TIGR02169 454 -EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1434 VKRKLQKDME-----------VTSQKLEEKAIAFDKLEKTK-------NRLQQELDDL--------------MVDLDHQR 1481
Cdd:TIGR02169 533 VGERYATAIEvaagnrlnnvvVEDDAVAKEAIELLKRRKAGratflplNKMRDERRDLsilsedgvigfavdLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1482 Q-----------IVSNLEKKQKKFDQM--------LAE-----------EKTISARYAEERDRAEAEAREKDtkalSMAR 1531
Cdd:TIGR02169 613 EpafkyvfgdtlVVEDIEAARRLMGKYrmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1532 ALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ 1611
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1612 AMKAQFDrdlQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKL 1691
Cdd:TIGR02169 769 ELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1692 QAQMKDYQRELEEARTSRDEIFTQSKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1764
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810
....*....|....*..
gi 688558683 1765 KAALLDEKRRLEARIAQ 1781
Cdd:TIGR02169 926 LEALEEELSEIEDPKGE 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1664 |
1.29e-29 |
|
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: 129.41 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 870 LRHWQWWRLftkvkpLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEE 949
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 950 MRARLVAKKQELEEILHDLESrveEEEERNQSLQNEKKKmqshiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDIL 1029
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLER---QLEELEAQLEELESK------------------LDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1030 LLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLq 1109
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1110 dQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEEL 1189
Cdd:TIGR02168 434 -ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1190 EAlKTELEDTLDTTAAQQELRSKREQEV-AELKKAIDD-ETRNHESQIQ----------------EMRQRHGTALEeiSE 1251
Cdd:TIGR02168 513 KN-QSGLSGILGVLSELISVDEGYEAAIeAALGGRLQAvVVENLNAAKKaiaflkqnelgrvtflPLDSIKGTEIQ--GN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1252 QLEQAKRVKGNLEKNKQTLESDNK---------ELTNEVKSLQQAksesEHKRKKLEAQLQEVMA---RFSEGEKVKGEL 1319
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKlrkalsyllGGVLVVDDLDNA----LELAKKLRPGYRIVTLdgdLVRPGGVITGGS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1320 ADRTHKI---QTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1396
Cdd:TIGR02168 666 AKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1397 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSqkleekaIAFDKLEKTKNRLQQELDDLMVD 1476
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK-------EELKALREALDELRAELTLLNEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1477 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1556
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1557 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ-----ATEDAKLRLEVnMQAMKAQFDRDLQARDEQNEEK 1631
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEE-AEALENKIEDDEEEARRRLKRL 977
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 688558683 1632 KRAL----------VKQVREMEAELEDERKQRALAVAAKKKLE 1664
Cdd:TIGR02168 978 ENKIkelgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1007-1781 |
2.50e-28 |
|
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: 125.18 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1007 RQKLQLEKVTAEA----KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEE 1082
Cdd:TIGR02169 200 LERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1083 RLKKEEKTRQ-ELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG---DEEVAQKNNALKQL---- 1154
Cdd:TIGR02169 280 KIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelEREIEEERKRRDKLteey 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1155 RELQAQLAELQEDLES-EKAARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhES 1233
Cdd:TIGR02169 360 AELKEELEDLRAELEEvDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1234 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF---- 1309
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRavee 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1310 ---SEGEKVKGELAD-----RTHKIQTE------LDNVSCLLEDAEKKGIKLTKDVsslesQLQDTQELLQEETRQKLNL 1375
Cdd:TIGR02169 515 vlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNVVVEDDAVAKEAIELLKRR-----KAGRATFLPLNKMRDERRD 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1376 SSRIR------------QLEEEKNNLLEQQEEEEESRKNLEKQLATL-QAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1442
Cdd:TIGR02169 590 LSILSedgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1443 EVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAE 1518
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1519 AREKDTKALSMARaLDEALEAKEefERLNKqLRAEMEDLisSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1598
Cdd:TIGR02169 750 EQEIENVKSELKE-LEARIEELE--EDLHK-LEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1599 TEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAAN 1678
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1679 KARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKE------NEKKLKSLEAEILQLQEDLASSERARRHAEQERD 1752
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
810 820
....*....|....*....|....*....
gi 688558683 1753 ELADEISNSASGKAALLDEKRRLEARIAQ 1781
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
108-753 |
3.34e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 117.54 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 108 LKDRYYSGLIYTYSGLFCV-VINPYKNL------PIYSENIIEMYRGKKRHE--MPPHIYAISE---------------- 162
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 163 ----SAYRCMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVAS----------------------------------- 203
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQpalskgseetckvsgstrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 204 -----------SHKGRKDHNI-----PPE----------SPKAVKLQNGILFYG--------ELERQL------------ 237
Cdd:cd14894 166 rteeartiallEAKGVEKYEIvlldlHPErwdemtsvsrSKRLPQVHVDGLFFGfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 238 ----LQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------KDERTFHV 302
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 303 FYQLLAGAGEH-----LRSDLLLEGFN--SYRFLSNGNIPIPG--------QQDKDNFQETMEAMHIMSFNHEEILSMLK 367
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 368 VVSAVLQFGNIVFKKERNTDQASMPEN---TAAQKLCHLLGMNVMEFTRAIL---SPRIKVGRDYVQKAQTKEQADFAVE 441
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLmtkSVSLQSTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 442 ALAKATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQql 505
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY-- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 506 fnhtmfileQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKAT----------DKTFVDKLVQE 575
Cdd:cd14894 564 ---------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 576 QGTHGKfQKPRQLKDKA----------DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDEiqnf 645
Cdd:cd14894 635 NSSRLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNES---- 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 646 qrasfydvSSLHESPgevdrivgldqvaGMNETAFGAAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHE 725
Cdd:cd14894 710 --------SQLGWSP-------------NTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAK 767
|
810 820
....*....|....*....|....*...
gi 688558683 726 KRAGKLEPHLVLDQLRCNGVLEGIRICR 753
Cdd:cd14894 768 KQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1403-1975 |
4.05e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 117.35 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1403 LEKQLATLQAQ---------LVETKKKLEDDVGAL--EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELD 1471
Cdd:COG1196 198 LERQLEPLERQaekaeryreLKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1472 DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1551
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1552 AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfDRDLQARDEQNEEK 1631
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1632 KRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE 1711
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1712 IftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE-----LADEISNSASGKAALLDEKRRLEARIAQLEEEL 1786
Cdd:COG1196 517 A--GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1787 EEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKilq 1866
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL--- 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1867 leEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQR 1946
Cdd:COG1196 672 --AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
570 580 590
....*....|....*....|....*....|...
gi 688558683 1947 ELDDATEAS----EGLSREVNTLKNRLRRGGPV 1975
Cdd:COG1196 750 EEALEELPEppdlEELERELERLEREIEALGPV 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
887-1585 |
1.78e-25 |
|
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: 115.54 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 887 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 966
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 967 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1046
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1047 DRVGEMTSQLAEEEEKAKNLGKVKNKQEM--------MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI---AEL 1115
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELaqlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEGY 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1116 QAQIDelkiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE----DLESEKAARNKAEKLKRDLSEELEA 1191
Cdd:TIGR02168 536 EAAIE------AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLVK 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1192 LKTELEDTL-----------DTTAAQQELRSKREQEVAELKK--------AIDDETRNHESQIQEMRQRhgtaLEEISEQ 1252
Cdd:TIGR02168 610 FDPKLRKALsyllggvlvvdDLDNALELAKKLRPGYRIVTLDgdlvrpggVITGGSAKTNSSILERRRE----IEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1253 LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDN 1332
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1333 VSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQA 1412
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1413 QLVETKKKLEDDVGALEGLEEVKRKLQKD-------MEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1485
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1486 NLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1564
Cdd:TIGR02168 926 QLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFL 1005
|
730 740
....*....|....*....|.
gi 688558683 1565 GKNVHELEKSKRTLEQQVEEM 1585
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEI 1026
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1153-1900 |
5.36e-25 |
|
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: 114.06 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1153 QLRELQAQLAELQEDLESEKAARNKAEKlkrDLSEELEALKTELEDTLDT----TAAQQELRSKREQEVAELKKA---ID 1225
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVI---DLQTKLQEMQMERDAMADIrrreSQSQEDLRNQLQNTVHELEAAkclKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1226 DETRNHESQIQEMRQ---RHGTALEEISEQLEQAKRVKGnleknKQTLESDNKElTNEVKSLQQAKSESehkRKKLEAQL 1302
Cdd:pfam15921 163 DMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFEEASG-----KKIYEHDSMS-TMHFRSLGSAISKI---LRELDTEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1303 QEVMAR-FSEGEKVKGELADRTHKI----QTELDNVSCLLEDAEKKGIKLTKDVSSLESQ---LQDTQELLQEETRQKLn 1374
Cdd:pfam15921 234 SYLKGRiFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1375 lSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLVETKKKLEDDVgalegleevkRKLQKDMEVTSQKLEEKAI 1454
Cdd:pfam15921 313 -SMYMRQLSD------------------LESTVSQLRSELREAKRMYEDKI----------EELEKQLVLANSELTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1455 AFDKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKTISARYAEERDR-AEAEAREKDTKAL---- 1527
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEALLKAMksec 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1528 --SMARALdEALEAKEEFERLNKQLRAEMEdliSSKDDVGKNVHELEKSKRTLE---QQVEEMRTQLEELEDELQAT--E 1600
Cdd:pfam15921 443 qgQMERQM-AAIQGKNESLEKVSSLTAQLE---STKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1601 DAKLRLEVNMQAMKAQfdrdlqarDEQNEEKkralvkQVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIE-AANK 1679
Cdd:pfam15921 519 ITKLRSRVDLKLQELQ--------HLKNEGD------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQlVGQH 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1680 ARDEAIKQLRK--LQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADE 1757
Cdd:pfam15921 582 GRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNE 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1758 ISNSASGKAALLDEKRRLEARIaqleeelEEEQSNMELLNDRFRkttMQVDTLNTELAGERSAAQKSENA---------- 1827
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNF-------RNKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSMEGSdghamkvamg 731
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1828 -RQQLER---QNKDLKSKLQELEGSVK--SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1900
Cdd:pfam15921 732 mQKQITAkrgQIDALQSKIQFLEEAMTnaNKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
960-1722 |
1.22e-24 |
|
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: 112.85 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 960 ELEEILHDLEsRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQ--------LEKVTAEAKIKKMEEDILLL 1031
Cdd:TIGR02169 171 KKEKALEELE-EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyellKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1032 EDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1111
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1112 IAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELqedlesEKAARNKAEKLKrDLSEELEA 1191
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------DKEFAETRDELK-DYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1192 LKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLE 1271
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1272 SDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF-------SEGEKVKGELAD-----RTHKIQTE------LDNV 1333
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveevlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1334 SCLLEDAEKKGIKLTKDVS------------------------------------------------------------- 1352
Cdd:TIGR02169 553 VVEDDAVAKEAIELLKRRKagratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaa 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1353 ----------SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1422
Cdd:TIGR02169 633 rrlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1423 DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1502
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1503 TISARyaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQV 1582
Cdd:TIGR02169 793 IPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1583 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDR------DLQARDEQNEEKKRALVKQVREMEAELEdERKQRALA 1656
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqieKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEE 949
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1657 VAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEI--FTQSKENEKK 1722
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIleRIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
948-1578 |
1.40e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.26 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 948 EEMRARL--------VAKK-QELEEILHDLESRVeeeeernqsLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE 1018
Cdd:COG1196 196 GELERQLeplerqaeKAERyRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1019 AKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKAK 1098
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1099 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKA 1178
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1179 EKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR 1258
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1259 VKGNLEKNKQTLESDNKELTNEVkslQQAKSESEHKRKKLEAQL---------QEVMARFSEGEKVKGELADRTHKIQTE 1329
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGL---AGAVAVLIGVEAAYEAALeaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1330 L------------DNVSCLLEDAEKKGIK-LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1396
Cdd:COG1196 577 LpldkiraraalaAALARGAIGAAVDLVAsDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1397 EESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1476
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEE-------LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1477 LDHQRQIVSNLEkkqkkFDQMLAEEKTISARYAEERDRAEAEAREKDTKAlSMAR-------ALDEALEAKEEFERLNKQ 1549
Cdd:COG1196 730 LEAEREELLEEL-----LEEEELLEEEALEELPEPPDLEELERELERLER-EIEAlgpvnllAIEEYEELEERYDFLSEQ 803
|
650 660
....*....|....*....|....*....
gi 688558683 1550 LraemEDLISSKDDVGKNVHELEKSKRTL 1578
Cdd:COG1196 804 R----EDLEEARETLEEAIEEIDRETRER 828
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1007-1596 |
1.63e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 109.00 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1007 RQKLQLEKV-TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1085
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1086 KEEKTRQELEKAKRkldaETTDLQDQIAELQAQIDELKIQLAKKEEELqavlargdEEVAQKNNALKQLRELQAQLAELQ 1165
Cdd:PRK03918 232 ELEELKEEIEELEK----ELESLEGSKRKLEEKIRELEERIEELKKEI--------EELEEKVKELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1166 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ---EVAELKKAID--DETRNHESQIQEMRQ 1240
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1241 RH-GTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE---------------SEHKRKKLeaqLQE 1304
Cdd:PRK03918 380 RLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKEL---LEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1305 VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK--KGIKLTKDVSSLESQLQ--DTQELLQ-----EETRQKLN- 1374
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKkyNLEELEKkaeeyEKLKEKLIk 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1375 LSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAI 1454
Cdd:PRK03918 537 LKGEIKSLKKE-----------LEKLEELKKKLAELEKKLDELEEELAE---LLKELEELGFESVEELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1455 AFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErdraeaEAREKDTKALSMARALD 1534
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELA 676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1535 EALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1596
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1362-1927 |
2.31e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1362 QELLQEETRQKLNLSS-RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1440
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1441 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1520
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1521 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1600
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1601 DAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRAlvKQVREMEAELEDERKQRALAVAAKKKLEM---------DLKDVE 1671
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavaVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1672 AQIEAANKARDEAIKQ--LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQ 1749
Cdd:COG1196 534 AAYEAALEAALAAALQniVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1750 ERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEeqsnMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQ 1829
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE----GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1830 QLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQY 1909
Cdd:COG1196 690 EEELELEEALLAEEEEE-----------RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 688558683 1910 KEQMEKANSRMKQLKRQL 1927
Cdd:COG1196 759 PPDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
892-1652 |
1.55e-22 |
|
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: 105.92 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 892 EEEMQAKDEELIKVKERQVKVE-------NELVEMERKHQQLLEEKNILAEQLQAE-TELFAEAEEMRARLVAKKQELEE 963
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 964 ILHDLESRVEEEEERNQSLqNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEakIKKMEEDILLLEDQNSKFLKEKK 1043
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRL-EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1044 LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK 1123
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1124 IQLAKKEEELQavlaRGDEEVAQKNNALKQLRELQAQLAELQED-----------LESEKAARNKAEKLKRDLSEELEAL 1192
Cdd:TIGR02169 406 RELDRLQEELQ----RLSEELADLNAAIAGIEAKINELEEEKEDkaleikkqewkLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1193 KTELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE----------------EIS 1250
Cdd:TIGR02169 482 EKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1251 EQLEQAKRVKG-------------------------------------------------------NLEKNKQ------- 1268
Cdd:TIGR02169 562 EAIELLKRRKAgratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvveDIEAARRlmgkyrm 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1269 -TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1347
Cdd:TIGR02169 642 vTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1348 TKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDD--- 1424
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSrip 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1425 --VGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1502
Cdd:TIGR02169 795 eiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1503 TISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTlEQQV 1582
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSL 953
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558683 1583 EEMRTQLEELEDELQATEDaklrleVNMQAMKaQFDRDLQARDEQnEEKKRALV---KQVREMEAELEDERKQ 1652
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEP------VNMLAIQ-EYEEVLKRLDEL-KEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
848-1490 |
8.11e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 8.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 848 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRLftkvkpllQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL 926
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 927 LEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshIQDLEEQLDEEEAA 1006
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1007 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1086
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1087 EEKTRQELEKAKRKLDAEttdlqdqIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE 1166
Cdd:COG1196 433 LEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1167 DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAL 1246
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1247 EEISEQLEQAKRVKGNLEKNKQTLESDNK----ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADR 1322
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARyyvlGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1323 THKIQTEldnvscLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1402
Cdd:COG1196 666 SRRELLA------ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1403 LEKQLATLQAQLVETKKKLEDDVGALEG-LEEVKRKLQK----DMEVtsqkLEEkaiaFDKLEKTKNRLQQELDDLMVDL 1477
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELEReLERLEREIEAlgpvNLLA----IEE----YEELEERYDFLSEQREDLEEAR 811
|
650
....*....|...
gi 688558683 1478 DHQRQIVSNLEKK 1490
Cdd:COG1196 812 ETLEEAIEEIDRE 824
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1235-1846 |
2.49e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1235 IQEMRQRHGTaLEEISEQLEQAKRVKGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGE 1313
Cdd:COG1196 195 LGELERQLEP-LERQAEKAERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1314 KVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQD-TQELLQEEtrqklnlsSRIRQLEEEKNNLLEQ 1392
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEElEEELAELE--------EELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1393 QEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1472
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1473 LMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalsmARALDEALEAKEEFERLNKQLRA 1552
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1553 EMEDLISSKDDVGKNVHELEKSKRtLEQQVEEMRTQLEELEDELQATEDAKLRLEVNmqamkaqfDRDLQARDEQNEEKK 1632
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1633 RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDyqRELEEARTSRDEI 1712
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE--AALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1713 FTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSN 1792
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 688558683 1793 MELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1846
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1171-1729 |
3.09e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 101.29 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1171 EKAARNKAEKLKrdlseELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID---DETRNHESQIQEMRQRHGTaLE 1247
Cdd:PRK03918 161 ENAYKNLGEVIK-----EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINeisSELPELREELEKLEKEVKE-LE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1248 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQ 1327
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1328 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEEKNNLLEQQ------------ 1393
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekel 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1394 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdmEVTSQKLEEkaiafDKLEKTKNRLQQELDDL 1473
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE-----EHRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1474 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARY--AEERDRAEAEAREKDTKALSmaRALDEALEAKEEFERLNKQLR 1551
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKelAEQLKELEEKLKKYNLEELE--KKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1552 A------EMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR-TQLEELEDELQATE----------DAKLRLEVNMQAMK 1614
Cdd:PRK03918 543 SlkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1615 AQFDRDLQARDEQNEEKKRA--LVKQVREMEAELEDERKQRAlaVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ 1692
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLeeLRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 688558683 1693 AQ---MKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAE 1729
Cdd:PRK03918 701 EEleeREKAKKELEKLEKALERV-EELREKVKKYKALLKE 739
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1040-1914 |
4.50e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 101.20 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1040 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQE--------------LEKAKRKLDAET 1105
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAkkaleyyqlkekleLEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1106 TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDL 1185
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1186 SEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHgtaLEEISEQLEQAKRVKGNLEK 1265
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKLQ---EKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1266 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQlqevMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI 1345
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL----KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1346 KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDV 1425
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1426 GALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD--------------HQRQIVSNLEKKQ 1491
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIavleidpilnlaqlDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1492 KKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHEL 1571
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1572 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERK 1651
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1652 QRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQaqmKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1731
Cdd:pfam02463 782 KTEKLKVEEEKEE-KLKAQEEELRALEEELKEEAELLEEEQ---LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1732 QLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1811
Cdd:pfam02463 858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1812 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1891
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
890 900
....*....|....*....|...
gi 688558683 1892 LKEVFMQVEDERRHADQYKEQME 1914
Cdd:pfam02463 1018 RLKEFLELFVSINKGWNKVFFYL 1040
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1040-1762 |
3.04e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.06 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1040 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQElEKAKRKLDAETTDLQDQIAELQAQI 1119
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA-EDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1120 DELKIQLAKKEEEL-QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnKAEKLKRDLSE---------EL 1189
Cdd:PTZ00121 1174 DAKKAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEakkaeeernNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1190 EALKTELEDTLDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQT 1269
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1270 LESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA--RFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1347
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1348 TKdvSSLESQLQDTQELLQEETRQKLNLSSRI---RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDd 1424
Cdd:PTZ00121 1411 KK--AAAAKKKADEAKKKAEEKKKADEAKKKAeeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE- 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1425 vgALEGLEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQI--VSNLEKKQKKFDQMLAEEk 1502
Cdd:PTZ00121 1488 --AKKKAEEAKKK--------ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEE- 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1503 tisARYAEERDRAEAEAREKDTKALSMARAlDEALEAKEEfeRLNKQLRAEMEDLISSKDDVGKnvHELEKSKRTLEQQV 1582
Cdd:PTZ00121 1557 ---LKKAEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEA--RIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1583 EEMRTQLEELEDELQatEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAlaVAAKKK 1662
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEA--EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKA 1704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1663 LEMDLKDVEA--QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE---IFTQSKENEKKLKSLEAEILQLQEDL 1737
Cdd:PTZ00121 1705 EELKKKEAEEkkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
730 740
....*....|....*....|....*
gi 688558683 1738 ASSERARRHAEQERdELADEISNSA 1762
Cdd:PTZ00121 1785 LDEEDEKRRMEVDK-KIKDIFDNFA 1808
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
913-1284 |
4.05e-20 |
|
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: 98.21 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 913 ENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSH 992
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 993 IQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1072
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1073 QEMMMVDLEERLKKEEKTRQELEkakrkldAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK 1152
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1153 QLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR----SKREQEVAELKKAIDDET 1228
Cdd:TIGR02168 909 KRSELRRELEELREKLA---QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKELG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1229 RNHESQIQEmrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSL 1284
Cdd:TIGR02168 986 PVNLAAIEE--------YEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1040-1624 |
6.07e-20 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 97.42 E-value: 6.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1040 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKakrkLDAETTDLQDQIAE----- 1114
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAEterer 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1115 --LQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLE----SEKAARNKAEKLKRD---- 1184
Cdd:PRK02224 275 eeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDaddl 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1185 ------LSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIddetrnhesqiqemrqrhgtalEEISEQLEQAKR 1258
Cdd:PRK02224 355 eeraeeLREEAAELESELEEA-------REAVEDRREEIEELEEEI----------------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1259 VKGNLEKNKQTLESDNKELTNEVKSlqqaksesehkrkkLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLE 1338
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAE--------------LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1339 DAEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEknnlleqqeeeeesRKNLEKQLATLQAQLVETK 1418
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEER--------------REDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1419 KKLE---DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFD-KLEKTKNRLQQ--ELDDLMVDLDHQRQIVSNLEKKQK 1492
Cdd:PRK02224 537 ERAEelrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNsKLAELKERIESleRIRTLLAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1493 KFDQMLAEEKTisaRYAEERDRAEAEAREKDtkalsmARALDEALEAKEEFERLNKQLRAEMEDLISSKDDvgknvheLE 1572
Cdd:PRK02224 617 ALAELNDERRE---RLAEKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQ 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1573 KSKRTLEQQVEEmrtqLEELEDELQATEDAKLRLEV------NMQAMKAQFDRDLQAR 1624
Cdd:PRK02224 681 AEIGAVENELEE----LEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQR 734
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
910-1498 |
1.53e-19 |
|
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: 95.86 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 910 VKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKM 989
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 990 QSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1065
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1066 LGKVKNKQEMMMVDLEERLKKEEKTRqELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVA 1145
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1146 QKNNALKQLRELQAQLAELQEDL-----ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL 1220
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLnqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1221 KKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA 1300
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1301 QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIR 1380
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1381 QLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE--DDVGALEGLEEVKRKLQKDMEVTSQ-------KLEE 1451
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQtqkslkkKQEE 586
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 688558683 1452 KAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1498
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1247-1958 |
1.81e-19 |
|
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: 95.91 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1247 EEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEH----KRKKLEAQLQEVMARFSEGEKVKGELADR 1322
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1323 THKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKL-NLSSRIRQLEEEKNNLLEQQEEEEESRK 1401
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIgELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1402 NLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQR 1481
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1482 QIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSK 1561
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1562 DDVGKNVHELEKSKRTLEQQVEEMRTQLEEL--------------------------------------EDELQATEDAK 1603
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaqlgsvgeryataievaagnrlnnvvvEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1604 LRLEVN-----------MQAMKA------------------QFDRDLQA------RDE---QNEEKKRALVKQVR--EME 1643
Cdd:TIGR02169 566 LLKRRKagratflplnkMRDERRdlsilsedgvigfavdlvEFDPKYEPafkyvfGDTlvvEDIEAARRLMGKYRmvTLE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1644 AELEDE--------RKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1715
Cdd:TIGR02169 646 GELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1716 SKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQsnMEL 1795
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE--LSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1796 LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSV------KSKFKASIAALEAKILQLEE 1869
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1870 QLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRqLEEAEEEATRANASRRKLQRELD 1949
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-PKGEDEEIPEEELSLEDVQAELQ 961
|
....*....
gi 688558683 1950 DATEASEGL 1958
Cdd:TIGR02169 962 RVEEEIRAL 970
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1160-1779 |
2.12e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.49 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1160 QLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttaaqqelrskrEQEVAELKKAIDDetrnHESQIQEMR 1239
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIE----------------EKEEKDLHERLNG----LESELAELD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1240 qrhgTALEEISEQLEQAKRVKGN----LEKNKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKV 1315
Cdd:PRK02224 220 ----EEIERYEEQREQARETRDEadevLEEHEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1316 KGELADRTHKIQTELDNVSCLLEDaekkgikLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqee 1395
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREE-------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA--------- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1396 eeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMV 1475
Cdd:PRK02224 359 -----EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1476 DLdhqrqivSNLEKKQKKFDQMLAEEKTISAryaeerdraeaearEKDTKALSMARALDEALEAKEEferlnkqLRAEME 1555
Cdd:PRK02224 434 TL-------RTARERVEEAEALLEAGKCPEC--------------GQPVEGSPHVETIEEDRERVEE-------LEAELE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1556 DLISSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqfdrDLQARDEQNEEKKRAL 1635
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIA----------------------ERRETIEEKRERAEEL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1636 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1715
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1716 SKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKR-RLEARI 1779
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEI 683
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
888-1775 |
6.19e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 94.27 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 888 VTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlVAKKQELEEILHD 967
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 968 LESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLED 1047
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1048 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLdaettdLQDQIAELQAQiDELKIQLA 1127
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL------EKLQEKLEQLE-EELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1128 KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTtaaqQ 1207
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----Q 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1208 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR---VKGNLEKNKQTLESDNKELTNEVKSL 1284
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglkVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1285 QQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ--TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1362
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKlrLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1363 ELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1442
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1443 EVTSQKLEEKAIAfdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREK 1522
Cdd:pfam02463 697 RQLEIKKKEQREK--EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1523 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDA 1602
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1603 KLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARD 1682
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1683 EAIKQLRKLQAQMKDYQRELEEartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSA 1762
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKE---------EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 688558683 1763 SGKAALLDEKRRL 1775
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
894-1585 |
1.42e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.28 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 894 EMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVE 973
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 974 EEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEdillledqNSKFLKEKKLLEDRVGEM 1052
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEE--------KKKADEAKKAEEKKKADE 1306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1053 TSQLAEEEEKAKNLGK----VKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAettdlqdqiAELQAQIDELKIQLAK 1128
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA---------AEEKAEAAEKKKEEAK 1377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1129 KEEElqaVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRdlseeLEALKTELEDTLDTTAA 1205
Cdd:PTZ00121 1378 KKAD---AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeaKKKAEEKKK-----ADEAKKKAEEAKKADEA 1449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1206 QQELRSKREQEvaELKKAIDDETRNHESQIQEMRQRHGTAL----EEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1281
Cdd:PTZ00121 1450 KKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1282 KSLQQAKS-----ESEHKRKKLEAQLQEVMARFSEGEKVkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1356
Cdd:PTZ00121 1528 KKAEEAKKadeakKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1357 QLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLVETKKKLEDDVGALEGLEE 1433
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEelkKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1434 VKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELD--DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisARYAEE 1511
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEAEEDKKKAEE----AKKDEE 1754
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558683 1512 RDRAEAEAREKDTKALSMARALDEALeAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1585
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM 1827
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
935-1313 |
3.08e-18 |
|
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: 92.05 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 935 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEK 1014
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1015 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEmtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQEL 1094
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1095 EKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA 1174
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1175 RNKAEKLKRDLSEELEALKTELedtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtALEEIS---- 1250
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEEL--------SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-----ALEPVNmlai 978
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558683 1251 EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKR-KKLEAQLQEVMARFSEGE 1313
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAfEAINENFNEIFAELSGGT 1042
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
883-1732 |
5.35e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 91.19 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 883 KPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL-LEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL 961
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLeLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 962 EEILHDLESRVEEEEERNQSLQN-EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1040
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEkEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1041 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1120
Cdd:pfam02463 336 EIEELE--------KELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1121 ELKIQLAKKEEELQAVLArgDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK---AEKLKRDLSEELEALKTELE 1197
Cdd:pfam02463 408 QLLLELARQLEDLLKEEK--KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdelELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1198 DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE- 1276
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQk 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1277 LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1356
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1357 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKR 1436
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1437 KLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1516
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1517 AEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1596
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1597 QATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElEDERKQRALAVAAKKKLEMDLKDVEAQIEA 1676
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE-EEPEELLLEEADEKEKEENNKEEEEERNKR 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1677 ANKARDEAIKQLRKLQAQMKdyqrELEEARTSRDEIFTQSKENEKKLKSLEAEILQ 1732
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFE----EKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1325-1971 |
5.74e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 91.00 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1325 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1404
Cdd:pfam01576 16 KVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1405 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1484
Cdd:pfam01576 96 NEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1485 SNLEKKQKKFDQMLAEektisaryAEERDRAEAEAREkdtkalsmaraldealeakeEFERLNKQLRAEMEDLISSKDDv 1564
Cdd:pfam01576 176 KSLSKLKNKHEAMISD--------LEERLKKEEKGRQ--------------------ELEKAKRKLEGESTDLQEQIAE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1565 gknvhelekskrtLEQQVEEMRTQLEELEDELQAtedAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEA 1644
Cdd:pfam01576 227 -------------LQAQIAELRAQLAKKEEELQA---ALARLE------------EETAQKNNALKKIRELEAQISELQE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1645 ELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE-EARTSRDEIFTQSKENEKKL 1723
Cdd:pfam01576 279 DLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1724 KSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1803
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1804 TMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQElEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANK 1883
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1884 IVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVN 1963
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
....*...
gi 688558683 1964 TLKNRLRR 1971
Cdd:pfam01576 598 NLEKKQKK 605
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
876-1472 |
3.18e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.58 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 876 WRLFTKVKPLLQVTRQEEEMQAKDEEliKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLV 955
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTE--NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 956 AKKQELEEilhdLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlEKVTAEAKIKKMEEDILLLEDQN 1035
Cdd:PRK03918 242 ELEKELES----LEGSKRKLEEKIRELEERIEELKKEIEELE---------------EKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1036 SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDaETTDLQDQIAEL 1115
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1116 QAQIDELKIQlaKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE-----LE 1190
Cdd:PRK03918 378 KKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1191 ALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDE---TRNHE--SQIQEMRQR-HGTALEEISEQLEQAKRVKGNLE 1264
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselIKLKElaEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1265 KNKQTLESDNKELtNEVKSLQQAKSESEHKRKKLEAQLQEVMAR-----FSEGEKVKG-------------ELADRTHKI 1326
Cdd:PRK03918 536 KLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEErlkelepfyneylELKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1327 QTELDNVSCL---LEDAEKKGIKLTKDVSSLESQLQDTQELLQEET-----RQKLNLSSRIRQLEEEKNNLLEQQEEEEE 1398
Cdd:PRK03918 615 EREEKELKKLeeeLDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558683 1399 SRKNLEKQLATLQaqlvETKKKLEDDVGALEGLEEVKRKLQKdmevtsQKLEEKAIAFDKLEKTKNRLQQELDD 1472
Cdd:PRK03918 695 TLEKLKEELEERE----KAKKELEKLEKALERVEELREKVKK------YKALLKERALSKVGEIASEIFEELTE 758
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
940-1778 |
1.76e-16 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 86.05 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 940 ETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKkmqshiQDLEEQLDEEEAARQKLQLEKVTAEA 1019
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1020 KIKKMEEDILLLEDQNSKFLKEkklledrvgemtsqlaeeeekakNLGKVKNKQEMmmvdleerlkkEEKTRQELEKAKR 1099
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDA-----------------------DIETAAADQEQ-----------LPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1100 KLDAETTDLQDQIAELQAQIdelkiqlAKKEEELQAVLARGDEEVAqknnalKQLRELQAQLAELQEDLES-EKAARNKA 1178
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRR-------SKIKEQNNRDIAGIKDKLA------KIREARDRQLAVAEDDLQAlESELREQL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1179 EKLKRDLSEELEALKTELEDT---LDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQ-LE 1254
Cdd:pfam12128 429 EAGKLEFNEEEYRLKSRLGELklrLNQATATPELLLQLENFDERIERA--REEQEAANAEVERLQSELRQARKRRDQaSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1255 QAKRVKGNLEKNKQTLEsdnkeltnEVKSLQQAKSESEHKRKKLEAQLQevmarfsegEKVKGELADRTHKIQTELDNVS 1334
Cdd:pfam12128 507 ALRQASRRLEERQSALD--------ELELQLFPQAGTLLHFLRKEAPDW---------EQSIGKVISPELLHRTDLDPEV 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1335 clleDAEKKGIKLTKDVSSLESQLQDTQELLQEEtrqklnlssriRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQL 1414
Cdd:pfam12128 570 ----WDGSVGGELNLYGVKLDLKRIDVPEWAASE-----------EELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1415 VETKKKLEDDVGALEGLEEVKRKLqkdmevTSQKLEEKaiafDKLEKTKNRLQQELDDLMVDLDHQRQIvsnLEKKQKKF 1494
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRL------FDEKQSEK----DKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAW 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1495 DQMLAEEKTiSARYAEERDRAEAEAREKDTKAlsmarALDEALEAKEE-FERLNKQLRAEMEDLISSKDDVGKNVHELEK 1573
Cdd:pfam12128 702 LEEQKEQKR-EARTEKQAYWQVVEGALDAQLA-----LLKAAIAARRSgAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1574 SKRTLEQQVEemrtqleeledelqatedaklRLEVNMQAMkAQFDRDLQardEQNEEKKRALVKQVREMEAELEDERKQR 1653
Cdd:pfam12128 776 EIRTLERKIE---------------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQL 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1654 ALAVAAKKkleMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQR-----ELEEARTSRDEIFTQSKENEKKLKSLEA 1728
Cdd:pfam12128 831 ARLIADTK---LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSE 907
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1729 EILQLQEDLASSERARRHAEQER--DELADEISNSASGKAALLDEKRRLEAR 1778
Cdd:pfam12128 908 SVKKYVEHFKNVIADHSGSGLAEtwESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1081-1656 |
2.74e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 85.35 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1081 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLA----KKEEELQAVLARGDEEVAQKNNALKQLR- 1155
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEa 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1156 --------------ELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1221
Cdd:COG4913 367 llaalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1222 KAIDDETRNHESQIQ------EMRQR------------HGTALEEISEQlEQAKRVKGNLEKNKQTLESDNKELTNEVKS 1283
Cdd:COG4913 447 DALAEALGLDEAELPfvgeliEVRPEeerwrgaiervlGGFALTLLVPP-EHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1284 LQQAKSESEHKRKKLEAQ-------LQEVMARF-------SEGE------------KVKGELADRTHKIQTELDNVSCLL 1337
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKphpfrawLEAELGRRfdyvcvdSPEElrrhpraitragQVKGNGTRHEKDDRRRIRSRYVLG 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1338 EDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeknnLLEQQEEEEESRKNLEKQLATLQAQLvet 1417
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAEL--- 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1418 kKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkFDQM 1497
Cdd:COG4913 678 -ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEER 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1498 LAE------EKTISARYAEERDRAEAEAREKDTKALSMARA-----------LDEALEAKEEFERLNKQLRAemEDLISS 1560
Cdd:COG4913 755 FAAalgdavERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadLDADLESLPEYLALLDRLEE--DGLPEY 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1561 KDDVGKNVHELEKSKRT-----LEQQVEEMRTQLEELEDELQATE---DAKLRLEVNMQ--AMKAQFDRDLQA------- 1623
Cdd:COG4913 833 EERFKELLNENSIEFVAdllskLRRAIREIKERIDPLNDSLKRIPfgpGRYLRLEARPRpdPEVREFRQELRAvtsgasl 912
|
650 660 670
....*....|....*....|....*....|...
gi 688558683 1624 RDEQNEEKKRALVKQVREMEAELEDERKQRALA 1656
Cdd:COG4913 913 FDEELSEARFAALKRLIERLRSEEEESDRRWRA 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1490 |
5.94e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 890 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLE 969
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 970 SRVEEEEERNQSLQN--EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEdillledqnSKFLKEKKLLED 1047
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA---------KKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1048 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKldaETTDLQDQIAELQAQIDELKIQ-- 1125
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEev 1597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1126 --LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRdlSEELEALKTELEdtldtt 1203
Cdd:PTZ00121 1598 mkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE------ 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1204 aAQQELRSKREQEvaELKKAIDDETRNHESQIQEmrqrhgtalEEISEQLEQAKrvKGNLEKNKQTLESDNKELTNEVKS 1283
Cdd:PTZ00121 1667 -AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE---------AEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKA 1732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1284 LQQAKSESEHKRKKLEAQLQE------VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQ 1357
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1358 --------LQDTQELLQEETRQKLNLSSriRQLEEEKNNLLEQQEEEEESRKNLEKqlatlQAQLVETKKKLEDDVGALE 1429
Cdd:PTZ00121 1813 ggkegnlvINDSKEMEDSAIKEVADSKN--MQLEEADAFEKHKFNKNNENGEDGNK-----EADFNKEKDLKEDDEEEIE 1885
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1430 GLEEVKRKLQKDMEV----TSQKLEEKAIAFDKLEKTKNRLQqelddlmvDLDHQRQIVSNLEKK 1490
Cdd:PTZ00121 1886 EADEIEKIDKDDIEReipnNNMAGKNNDIIDDKLDKDEYIKR--------DAEETREEIIKISKK 1942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
893-1608 |
6.38e-16 |
|
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: 84.40 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 893 EEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRARLVAKK---QELEEILHDLE 969
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEgvlQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 970 srveeeeernqslQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQNSKFLKEKK-----L 1044
Cdd:pfam15921 198 -------------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkielL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1045 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK-EEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELK 1123
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQL----SDLESTVSQLRSELREAK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1124 IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTT 1203
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1204 AAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISE---QLEQAK----RVKGNLEKNKQTLESDNKE 1276
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltaQLESTKemlrKVVEELTAKKMTLESSERT 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1277 LTNEVKSLQQAK-------SESEHKRKKLEAQLQEVMARFSEG----------EKVKGELADRTHKIQ---TELDNVSCL 1336
Cdd:pfam15921 498 VSDLTASLQEKEraieatnAEITKLRSRVDLKLQELQHLKNEGdhlrnvqtecEALKLQMAEKDKVIEilrQQIENMTQL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1337 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeeESRKNLEK-QLATLQAQLV 1415
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR------------VSDLELEKvKLVNAGSERL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1416 ETKKKLEDDVGALegLEEVK------RKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1489
Cdd:pfam15921 646 RAVKDIKQERDQL--LNEVKtsrnelNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1490 KQ-KKFDQMLAEEKTISARyaeerdRAEAEAREKDTKAL--SMARALDEALEAKEEFERLNKqlraEMEDLISSKDDVGK 1566
Cdd:pfam15921 721 SDgHAMKVAMGMQKQITAK------RGQIDALQSKIQFLeeAMTNANKEKHFLKEEKNKLSQ----ELSTVATEKNKMAG 790
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 688558683 1567 NVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLEV 1608
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
891-1730 |
6.45e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 84.33 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 891 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNIlAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLES 970
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 971 RVEEEEERNQSLQ----------NEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1040
Cdd:TIGR00606 277 RKKQMEKDNSELElkmekvfqgtDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1041 E-------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIA 1113
Cdd:TIGR00606 357 DrhqehirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1114 ELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAEL--------------------QEDLESEKA 1173
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskaeknsltetlkkevkslqNEKADLDRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1174 ARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL---------KKAIDDETRNHESQIQEMRQRHGT 1244
Cdd:TIGR00606 517 LRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1245 ALEEIsEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE---------AQLQEVMARFSEGEKV 1315
Cdd:TIGR00606 596 LNKEL-ASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEksskqramlAGATAVYSQFITQLTD 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1316 KGE----LADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLL 1390
Cdd:TIGR00606 675 ENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEkRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1391 EQQEEEEESRKNL---EKQLATLQAQLvETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLE--EKAIAFDKLEKTKNR 1465
Cdd:TIGR00606 755 KVNRDIQRLKNDIeeqETLLGTIMPEE-ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQE 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1466 LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEA---EAREKDTKALSMARALDEALEAKEE 1542
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQDSP 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1543 FERLNKQLRAEMEDLISSKDDVGKNVH-ELEKSKRTLEQQVEEMRTQLEELEDelqATEDAKLRLEVNMQAMKAQFdrdl 1621
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL---- 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1622 qardEQNEEKKRALVKQVREMEAELEDERKQRALAV--AAKKKLEMDLKDVEAQIeaanKARDEAIKQLRKLQaQMKDYQ 1699
Cdd:TIGR00606 987 ----EECEKHQEKINEDMRLMRQDIDTQKIQERWLQdnLTLRKRENELKEVEEEL----KQHLKEMGQMQVLQ-MKQEHQ 1057
|
890 900 910
....*....|....*....|....*....|....
gi 688558683 1700 RELEEARTSRDE---IFTQSKENEKKLKSLEAEI 1730
Cdd:TIGR00606 1058 KLEENIDLIKRNhvlALGRQKGYEKEIKHFKKEL 1091
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
869-1567 |
7.51e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 7.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 869 KLRHWQWWRLFTKVKPLLQVTRQ---EEEMQAKDEELIKVKERQVKVENELVEMERKhqqlLEEKNILAEQLQAETELFA 945
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 946 EAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQ-NEKKKMQSHIQDLEEQLDEEEAARQ-----KLQLEKVTAEA 1019
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKKKEEAKKKADAAKKKaeekkKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1020 KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvKNKQEMMMVDLEERLKKEEKTRQELEKAKR 1099
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1100 KLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAE 1179
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1180 KLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAlEEISEQLEQAKRV 1259
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKV 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1260 ----KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRthkiqteldnvsc 1335
Cdd:PTZ00121 1636 eqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKK------------- 1696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1336 llEDAEKKGIKLTKdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnLLEQQEEEEESRKNLEKQLATLQAQLV 1415
Cdd:PTZ00121 1697 --EAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK--KKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1416 ETKKKLEDDVgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ-KKF 1494
Cdd:PTZ00121 1771 EEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEaDAF 1849
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558683 1495 DQMLAEEKTISaryAEERDRAEAEAREKDTKalsmaRALDEALEAKEEFERLNKQlraEMEDLISSKDDVGKN 1567
Cdd:PTZ00121 1850 EKHKFNKNNEN---GEDGNKEADFNKEKDLK-----EDDEEEIEEADEIEKIDKD---DIEREIPNNNMAGKN 1911
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1247-1966 |
9.51e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1247 EEISEQLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmARFSEGEKVKGELADRT 1323
Cdd:PTZ00121 1053 DGNHEGKAEAKAHVGQDEGLKPSYkdfDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1324 HKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNL 1403
Cdd:PTZ00121 1131 EEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1404 EKQLATLQAQLVETKKKLEddvgALEGLEEVKRKlqkdmevtsqklEEKAiafDKLEKTKNRLQ-QELDDLMVDLDHQRQ 1482
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAE----AVKKAEEAKKD------------AEEA---KKAEEERNNEEiRKFEEARMAHFARRQ 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1483 IVSNLEKKQKKFDQMLAEE--KTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISS 1560
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEkkKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1561 KDDVGKNVHELEKSKR---TLEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKaQFDRDLQARDEQNEEKKRA 1634
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEkaeAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKA 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1635 L-VKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIF 1713
Cdd:PTZ00121 1428 EeKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1714 TQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE---LADEISNSASGKAAllDEKRRLEARIAQLEEELEEEQ 1790
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekkKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1791 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLE--RQNKDLKSKLQEL----EGSVKSKFKASIAALEAKI 1864
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLkkkeAEEKKKAEELKKAEEENKI 1661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1865 LQLEEQLEQEAKERAAAN-KIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeAEEEATRANASRRK 1943
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKE 1738
|
730 740
....*....|....*....|....*
gi 688558683 1944 LQRELDDATEA--SEGLSREVNTLK 1966
Cdd:PTZ00121 1739 AEEDKKKAEEAkkDEEEKKKIAHLK 1763
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1332-1851 |
1.02e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.57 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1332 NVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQeetrqklNLSSRIRQLEEEKNNLLEQQEEEEEsrknLEKQLATLQ 1411
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELE-------KLEKEVKELEELKEEIEELEKELES----LEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1412 AQLVETKKKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ 1491
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1492 KKFDQMLAEEKTISARYAEERDRAEAeaREKDTKALSMARALdealeaKEEFERLNKQLRAEmedlisSKDDVGKNVHEL 1571
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAK------KEELERLKKRLTGL------TPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1572 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFDRDLQARDEQNEEKKRALvkqvREMEAELEDERK 1651
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL----EEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1652 QRALAVAAKKKLEMDLKDVEAQIEAANKAR--DEAIKQLRKLQAQMKDYQRE-LEEARTSRDEIFTQSKENEKKLKSLEA 1728
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1729 EILQLQE---DLASSERARRHAEQERDELADEISNSASGKAALLDEK---------------------RRLEARIAQLEE 1784
Cdd:PRK03918 547 ELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaekelEREEKELKKLEE 626
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1785 ELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSaaQKSENARQQLERQNKDLKSKLQELEGSVKS 1851
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
906-1734 |
2.21e-15 |
|
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: 82.47 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 906 KERQVKVENELVEMERKHQQLLEEKNILAEQlqaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNE 985
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEK---------QKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 986 KKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDilLLEDQNSKFLKEKKLL---EDRVGEMTSQLAEEEEK 1062
Cdd:pfam15921 144 RNQLQNTVH----------------ELEAA------KCLKED--MLEDSNTQIEQLRKMMlshEGVLQEIRSILVDFEEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1063 AKNlgKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI-DELKIQLAKKEEELQAVLARGD 1141
Cdd:pfam15921 200 SGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1142 EEVA----QKNNALKQLRELQAQLAELQEDlesekaARNKAEKLKRDLSE----------ELEALKTELEDTLDTTAAQQ 1207
Cdd:pfam15921 278 VEITglteKASSARSQANSIQSQLEIIQEQ------ARNQNSMYMRQLSDlestvsqlrsELREAKRMYEDKIEELEKQL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1208 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQA 1287
Cdd:pfam15921 352 VLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1288 KSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL---TKDVSSLESQLQDTQEL 1364
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLessERTVSDLTASLQEKERA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1365 LQEETRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEV 1444
Cdd:pfam15921 512 IEATNAEITKLRSRV----DLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI---LRQQIENMTQLVGQHGRT 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1445 TSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfDQMLAEEKTISAryAEERDRAEAEAREKDT 1524
Cdd:pfam15921 585 AGAMQVEKA----QLEKEINDRRLELQEFKILKDKKDAKIRELEARVS--DLELEKVKLVNA--GSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1525 KALSMARALDEALEA-KEEFERLNKQLRAEMEdlisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1603
Cdd:pfam15921 657 QLLNEVKTSRNELNSlSEDYEVLKRNFRNKSE--------------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1604 ---LRLEVNMQ----AMKAQFDrdlqardeqneekkrALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQiea 1676
Cdd:pfam15921 723 ghaMKVAMGMQkqitAKRGQID---------------ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE--- 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1677 ankaRDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQ 1734
Cdd:pfam15921 785 ----KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1404-1971 |
3.76e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1404 EKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafdklEKtknrlQQELDDLMVDLDHQRQI 1483
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------ER-----REELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1484 VSNLEKKQKKFDQMLAEEKTISARYAEERD--RAEAEAREKDTKALSMARaldEALEAKEEferlnkQLRAEMEDLISSK 1561
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARR---EELEDRDE------ELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1562 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdRDLQARDEQNEEKKRALVKQVRE 1641
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV---------------EDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1642 MEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAikqlRKLQAQMK--DYQRELEEArtsrdEIFTQSKEN 1719
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA----EALLEAGKcpECGQPVEGS-----PHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1720 EKKLKSLEAEILQLQEDLASSErarrhaeqERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDR 1799
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1800 frkttmqVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfkASIAALEAKILqleeqleqeakerA 1879
Cdd:PRK02224 546 -------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIA-------------D 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1880 AANKIVRRTEKKlkEVFMQVEDERRhadqykEQMEKANSRMKQLKRQ-----LEEAEEEATRANASRRKLQRELDDATEA 1954
Cdd:PRK02224 604 AEDEIERLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
570
....*....|....*..
gi 688558683 1955 SEGLSREVNTLKNRLRR 1971
Cdd:PRK02224 676 RDDLQAEIGAVENELEE 692
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1166-1896 |
7.54e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1166 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQrhgta 1245
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----- 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1246 lEEISEQLEQAKRVkgnlEKNKQTLESDNKEltnEVKSLQQAKSESEHKRKKLEAQLQEVmaRFSEGEKvKGELADRTHK 1325
Cdd:PTZ00121 1166 -AEEARKAEDAKKA----EAARKAEEVRKAE---ELRKAEDARKAEAARKAEEERKAEEA--RKAEDAK-KAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1326 IQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEK 1405
Cdd:PTZ00121 1235 AKKDAEEAK--KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1406 QlATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQElddlmvdldhqrQIVS 1485
Cdd:PTZ00121 1310 K-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA---DEAEAAEEKAEAA------------EKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1486 NLEKKQKKFDQMLAEEKtisaRYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVG 1565
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEK----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1566 KNVHELEKSKRTLEQQVEEMRT--QLEELEDELQATEDAKLRLEVNMQamKAQFDRDLQARDEQNEEKKRALVKQVREME 1643
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1644 AELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1723
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1724 KSLEA----EILQLQEDLASSERARRHAEQERDELADEISNS---------ASGKAALLDEKRRLEARIAQLEEELEEEQ 1790
Cdd:PTZ00121 1608 KAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1791 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQ---KSENAR----QQLERQNKDLKSKLQEL--EGSVKSKFKASIAALE 1861
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENkikaEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEE 1767
|
730 740 750
....*....|....*....|....*....|....*..
gi 688558683 1862 AKILQLEEQLEQEAKERAAANKIVRR--TEKKLKEVF 1896
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRmeVDKKIKDIF 1804
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1155-1864 |
1.29e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1155 RELQAQLAELQEDLESEKAARNKAEKLKR--DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaiDDETRNHE 1232
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR---LELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1233 SQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE-LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1311
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1312 GEKvkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlle 1391
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL--------- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1392 qqeeeeesRKNLEKQLATLQAQ------LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNR 1465
Cdd:COG4913 446 --------RDALAEALGLDEAElpfvgeLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1466 LQqelddlmVDLDHqrqivsnLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFE 1544
Cdd:COG4913 512 GR-------LVYER-------VRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1545 RLNKQLRAEmeDLISSkddvGKNVHELEKSKRTLEQQV--EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQ 1622
Cdd:COG4913 572 RHPRAITRA--GQVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEA--------LE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1623 ARDEQNEEKKRALVKQVREMEAELEDERKQRALAvaakkklemdlkDVEAQIEAANKARDEaikqLRKLQAQMKDYQREL 1702
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEIDVASAEREIA------------ELEAELERLDASSDD----LAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1703 EEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQL 1782
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1783 EEELEEEQSNMELLNDRFRKT-TMQVDTLNTELAGERSAAQKsenaRQQLERQnkDLKSKLQELEGSVKSKFKASIAALE 1861
Cdd:COG4913 779 RARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEED--GLPEYEERFKELLNENSIEFVADLL 852
|
...
gi 688558683 1862 AKI 1864
Cdd:COG4913 853 SKL 855
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
900-1575 |
1.75e-14 |
|
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: 79.38 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 900 EELIKVKERQVKVENELVEMERKHQqllEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHD----------LE 969
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 970 SRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIK-KMEEDILLLEDQNSKFLKEKKLLEDR 1048
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1049 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTD----LQDQIAELQAQIDELKI 1124
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1125 ------QLAKKEE----ELQAVLARGDEEVAQKNNALKQLREL-----------QAQLAELQEDLESEKAARNKAEKLKR 1183
Cdd:pfam05483 322 atkticQLTEEKEaqmeELNKAKAAHSFVVTEFEATTCSLEELlrteqqrleknEDQLKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1184 DLSEELEALKT---ELEDTLDTTAAQQELRSK---REQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISEQLE 1254
Cdd:pfam05483 402 NKEVELEELKKilaEDEKLLDEKKQFEKIAEElkgKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1255 QAKRVKGNLEKNKQTLESDNKELTNE----VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1330
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1331 DNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1410
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKL 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1411 QAQLVETKKKLEDDVGALEGLEEVKRklqkdmeVTSQKLEEKAIAFDKLEKTKNRLQQELDdlmVDLDHQ-RQIVSNLEK 1489
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDKK-------ISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKiAEMVALMEK 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1490 KQKKFDQMLaeektisaryaEERDRAEAEAREKDTKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNV 1568
Cdd:pfam05483 712 HKHQYDKII-----------EERDSELGLYKNKEQEQSSAKAALEIELSnIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
....*..
gi 688558683 1569 HELEKSK 1575
Cdd:pfam05483 781 AILKDKK 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
885-1470 |
1.87e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 885 LLQVTRQEEEMQAKDeelikVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLvakkQELEEI 964
Cdd:PRK02224 189 LDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 965 LHDLESRVEEEEERNQSLQNEkkkmqshIQDLEeqldeeeAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1044
Cdd:PRK02224 260 IEDLRETIAETEREREELAEE-------VRDLR-------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1045 LEDRVGEMTSQLAEEEEKAKNLGKvknkqemMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1124
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1125 QLAKKEEELQAVLARGDEEVAQKNnalkqlrELQAQLAELQEDLESEKAARNKAEKLKR-----------------DLSE 1187
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERD-------ELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsphvETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1188 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID--DETRNHESQIQEMRQRHGTALEEISEQLEQakrvkgnLEK 1265
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEE-------LRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1266 NKQTLEsdnkeltnevkslqqakSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTeLDNVSCLLEDAEKKGi 1345
Cdd:PRK02224 545 RAAELE-----------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1346 kltKDVSSLESQLQDTQElLQEETRQKL-NLSSRIRQLEEEknNLLEQQEEEEESRKNLEKQLATLQ---AQLVETKKKL 1421
Cdd:PRK02224 606 ---DEIERLREKREALAE-LNDERRERLaEKRERKRELEAE--FDEARIEEAREDKERAEEYLEQVEeklDELREERDDL 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 688558683 1422 EDDVGALEG----LEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQQEL 1470
Cdd:PRK02224 680 QAEIGAVENeleeLEELRERR-EALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
885-1633 |
3.93e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.47 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 885 LLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQqlleeknilaEQLQAETELFAEAEEMRARLVAKKQELEEI 964
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE----------KELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 965 LHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1044
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1045 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1124
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1125 QLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA 1204
Cdd:pfam02463 518 DGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1205 AQQELRSKREQEVAELKKAIDDETRNHES---QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1281
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEgilKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1282 KSLQQAKSESE----HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQ 1357
Cdd:pfam02463 678 IQELQEKAESElakeEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1358 LQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLvETKKKLEDDVGALEGLEEVKRK 1437
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA-ELLEEEQLLIEQEEKIKEEELE 836
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1438 LQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEA 1517
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEELLQELL-----LKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1518 EAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQ 1597
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-------EEEERNKRLLLAKEELGKVNLMAIEEFE 984
|
730 740 750
....*....|....*....|....*....|....*.
gi 688558683 1598 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKR 1633
Cdd:pfam02463 985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
848-1500 |
4.22e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.47 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 848 AKKQQQLSALKVLqRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELiKVKERQVKVENELVEMERKHQQLL 927
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-RAQEAVLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 928 EEKNILAEQLQaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAAR 1007
Cdd:TIGR00618 297 AHIKAVTQIEQ-------QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1008 QKLQleKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKE 1087
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1088 EKTRQ-------ELEKAKRKLDAETTDLQDQ-----------------IAELQAQIDELKIQLAKKEEELQAV------- 1136
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKeqihlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1137 --LARGDEEVAQKNNALK----QLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR 1210
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1211 SK-----REQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQL------EQAKRVKGNLEKNKQTLESDNKELTN 1279
Cdd:TIGR00618 608 DMlaceqHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrEHALSIRVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1280 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvSSLESQLQ 1359
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA-RTEAHFNN 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1360 DTQELLQEETRQKL-----NLSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLvetKKKLEDDVGALEGLEEv 1434
Cdd:TIGR00618 767 NEEVTAALQTGAELshlaaEIQFFNRLREE------------------DTHLLKTLEAEI---GQEIPSDEDILNLQCE- 824
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1435 krKLQKDMEVTSQKLEEkaiafdklektKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1500
Cdd:TIGR00618 825 --TLVQEEEQFLSRLEE-----------KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1247-1915 |
4.70e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 77.75 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1247 EEISEQLEQAKRVKGNLEKNKQ---TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegEKVKGELADRT 1323
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDkinKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKEN-------KKNIDKFLTEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1324 HKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLS---SRIRQLEEEKNNLLEQQEEEEESR 1400
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1401 KNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL--MVDLD 1478
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1479 HQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEME 1555
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1556 DLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQatedaKLRLEVNmqamkaqfdrDLQARDEQNEEKKRAL 1635
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE-----RLKETII----------KNNSEIKDLTNQDSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1636 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1715
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1716 SKENEKKLKSLEAEILQLQEDLASSErarrhAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1795
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKEN-----LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1796 -------LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkSKFKASIAALE--AKILQ 1866
Cdd:TIGR04523 608 kekkissLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII----KKIKESKTKIDdiIELMK 683
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558683 1867 LEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEK 1915
Cdd:TIGR04523 684 DWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELEN 732
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
922-1671 |
7.70e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 77.32 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 922 KHQQLLEEKNILAEQLQAETELfaeAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQshiqdleeqld 1001
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLC---TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1002 eeeaARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFlkekklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLE 1081
Cdd:TIGR00618 254 ----EQLKKQQLLKQLRARIEELRAQEAVLEETQERI------------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1082 ERLKKEEKTRQELEKAKrKLDAETTDLQDQIAELQAQIDELKIQ-----LAKKEEELQAVLARGDEEVAQKNNALKQLRE 1156
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQEIHIRDAhevatSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1157 LQAQLAELQEDLESEKAARNKAEklkRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQ 1236
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1237 EMRQrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1316
Cdd:TIGR00618 474 QLQT-----KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1317 GELADRTHKIQTELDNVSCLLEDAEKKGIK---LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQ 1393
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCdnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1394 EEEEESRkNLEKQLATLQAQLVETKKKLEDdvgaleglEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1473
Cdd:TIGR00618 629 DVRLHLQ-QCSQELALKLTALHALQLTLTQ--------ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1474 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAE 1553
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1554 MEDLISskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLqardeqneEKKR 1633
Cdd:TIGR00618 780 LSHLAA----------EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKS 841
|
730 740 750
....*....|....*....|....*....|....*...
gi 688558683 1634 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVE 1671
Cdd:TIGR00618 842 ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1418-1781 |
2.56e-13 |
|
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: 75.87 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1418 KKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqivsnlekkqkkfdqm 1497
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----------------------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1498 laeektisaRYAEERDRAEaearekDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1577
Cdd:TIGR02169 212 ---------RYQALLKEKR------EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1578 LEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1649
Cdd:TIGR02169 277 LNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1650 RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN-------EKK 1722
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlNAA 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1723 LKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQ 1781
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1615-1959 |
4.47e-13 |
|
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: 75.10 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1615 AQFDRDLQ------ARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLE--------MDLKDVEAQIEAANKA 1680
Cdd:TIGR02169 166 AEFDRKKEkaleelEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyellKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1681 RDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSK---ENE-----KKLKSLEAEILQLQEDLASSERARRHAEQERD 1752
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgEEEqlrvkEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1753 ELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLE 1832
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1833 RQNKDLKSKLQELEGSVkSKFKASIAALEAKILQLEEQLEQEAKEraaankiVRRTEKKLKEVFMQVEDERRHADQYKEQ 1912
Cdd:TIGR02169 406 RELDRLQEELQRLSEEL-ADLNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 688558683 1913 MEKANSRMKQLKRQLEeaeeeatRANASRRKLQRELDDATEASEGLS 1959
Cdd:TIGR02169 478 YDRVEKELSKLQRELA-------EAEAQARASEERVRGGRAVEEVLK 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1104-1763 |
5.36e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1104 ETTDLQDQIAELQAQIDELkiqlakkeEELQAVLargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK-----A 1178
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1179 EKLKRDLSEELEALKTELEDTldttaaqqelrskrEQEVAELKKAIdDETRNHESQIQEMRQRHGTaleeisEQLEQAKR 1258
Cdd:COG4913 287 QRRLELLEAELEELRAELARL--------------EAELERLEARL-DALREELDELEAQIRGNGG------DRLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1259 vkgnleknkqtlesdnkeltnEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvkgELADRTHKIQTELDNVSCLLE 1338
Cdd:COG4913 346 ---------------------EIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1339 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlleqqeeeeesRKNLEKQLATLQAQ----- 1413
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-----------------RDALAEALGLDEAElpfvg 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1414 -LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNRLQqelddlmVDLDHqrqivsnLEKKQK 1492
Cdd:COG4913 465 eLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLRGR-------LVYER-------VRTGLP 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1493 KFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFERLNKQLRAemEDLISSKDDVG-KNVHE 1570
Cdd:COG4913 525 DPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELRRHPRAITR--AGQVKGNGTRHeKDDRR 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1571 LEKSKRTL----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdLQARDEQNEEKKRalVKQVREMEAEL 1646
Cdd:COG4913 597 RIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDEID--VASAEREIAEL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1647 EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftQSKENEKKLKSL 1726
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALL 751
|
650 660 670
....*....|....*....|....*....|....*..
gi 688558683 1727 EAEILQLQEDlASSERARRHAEQERDELADEISNSAS 1763
Cdd:COG4913 752 EERFAAALGD-AVERELRENLEERIDALRARLNRAEE 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1246-1900 |
9.04e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.52 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1246 LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA---RFSEGEKVKGELadr 1322
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSdlsKINSEIKNDKEQ--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1323 THKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1402
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1403 LEKQLATLQAqLVETKKKLEDDvgaLEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDlmvdldhQRQ 1482
Cdd:TIGR04523 199 LELLLSNLKK-KIQKNKSLESQ---ISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDE-------QNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1483 IVSNLEKKQKKFDQmlAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRaEMEDLISSKD 1562
Cdd:TIGR04523 265 IKKQLSEKQKELEQ--NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS-QNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1563 DVgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREM 1642
Cdd:TIGR04523 342 EQ---ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1643 EAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKK 1722
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1723 LKSLEAEILQLqedlasserarrhaEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEeleeeqsnmELLNDRFRK 1802
Cdd:TIGR04523 498 LKKLNEEKKEL--------------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED---------ELNKDDFEL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1803 TTmqvDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAAN 1882
Cdd:TIGR04523 555 KK---ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
650
....*....|....*...
gi 688558683 1883 KIVRRTEKKLKEVFMQVE 1900
Cdd:TIGR04523 631 SIIKNIKSKKNKLKQEVK 648
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1055-1781 |
1.73e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.06 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1055 QLAEEEEK----AKNLGKVKNKQEMMMVDLE---ERL----------KKEEKTRQELEKAKRKLDAET---TDLQDQIAE 1114
Cdd:COG3096 300 QLAEEQYRlvemARELEELSARESDLEQDYQaasDHLnlvqtalrqqEKIERYQEDLEELTERLEEQEevvEEAAEQLAE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1115 LQAQ-------IDELKIQLAKKEEEL-----------QAVLARGDEEVAQKNNAL--KQLRELQAQL-AELQEDLESEKA 1173
Cdd:COG3096 380 AEARleaaeeeVDSLKSQLADYQQALdvqqtraiqyqQAVQALEKARALCGLPDLtpENAEDYLAAFrAKEQQATEEVLE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1174 ARNK---AEKLKRDLSEELEALK-----TELEDTLDTtaAQQELRSKREQE-----VAELKKAIDDETRNHESQIQEMRQ 1240
Cdd:COG3096 460 LEQKlsvADAARRQFEKAYELVCkiageVERSQAWQT--ARELLRRYRSQQalaqrLQQLRAQLAELEQRLRQQQNAERL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1241 rhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfsegEKVKGELA 1320
Cdd:COG3096 538 -----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR----APAWLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1321 DRTHKIQTEldnVSCLLEDAekkgikltkdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR 1400
Cdd:COG3096 609 DALERLREQ---SGEALADS-----------QEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRL 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1401 KNLEKQL-ATLQAQLVEtKKKLEDD--VGALEG----------LEEVKRKLQkDMEVTSQKL---EEKAIAFDKlektKN 1464
Cdd:COG3096 675 LALAERLgGVLLSEIYD-DVTLEDApyFSALYGparhaivvpdLSAVKEQLA-GLEDCPEDLyliEGDPDSFDD----SV 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1465 RLQQELDDLMVDLDHQRQI-VSNLEK--------KQKKFDQMLAEEKTISARYAEER------DRAEAEAREKDTKALSM 1529
Cdd:COG3096 749 FDAEELEDAVVVKLSDRQWrYSRFPEvplfgraaREKRLEELRAERDELAEQYAKASfdvqklQRLHQAFSQFVGGHLAV 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1530 ARALDEALEAKE------EFERLNKQLRAEMEDLISSKDDVGKNVHELEK--------SKRTLEQQVEEMRTQLEELED- 1594
Cdd:COG3096 829 AFAPDPEAELAAlrqrrsELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllADETLADRLEELREELDAAQEa 908
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1595 --ELQATEDAKLRLEVNMQAMK---AQFDRdLQARDEQNEEKKRALVKQVREMEaeledERKQRALAVAAKKKLEM---- 1665
Cdd:COG3096 909 qaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----EVVQRRPHFSYEDAVGLlgen 982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1666 -DLKD-VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEaeilqLQEDLASSERA 1743
Cdd:COG3096 983 sDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG-----VQADAEAEERA 1057
|
810 820 830
....*....|....*....|....*....|....*...
gi 688558683 1744 RrhaeQERDELADEISNSASGKAALLDEKRRLEARIAQ 1781
Cdd:COG3096 1058 R----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1403-1950 |
1.94e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1403 LEKQLATLQaQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIafDKLEKTKNRLQQELDDLMVDLDHQRQ 1482
Cdd:COG4913 247 AREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1483 IVSNLEKkqkkfdQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLI 1558
Cdd:COG4913 324 ELDELEA------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1559 SSKDDVGKNVHELEKSKRTLEQQveemrtqLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQneekkralVK- 1637
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE--------LPf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1638 -----QVREMEAE-----------------LEDERKQRALAVAAKKKLEMDL-------KDVEAQIEAA----------- 1677
Cdd:COG4913 463 vgeliEVRPEEERwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRLvyervrtGLPDPERPRLdpdslagkldf 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1678 --NKARDEAIKQLRKL--------QAQMKDYQREL---------EEARTSRDEIFTQSK-----ENEKKLKSLEAEILQL 1733
Cdd:COG4913 543 kpHPFRAWLEAELGRRfdyvcvdsPEELRRHPRAItragqvkgnGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1734 QEDLASSERARRHAEQERDELAD---------EISNSASGKAALLDEKRRLEARIAQleeeleeeqsnMELLNDRFRKTT 1804
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELER-----------LDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1805 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKI 1884
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-----------DRLEAAEDLARLELRALLEERFAAALG 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1885 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKAnsrMKQLKRQLEEAEEEATRANASRRKLQRELDD 1950
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDR 823
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1084-1757 |
2.14e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.69 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1084 LKKEEKTRQELEKAKRKLDAET---TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQ 1160
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTqlaLMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1161 LAELQEDLESEKAARNKAEKLKRDLS------EELEALKTELEDT-------------LDTTAAQQELRSKREQEVAELK 1221
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKqlrariEELRAQEAVLEETqerinrarkaaplAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1222 KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE----LTNEVKSLQQAKSESEHKRK- 1296
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCqqhtLTQHIHTLQQQKTTLTQKLQs 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1297 ------KLEAQLQEVMARFSEGEKVKGELADRTHKIQTELD----------NVSCLLEDAEKKGIKLTKDVSSLESQLQD 1360
Cdd:TIGR00618 398 lckeldILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRyaelcaaaitCTAQCEKLEKIHLQESAQSLKEREQQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1361 TQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLAT--LQAQLVETKKKLEDDVGALEGLEEVKRK- 1437
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVYHQLTSERKq 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1438 ---LQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDR 1514
Cdd:TIGR00618 558 rasLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1515 AEAEAREKDTKAlsmARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHE-LEKSKRTLEQQVEEMRTQLEELE 1593
Cdd:TIGR00618 638 SQELALKLTALH---ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIE 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1594 delqatEDAKLRLEVNMQAMKAQfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQ 1673
Cdd:TIGR00618 715 ------EYDREFNEIENASSSLG--SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1674 IEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEK----KLKSLEAEILQLQEDLASSERARRHAEQ 1749
Cdd:TIGR00618 787 IQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
....*...
gi 688558683 1750 ERDELADE 1757
Cdd:TIGR00618 867 EQAKIIQL 874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1402-1970 |
8.33e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 8.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1402 NLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLmvdlDHQR 1481
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1482 QIVSNLEKKQKKFDQmlaEEKTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKqlraEMEDLISSK 1561
Cdd:PRK03918 238 EEIEELEKELESLEG---SKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSE----FYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1562 DDVGKNVHELEKSKRTLEQQV---EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqFDRDLQARDEQNEEKKRALVKQ 1638
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1639 VREMEAELEDERKqralavaAKKKLEMDLKDVEAQI---EAANKARDEAIKQLRKLQAQMKDYQRELEEARtsRDEIFtq 1715
Cdd:PRK03918 386 PEKLEKELEELEK-------AKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKCPVCGRELTEEH--RKELL-- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1716 sKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsgkaaLLDEKRRLEARIAQLEEELEEEQSN-ME 1794
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLEELEKKAEeYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1795 LLNDRFRKTTMQVDTLNTELagerSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLeqe 1874
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY--- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1875 aKERAAANKIVRRTEKKLKEVfmqvEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEAT-----RANASRRKLQRELD 1949
Cdd:PRK03918 602 -NEYLELKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeELREEYLELSRELA 676
|
570 580
....*....|....*....|.
gi 688558683 1950 DATEASEGLSREVNTLKNRLR 1970
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLE 697
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1051-1779 |
1.11e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 70.37 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1051 EMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL--QDQIAELQAQIDELKIQLak 1128
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqQEKIERYQADLEELEERL-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1129 keEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESE----------KAARNKAEKLKRD-------LSE 1187
Cdd:PRK04863 365 --EEQNEVVEEADEQQeeneARAEAAEEEVDELKSQLADYQQALDVQqtraiqyqqaVQALERAKQLCGLpdltadnAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1188 ELEALKTELED-TLDTTAAQQELRSK---REQ--EVAELKKAIDDET-------------------RNHESQIQEMRQRH 1242
Cdd:PRK04863 443 WLEEFQAKEQEaTEELLSLEQKLSVAqaaHSQfeQAYQLVRKIAGEVsrseawdvarellrrlreqRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1243 GTALEEISEQ------LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvk 1316
Cdd:PRK04863 523 SELEQRLRQQqraerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA-- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1317 geLADRTHKIQTELDNVSclledaEKKGIKLTkDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNnlleqqeee 1396
Cdd:PRK04863 601 --RAPAWLAAQDALARLR------EQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE--------- 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1397 eesrknlekQLATLQAQLVETKKKLEDDVGAL---EGLEEVkrKLQkDMEVTSQKLEE--KAIAFDKLEKTKNRLQQE-- 1469
Cdd:PRK04863 663 ---------RLSQPGGSEDPRLNALAERFGGVllsEIYDDV--SLE-DAPYFSALYGParHAIVVPDLSDAAEQLAGLed 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1470 -LDDLMV---DLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErDRAEAEAREKDTKALSMARALDEALEAKEEF-- 1543
Cdd:PRK04863 731 cPEDLYLiegDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEV-PLFGRAAREKRIEQLRAEREELAERYATLSFdv 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1544 ---ERLNKQLR----------------AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL--------------- 1589
Cdd:PRK04863 810 qklQRLHQAFSrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnllad 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1590 -------EELEDELQATEDAKL-------------RLEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMeaeleDE 1649
Cdd:PRK04863 890 etladrvEEIREQLDEAEEAKRfvqqhgnalaqlePIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TE 963
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1650 RKQRALAVAAKKKLEMDLKDVE------AQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1723
Cdd:PRK04863 964 VVQRRAHFSYEDAAEMLAKNSDlneklrQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1724 KSleaeiLQLQEDLASSERARRHaeqeRDELADEISNSASGKAALLDEKRRLEARI 1779
Cdd:PRK04863 1044 QD-----LGVPADSGAEERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1016-1809 |
1.17e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 70.46 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1016 TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM------MVDLEERLKKEEK 1089
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIehnlskIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1090 TRQELEKAKRKLDAETTDLQDQIAElqaQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLaELQEDLE 1169
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDE---QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL-LVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1170 SEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQevaeLKKAIDDETRNHESQIQEMRQRHGTALEEI 1249
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTL----VIERQEDEAKTAAQLCADLQSKERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1250 SEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEhKRKKLEAQLQEVMARFSegekvkgeLADRTHKIQTE 1329
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELRKAERELS--------KAEKNSLTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1330 LDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQL 1407
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmlTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1408 ATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDME-VTSQKLEEKAIAFDKLekTKNRLQQELDDLMVDLDHQRQIVSN 1486
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEsKEEQLSSYEDKLFDVC--GSQDEESDLERLKEEIEKSSKQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1487 LEKKQKKFDQMLAEEKTISARYAEERDR---AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSK-- 1561
Cdd:TIGR00606 658 LAGATAVYSQFITQLTDENQSCCPVCQRvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRqs 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1562 --DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQaTEDAKLRLEVNMQAMKAQFDRdLQARDEQNEekkralvKQV 1639
Cdd:TIGR00606 738 iiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKI 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1640 REMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIKQLRKLQA---QMKDYQRELEEARTSRDEIFT 1714
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQQVNQEKQEKQheLDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEE 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1715 QSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADeiSNSASGKAALL------------------------- 1769
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS--SKETSNKKAQDkvndikekvknihgymkdienkiqd 966
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 688558683 1770 ---DEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1809
Cdd:TIGR00606 967 gkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT 1009
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1198 |
1.53e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 847 FAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPL-LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQ 925
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 926 LLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeea 1005
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-------- 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1006 arqklqlekvtaeAKIKKMEEDILLLEDQnskflkekklledrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1085
Cdd:TIGR02168 845 -------------EQIEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1086 KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQK-NNALKQLRELQAQLAEL 1164
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRL 977
|
330 340 350
....*....|....*....|....*....|....
gi 688558683 1165 QEDLESEKAARNKAEKLKRDLSEELEALKTELED 1198
Cdd:TIGR02168 978 ENKIKELGPVNLAAIEEYEELKERYDFLTAQKED 1011
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1081-1974 |
1.68e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.98 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1081 EERLKKEEKT---RQELEKAKRKLDAEttdlQDQIAELQAQIDELKIQLAKKEEELQAvlarGDEEVAQKNNALKQLREL 1157
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQA----ASDHLNLVQTALRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1158 ---QAQLAELQEDLESEKAARnkaeklkrdlsEELEALKTELEDTLdtTAAQQELRSKREQeVAELKKAID-DETRNheS 1233
Cdd:COG3096 350 eryQEDLEELTERLEEQEEVV-----------EEAAEQLAEAEARL--EAAEEEVDSLKSQ-LADYQQALDvQQTRA--I 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1234 QIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegE 1313
Cdd:COG3096 414 QYQQAVQ----ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV-------C 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1314 KVKGELaDRthkiqteldnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEknnLLE 1391
Cdd:COG3096 483 KIAGEV-ER---------------SQAWQTARELLRRYRSQQALAQRLQQLRAQlaELEQRLRQQQNAERLLEE---FCQ 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1392 QQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVgalEGLEEVKRKLQkDMEVTSQKLEEKA----IAFDKLEKTKNRLQ 1467
Cdd:COG3096 544 RIGQQLDAAEELEELLAELEAQLEELEEQAAEAV---EQRSELRQQLE-QLRARIKELAARApawlAAQDALERLREQSG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1468 QELDDLmVDLDHQRQIVSNLEKKQKKFDQMLAEEKtisARYAEERDRAEAEAREKDTKALSMARAL----------DEAL 1537
Cdd:COG3096 620 EALADS-QEVTAAMQQLLEREREATVERDELAARK---QALESQIERLSQPGGAEDPRLLALAERLggvllseiydDVTL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1538 EAKEEFERLNKQLR---------------AEMED------LIS----SKDDVGKNVHELEK------SKRTL-------- 1578
Cdd:COG3096 696 EDAPYFSALYGPARhaivvpdlsavkeqlAGLEDcpedlyLIEgdpdSFDDSVFDAEELEDavvvklSDRQWrysrfpev 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1579 --------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDL-----QARDEQNEEKKRALVKQVREMEA 1644
Cdd:COG3096 776 plfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELER 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1645 ELED----ERKQRALAVAAKKKLEMdlkdVEAQIEAANKARDEAikqlrkLQAQMKDYQRELEEARTSRDEIFTQSK--- 1717
Cdd:COG3096 851 ELAQhraqEQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELDAAQEAQAFIQQHGKala 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1718 ENEKKLKSLEAEILQ---LQEDLASSERARRHAEQERDELADEISNSA----SGKAALLDEKRRLEARIAQLEEELEEEQ 1790
Cdd:COG3096 921 QLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEKLRARLEQAEEAR 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1791 SNmelLNDRFRKTTMQVDTLNTELAGERSAAQkseNARQQLerqnKDLKSKLQELEGSVKSkfkasiaaleakilqleeq 1870
Cdd:COG3096 1001 RE---AREQLRQAQAQYSQYNQVLASLKSSRD---AKQQTL----QELEQELEELGVQADA------------------- 1051
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1871 leqEAKERAAANKivrrtekklkevfmqvederrhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDD 1950
Cdd:COG3096 1052 ---EAEERARIRR-----------------------DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQ 1105
|
970 980 990
....*....|....*....|....*....|....
gi 688558683 1951 ATEASEG----------LSREvNTLKNRLRRGGP 1974
Cdd:COG3096 1106 EREQVVQakagwcavlrLARD-NDVERRLHRREL 1138
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1080-1862 |
1.89e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.87 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1080 LEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRE--- 1156
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSele 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1157 -LQAQL-AELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhesq 1234
Cdd:pfam12128 326 aLEDQHgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAK---- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1235 IQEMRQRHGTALEEISEQLEQAKRvkgnleknkQTLESDNKELTNEVKSLQQAKSEsehkrkkleAQLQEVMARFSEGEK 1314
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALESELR---------EQLEAGKLEFNEEEYRLKSRLGE---------LKLRLNQATATPELL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1315 VKGELAD-RTHKIQTELdnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqq 1393
Cdd:pfam12128 464 LQLENFDeRIERAREEQ-------EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ-------- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1394 eeeeesrknLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLektknRLQQelddl 1473
Cdd:pfam12128 529 ---------LFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKL-----DLKR----- 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1474 mvdLDHQRQIVSNlekkqkkfDQMLAEEKTISARYAEERDRAEAEarekdTKALSMARALDEALEAKEEFERlnkqlrae 1553
Cdd:pfam12128 590 ---IDVPEWAASE--------EELRERLDKAEEALQSAREKQAAA-----EEQLVQANGELEKASREETFAR-------- 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1554 mEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEledELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKR 1633
Cdd:pfam12128 646 -TALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE---RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1634 ALVKQVREMEAELEDERKQRALAVAAKkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIf 1713
Cdd:pfam12128 722 VVEGALDAQLALLKAAIAARRSGAKAE------LKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV- 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1714 TQSKENEKKLKSLEAEILQLQedlasSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNM 1793
Cdd:pfam12128 795 LRYFDWYQETWLQRRPRLATQ-----LSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM 869
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1794 ELLNdrfrktTMQVDTLNTELAGERSaaqksenarqQLERQNKDLKSKLQELEGSVKSK---FKASIAALEA 1862
Cdd:pfam12128 870 SKLA------TLKEDANSEQAQGSIG----------ERLAQLEDLKLKRDYLSESVKKYvehFKNVIADHSG 925
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
34-79 |
3.32e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 59.75 E-value: 3.32e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 688558683 34 TAKKLVWVPSERHGFEAASIREERGEEVLVELaENGKKAMVNKDDI 79
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1040-1258 |
3.71e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.10 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1040 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1119
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1120 DELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLeseKAARNKAEKLKRDLSEELEALKTELEDT 1199
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL---RADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1200 LDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKR 1258
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1079-1320 |
6.84e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1079 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvlargdeevaqknnALKQLRELQ 1158
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--------------LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1159 AQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhESQIQEM 1238
Cdd:COG4942 97 AELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1239 RQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG--EKVK 1316
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgfAALK 252
|
....
gi 688558683 1317 GELA 1320
Cdd:COG4942 253 GKLP 256
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1082-1753 |
6.95e-11 |
|
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: 67.44 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1082 ERLKK-EEKTRQELEKAKRKLDAETTDLQDQ---IAELQAQIDELKIQLakkEEELQAvlargDEEVAQKNNALKQ---- 1153
Cdd:pfam05483 88 EKIKKwKVSIEAELKQKENKLQENRKIIEAQrkaIQELQFENEKVSLKL---EEEIQE-----NKDLIKENNATRHlcnl 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1154 LRELQAQLAELQEDLESEkaaRNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKREQE---VAELKKAIDDETR 1229
Cdd:pfam05483 160 LKETCARSAEKTKKYEYE---REETRQVYMDLNNNIEKMILAFEElRVQAENARLEMHFKLKEDhekIQHLEEEYKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1230 NHESQI---------QEMRQRHGT-ALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE 1299
Cdd:pfam05483 237 DKEKQVsllliqiteKENKMKDLTfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1300 AQLQ---EVMARFSEGEKVKGELADRTHK----IQTELDNVSCLLED---AEKKGIKLTKD-VSSLESQLQDTQELLQEE 1368
Cdd:pfam05483 317 EDLQiatKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEEllrTEQQRLEKNEDqLKIITMELQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1369 TRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQ------LVETKKK----LEDDVGALEGLEEVKRKL 1438
Cdd:pfam05483 397 TKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKeqelifLLQAREKeihdLEIQLTAIKTSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1439 QKDMEVTSQKLEEKAIAF----DKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKfdqMLAEEKTISARYAEERDR 1514
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELtahcDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1515 AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELED 1594
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1595 ELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQI 1674
Cdd:pfam05483 630 QLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALM 709
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1675 EAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRdeiftqskenEKKLKSLEAEILQLQEDLASSERARRHAEQERDE 1753
Cdd:pfam05483 710 EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL----------EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
941-1672 |
7.07e-11 |
|
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: 67.44 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 941 TELFAEAEEMR-------ARLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQshiqdleeqldeeeaarqkLQLE 1013
Cdd:pfam05483 81 SKLYKEAEKIKkwkvsieAELKQKENKLQENRKIIEAQRKAI----QELQFENEKVS-------------------LKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1014 KVTAEAKikkmeeDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNL-GKVKNKQEMMMVDLEERLKKEEKTRQ 1092
Cdd:pfam05483 138 EEIQENK------DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVyMDLNNNIEKMILAFEELRVQAENARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1093 E----LEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQAQlaELQEDL 1168
Cdd:pfam05483 212 EmhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKD-LTFLLEESRDKANQLEEKTKLQDE--NLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1169 ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAiddetRNHESQIQEMRQRHGTALEE 1248
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1249 ISEQLEQakrvkgNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQT 1328
Cdd:pfam05483 364 LLRTEQQ------RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1329 ELDNVSCLLEDAEKK----GIKLTKDVSSLESQLQDTQELLQEETRQKLnlssRIRQLEEEKNNLLEQQEEEEESRKNLE 1404
Cdd:pfam05483 437 KEQELIFLLQAREKEihdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKL----KNIELTAHCDKLLLENKELTQEASDMT 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1405 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTS----QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQ 1480
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVReefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1481 RQIVSNLEK----KQKKFDQMLAEEKTIsaryaeeRDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1556
Cdd:pfam05483 593 ENKCNNLKKqienKNKNIEELHQENKAL-------KKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIED 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1557 LISSKDDVgknVHELEKSKRTLEQQVeemrtqleELEDELQATEDAKLRLEVN-MQAMKAQFDRDLQARDEQ-----NEE 1630
Cdd:pfam05483 666 KKISEEKL---LEEVEKAKAIADEAV--------KLQKEIDKRCQHKIAEMVAlMEKHKHQYDKIIEERDSElglykNKE 734
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 688558683 1631 KKRALVKQVREME-----AELEDERKQRALAVAAKKKLEMDLKDVEA 1672
Cdd:pfam05483 735 QEQSSAKAALEIElsnikAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1109-1330 |
7.35e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1109 QDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1188
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1189 LEALKTELEDTLDTTAAQ--QELRSKREQEVAELKKAID-DETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEK 1265
Cdd:COG4942 92 IAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1266 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1330
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
894-1311 |
8.97e-11 |
|
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: 67.44 E-value: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 894 EMQAKDEELikvKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLESRVE 973
Cdd:pfam05483 385 ELQKKSSEL---EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE-KIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 974 EEEERNQSLQNEKKKMqshiqdleeqldeeeaarqKLQLEKvtaeAKIKKMEedillLEDQNSKFLKEKKLLEDRVGEMT 1053
Cdd:pfam05483 461 AIKTSEEHYLKEVEDL-------------------KTELEK----EKLKNIE-----LTAHCDKLLLENKELTQEASDMT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1054 SQLAEEEEKAKNlgkVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL 1133
Cdd:pfam05483 513 LELKKHQEDIIN---CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1134 QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1213
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1214 EQ--------------EVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKN----KQTLESDNK 1275
Cdd:pfam05483 670 EEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEqssaKAALEIELS 749
|
410 420 430
....*....|....*....|....*....|....*.
gi 688558683 1276 ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1311
Cdd:pfam05483 750 NIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
885-1473 |
9.96e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.17 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 885 LLQVTRQEE--EMQAKDEELIKVKERQVK-----VENELVEMERKHQQLLEEKNILAEQ----LQAETELFAEAEEMRAR 953
Cdd:pfam12128 272 TLIASRQEErqETSAELNQLLRTLDDQWKekrdeLNGELSAADAAVAKDRSELEALEDQhgafLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 954 LVAKKQELEEILHDLESRVEEEEERNQSLqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDI-LLLE 1032
Cdd:pfam12128 352 WQSELENLEERLKALTGKHQDVTAKYNRR--RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELrEQLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1033 DQNSKFLKEKKLLEDRVGEMTSQLAE---EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1109
Cdd:pfam12128 430 AGKLEFNEEEYRLKSRLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1110 D---QIAELQAQIDELKIQLAKK---------------EEELQAVLARG------------DEEVAQKNNA------LKQ 1153
Cdd:pfam12128 510 QasrRLEERQSALDELELQLFPQagtllhflrkeapdwEQSIGKVISPEllhrtdldpevwDGSVGGELNLygvkldLKR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1154 L---------RELQAQLAELQEDLESEKA-----------ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1213
Cdd:pfam12128 590 IdvpewaaseEELRERLDKAEEALQSAREkqaaaeeqlvqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1214 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKgnlEKNKQTLESDnkeLTNEVKSLQQAKSESEH 1293
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK---QAYWQVVEGA---LDAQLALLKAAIAARRS 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1294 KRKKLEAQLQEVMARFSEGEKVKGelaDRTHKIQTELDNVSCLLEDAEKKGikltKDVSSLESQLQDTqeLLQEETRQKL 1373
Cdd:pfam12128 744 GAKAELKALETWYKRDLASLGVDP---DVIAKLKREIRTLERKIERIAVRR----QEVLRYFDWYQET--WLQRRPRLAT 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1374 NLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVK-----RKLQKDMEVTSQK 1448
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERLAQ 894
|
650 660
....*....|....*....|....*
gi 688558683 1449 LEEkaiAFDKLEKTKNRLQQELDDL 1473
Cdd:pfam12128 895 LED---LKLKRDYLSESVKKYVEHF 916
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
960-1314 |
9.99e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.97 E-value: 9.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 960 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1039
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1040 KEKKLLEDRVgemtsqlaeeeekaKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1119
Cdd:TIGR04523 419 QEKELLEKEI--------------ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1120 DELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRDLSEELEALKTELedt 1199
Cdd:TIGR04523 485 EQKQKELKSKEKELKKL----NEEKKELEEKVKDLTKKISSLKEKIEKLESEK---KEKESKISDLEDELNKDDFEL--- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1200 ldTTAAQQELRSKREQEVAELKKAIDDETRNHEsQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTN 1279
Cdd:TIGR04523 555 --KKENLEKEIDEKNKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
330 340 350
....*....|....*....|....*....|....*
gi 688558683 1280 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEK 1314
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
810-1332 |
1.01e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 810 FFRTGVLahleEERDL--KITDIIIYFQSVCRgylARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWW 876
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 877 RLFTKVKpLLQ--VTRQEEEMQAKDEELIKVKERQVKVENELVEMerkHQQLLEEKNILAEQLQAETElfaEAEEMRARL 954
Cdd:COG4913 285 FAQRRLE-LLEaeLEELRAELARLEAELERLEARLDALREELDEL---EAQIRGNGGDRLEQLEREIE---RLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 955 VAKKQELEEILHDLESRVEEEEernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 1034
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1035 NS----KFLKEKKLLEDRVGEMTS---------QLAEEEEK-------------------AKNLGKV-----KNKQEMMM 1077
Cdd:COG4913 435 KSnipaRLLALRDALAEALGLDEAelpfvgeliEVRPEEERwrgaiervlggfaltllvpPEHYAAAlrwvnRLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1078 VDLEERLKKEEKTRQELEKAK--RKLDAETTDLQDQI-AELQAQIDELKIQlakKEEELQ--------AVLARGDEEVAQ 1146
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLeAELGRRFDYVCVD---SPEELRrhpraitrAGQVKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1147 KN-------------NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELE---DTLDTTAAQQELR 1210
Cdd:COG4913 592 KDdrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1211 SKrEQEVAELKKAIDDetrnhesqIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQA--- 1287
Cdd:COG4913 672 EL-EAELERLDASSDD--------LAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRlea 738
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 688558683 1288 --KSESEHKRKKLEAQLQEVMARFSEGEKVKgELADRTHKIQTELDN 1332
Cdd:COG4913 739 aeDLARLELRALLEERFAAALGDAVERELRE-NLEERIDALRARLNR 784
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1575-1781 |
1.94e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1575 KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnMQAMKAQFDR--DLQARDEQNEEKKRALVKQVREMEAELEDERKQ 1652
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1653 RALAvaAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ-AQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1731
Cdd:COG4913 299 ELRA--ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 688558683 1732 QLQEDLAS-SERARRHAE---QERDELADEISNSASGKAALLDEKRRLEARIAQ 1781
Cdd:COG4913 377 ASAEEFAAlRAEAAALLEaleEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1532-1766 |
1.95e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1532 ALDEALEAKEEFERLNKQL---RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1608
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIaelEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1609 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQL 1688
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1689 RKLQAQMKDYQRELEEARTSRDEIFTQSkenEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1766
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1060-1460 |
2.00e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1060 EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQA--VL 1137
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1138 ARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEV 1217
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1218 AELKKAIDDETRNHESQIQEMRQRHgtALEEISEQLEQAKR-------------------------------VKGNLEKN 1266
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLllliaaallallglggsllsliltiagvlflVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1267 KQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIK 1346
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1347 LTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEE--EKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1422
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 688558683 1423 DDVGALEGLEEVKRKLQKDMEVtSQKLEEKAIAFDKLE 1460
Cdd:COG4717 450 ELREELAELEAELEQLEEDGEL-AELLQELEELKAELR 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1336-1974 |
2.74e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1336 LLEDAEKKGIKLTKDVSSLESQ--LQDTQELLQEETRQKLnLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQ 1413
Cdd:COG4913 253 LLEPIRELAERYAAARERLAELeyLRAALRLWFAQRRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1414 LvetkkkLEDDVGALEGLEEVKRKLQKDMEVTSQKLEekaiafdklektknRLQQELDDLMVDLDHQRQIvsnLEKKQKK 1493
Cdd:COG4913 332 I------RGNGGDRLEQLEREIERLERELEERERRRA--------------RLEALLAALGLPLPASAEE---FAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1494 FDQMLAEEKTISARYAEERDRAEAEARekdtkalsmaraldealEAKEEFERLNKQLRAemedlisskddvgknvheLEK 1573
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALR-----------------DLRRELRELEAEIAS------------------LER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1574 SKRTLEQQVEEMRTQLEEL----EDELQ--------ATEDA----------------------------------KLRLE 1607
Cdd:COG4913 434 RKSNIPARLLALRDALAEAlgldEAELPfvgelievRPEEErwrgaiervlggfaltllvppehyaaalrwvnrlHLRGR 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1608 VNMQAMKAQFDRDLQARDEQN---------------------------------EEKKRA--------LVKQVREMeAEL 1646
Cdd:COG4913 514 LVYERVRTGLPDPERPRLDPDslagkldfkphpfrawleaelgrrfdyvcvdspEELRRHpraitragQVKGNGTR-HEK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1647 EDERKQRALAV----AAKKklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTqskenEKK 1722
Cdd:COG4913 593 DDRRRIRSRYVlgfdNRAK-----LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD-----EID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1723 LKSLEAEILQLQEDLASSERAR---RHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDR 1799
Cdd:COG4913 663 VASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1800 FRKTTMQ-VDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSV---KSKFK-------ASIAALE--AKILQ 1866
Cdd:COG4913 743 ARLELRAlLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMrafNREWPaetadldADLESLPeyLALLD 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1867 LEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHAdqyKEQMEKANSRMKQLK----RQLeeAEEEATRANASRR 1942
Cdd:COG4913 823 RLEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRIPfgpgRYL--RLEARPRPDPEVR 897
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 688558683 1943 KLQRELDDATEASEGLSRE--------VNTLKNRLRRGGP 1974
Cdd:COG4913 898 EFRQELRAVTSGASLFDEElsearfaaLKRLIERLRSEEE 937
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1007-1778 |
3.19e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.75 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1007 RQKLQLEKVTAEAKIKKMEEDILLLEDQnskfLKEKKLLedrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKk 1086
Cdd:PRK04863 336 HLNLVQTALRQQEKIERYQADLEELEER----LEEQNEV---VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALD- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1087 EEKTR--------QELEKAKRKLDA---ETTDLQDQIAELQAQIDEL---------KIQLAKK-----EEELQAVLARGD 1141
Cdd:PRK04863 408 VQQTRaiqyqqavQALERAKQLCGLpdlTADNAEDWLEEFQAKEQEAteellsleqKLSVAQAahsqfEQAYQLVRKIAG 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1142 E---EVAQKN--NALKQLRE----------LQAQLAELQEDLESEKAAR------NKAEKLKRDLSEELEALKTELEDTL 1200
Cdd:PRK04863 488 EvsrSEAWDVarELLRRLREqrhlaeqlqqLRMRLSELEQRLRQQQRAErllaefCKRLGKNLDDEDELEQLQEELEARL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1201 DTTAAQQElrskreqEVAELKKAIDDETRNHESQIQEMRQRhGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNE 1280
Cdd:PRK04863 568 ESLSESVS-------EARERRMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLER 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1281 VKSLQQAKSESEHKRKKLEAQLQEVMAR-FSEGEKVKGeLADRTHKIQ-TEL-DNVSclLEDA----------------- 1340
Cdd:PRK04863 640 ERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNA-LAERFGGVLlSEIyDDVS--LEDApyfsalygparhaivvp 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1341 EKKGIK---------------LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNlleqqeeeeeSRKNLEK 1405
Cdd:PRK04863 717 DLSDAAeqlagledcpedlylIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLF----------GRAAREK 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1406 QLATLQAQ---LVETKKKLEDDVgalegleevkRKLQKDMEVTSQKL-EEKAIAFD-----KLEKTKNRLQQ---ELDDL 1473
Cdd:PRK04863 787 RIEQLRAEreeLAERYATLSFDV----------QKLQRLHQAFSRFIgSHLAVAFEadpeaELRQLNRRRVElerALADH 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1474 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTIsaryAEER--DRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1551
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALNRLLPRLNLL----ADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ 931
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1552 AEMEDLisskDDVGKNVHELEKSKRTLEQQVEEMrTQLEELEDELqATEDAklrleVNMQAMKAQFDRDLQARDEQNEEK 1631
Cdd:PRK04863 932 SDPEQF----EQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHF-SYEDA-----AEMLAKNSDLNEKLRQRLEQAEQE 1000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1632 KRALVKQVREMEAELEDerkqralavaaKKKLEMDLKdveAQIEAANKARDEAIKQLRKLQAQmkdYQRELEE-ARTSRD 1710
Cdd:PRK04863 1001 RTRAREQLRQAQAQLAQ-----------YNQVLASLK---SSYDAKRQMLQELKQELQDLGVP---ADSGAEErARARRD 1063
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558683 1711 EIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL------DEKRRLEAR 1778
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLrlvkdnGVERRLHRR 1137
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1022-1530 |
3.30e-10 |
|
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: 65.23 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1022 KKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEE--EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELE 1095
Cdd:pfam10174 137 KTLEEMELRIETQkqtlGARDESIKKLLEMLQSKGLPKKSGEEdwERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELH 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1096 KAKRKLD--AETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQlaelqedlesEKA 1173
Cdd:pfam10174 217 RRNQLQPdpAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSH----------SKF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1174 ARNKAEKLKRDLSE---ELEALKTELE-------------DTLDTTAAQQELRSKREQ-EVAELKKAIDDETR---NHES 1233
Cdd:pfam10174 287 MKNKIDQLKQELSKkesELLALQTKLEtltnqnsdckqhiEVLKESLTAKEQRAAILQtEVDALRLRLEEKESflnKKTK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1234 QIQEMRQRHGTALEEIS------------------------EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKS 1289
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRdlkdmldvkerkinvlqkkienlqEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALS 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1290 ESE-------HKRKKLEAQLQEVMARFSEGEKV--------KGELADRTHKIQTELDNVSCLLEDAEKKGIKL------- 1347
Cdd:pfam10174 447 EKEriierlkEQREREDRERLEELESLKKENKDlkekvsalQPELTEKESSLIDLKEHASSLASSGLKKDSKLksleiav 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1348 ---TKDVSSLESQLQDTQElLQEETRQKLNLSSRIRQLEEEknnLLEQQEEEEESRKNLEKQLATLQAqlVETKKKLEDD 1424
Cdd:pfam10174 527 eqkKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE---VARYKEESGKAQAEVERLLGILRE--VENEKNDKDK 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1425 -VGALEGLEEVKRKLQ--KDMEVTSQKLEEKAIAFDKLEK--------TKNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1493
Cdd:pfam10174 601 kIAELESLTLRQMKEQnkKVANIKHGQQEMKKKGAQLLEEarrrednlADNSQQLQLEELMGALEKTRQELDATKARLSS 680
|
570 580 590
....*....|....*....|....*....|....*..
gi 688558683 1494 FDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1530
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA 717
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1281-1751 |
3.33e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1281 VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ- 1359
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1360 -DTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEddvgalEGLEEVKRKL 1438
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEER-----------LEELRELEEELEELEAELAELQEELE------ELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1439 QKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH--QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1516
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1517 AEAREKDTKALSMA----------RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR 1586
Cdd:COG4717 271 LILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1587 TQLEELEDELQ--ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVREMEAELEDERK--QRALAVAAKKK 1662
Cdd:COG4717 351 ELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGelEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1663 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY--QRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLASS 1740
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEEL-------KAELRELAEEWAALKLALELL 502
|
490
....*....|.
gi 688558683 1741 ERARRHAEQER 1751
Cdd:COG4717 503 EEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1654-1888 |
4.98e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1654 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQL 1733
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1734 QEDLasserarrhaEQERDELADEIS----NSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLnDRFRKTTMQVDT 1809
Cdd:COG4942 96 RAEL----------EAQKEELAELLRalyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1810 LNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1888
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1399-1662 |
7.22e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1399 SRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1478
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1479 HQRQivsNLEKKQKKFDQMLAEektisaryaeerdrAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLI 1558
Cdd:COG4942 94 ELRA---ELEAQKEELAELLRA--------------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1559 SSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQARDEQNEEKKRALVKQ 1638
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 688558683 1639 VREMEAELEDERKQRALAVAAKKK 1662
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1325-1969 |
7.49e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1325 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1404
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1405 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1484
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1485 SNLEKKQKKFDQMLAEektisaryaeerdraeAEAREKDTKALSmaralDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1564
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQ----------------ISELKKQNNQLK-----DNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1565 GKNVHELEKSkrtlEQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA 1644
Cdd:TIGR04523 263 NKIKKQLSEK----QKELEQNNKKIKELEKQLN---QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1645 ELEDERKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLK 1724
Cdd:TIGR04523 336 IISQLNEQIS-------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1725 SLEAEILQLQEDLASSERARRHAEQERDELADEISNsasgkaaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTT 1804
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-------LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1805 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKsKFKASIAALEAKILQleeqleqeaKERAAANKI 1884
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISD---------LEDELNKDD 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1885 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNT 1964
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
....*
gi 688558683 1965 LKNRL 1969
Cdd:TIGR04523 632 IIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1515-1740 |
1.34e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1515 AEAEAREKDTKALSMARA-LDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE 1593
Cdd:COG4942 17 AQADAAAEAEAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1594 DELQATEDAKLRLEVNMQAMK--------------AQFDRDLQARDEQNeekkRALVKQVREMEAELEDERKQRALAVAA 1659
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLA----PARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1660 KKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLAS 1739
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPA 245
|
.
gi 688558683 1740 S 1740
Cdd:COG4942 246 A 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1108-1852 |
1.57e-09 |
|
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: 63.20 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1108 LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLREL-QAQLAELQE-DLESEKAARNKAEKLK--R 1183
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEEIQenK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1184 DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqemrqrhgTALEEISEQLEQAK-----R 1258
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlemhfK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1259 VKGNLEKNKQTLESDNKELTN---EVKSLQQAKSESEHKRKKLEAQLQEVMARFSE-GEKVK------GELADRTHKIQT 1328
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDkekQVSLLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKlqdenlKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1329 ELDNVSCLLEDAEKKGIKLTKDV---SSLESQLQDTQELLQEET-RQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1404
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLqiaTKTICQLTEEKEAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1405 KQLATLQAQLVETKKKLEDdVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqiv 1484
Cdd:pfam05483 377 DQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLL---------- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1485 SNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLISS 1560
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENKELTQEASDMTLELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1561 KddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDEL-QATEDAKLRLEVNMQAMKAQFDRDLQARDEQN--EEKKRALVK 1637
Cdd:pfam05483 526 K----KQEERMLKQIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKK 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1638 QVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFtqsk 1717
Cdd:pfam05483 602 QIENKNKNIEELHQENK---ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL---- 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1718 ENEKKLKSLEAEILQLQEdlasserarrhaeqerdELADEISNSASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLN 1797
Cdd:pfam05483 675 EEVEKAKAIADEAVKLQK-----------------EIDKRCQHKIAEMVALMEKHKHQYDKIIEER------DSELGLYK 731
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1798 DRFRKTTMQVDTLNTELAGERsAAQKSENARQQLERQNKD-LKSKLQELEGSVKSK 1852
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIK-AELLSLKKQLEIEKEEKEkLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1526-1767 |
1.58e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1526 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR 1605
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1606 LEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAI 1685
Cdd:COG4942 88 LEKEIAELRAE----LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1686 KQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGK 1765
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 688558683 1766 AA 1767
Cdd:COG4942 244 PA 245
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1114-1947 |
1.61e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.53 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1114 ELQAQIDEL--KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1191
Cdd:TIGR00606 170 ALKQKFDEIfsATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1192 LKT---ELEDTL-------DTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKG 1261
Cdd:TIGR00606 250 LKNrlkEIEHNLskimkldNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1262 NLEKNKQTLESDNKELTNEVKSLQ-QAKSESEHKRKKlEAQLQEVMARFSEGEKVKGELADRthkiqtELDNVSCL-LED 1339
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLATRLELDGFERGPFSER------QIKNFHTLvIER 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1340 AEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrknLEKQlatlQAQLVETKK 1419
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEI----------------LEKK----QEELKFVIK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1420 KLEDDVGALEGLEEVKRKLQKDMEVTSqKLEEKAIAFDKLEKTKNRLQQELDdlmvdldhqrqivsnLEKKQKKFDQMLA 1499
Cdd:TIGR00606 462 ELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQNEKAD---------------LDRKLRKLDQEME 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1500 EEKtisaRYAEERDRAEAEAREKDTKalsmaraldealeakeeFERLNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLE 1579
Cdd:TIGR00606 526 QLN----HHTTTRTQMEMLTKDKMDK-----------------DEQIRKIKSRHSDELTSLLGYF-PNKKQLEDWLHSKS 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1580 QQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFDRDLQARDEQneekkralvkqvremEAELEDerkqRALAVAA 1659
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ---------------LSSYED----KLFDVCG 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1660 KKKLEMDLKDVEAQIEAANKardeaikQLRKLQAQMKDYQRELEEARTSR-------DEIFTQSKENEKKLKSLEAEILQ 1732
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRL 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1733 LQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMElLNDRFRKTTMQVDTLNT 1812
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAK 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1813 ELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVK----SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1888
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1889 EKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRE 1947
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
935-1323 |
1.74e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.83 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 935 EQLQAETELFAEAEEMRA-------RLVAKKQELEEILHDLESRVEEEEERNQSLQNEK--KKMQSHIQDLEEQLDEEEA 1005
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1006 ARQKLQLEKVTAEAKIKKmeEDILLLEDQNSKFLKEKKL----LEDRVGEMtsQLAEEEEKAKNLGKVKNKQEMMMvdle 1081
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKREL--ERIRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1082 ERLKKEEKTRQELEKAkRKLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLR-ELQAQ 1160
Cdd:pfam17380 386 ERQQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIR---AEQEEARQREVRRLEEERAREMERVRLEEqERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1161 LAELQEDLESEKAARNKAEKLKRDLSEelealkteledtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQ 1240
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKR-----------------AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1241 RHGTALEEiseqleqAKRVKGNLEKNKQtlesdnKELtNEVKSLQQAKSESEHKRKKLEA--QLQEVMARFSEGEKVKGE 1318
Cdd:pfam17380 525 RQKAIYEE-------ERRREAEEERRKQ------QEM-EERRRIQEQMRKATEERSRLEAmeREREMMRQIVESEKARAE 590
|
....*
gi 688558683 1319 LADRT 1323
Cdd:pfam17380 591 YEATT 595
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
886-1260 |
1.76e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 886 LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL---- 961
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 962 EEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKE 1041
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1042 KK------------LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1109
Cdd:COG4717 271 LIltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1110 DQIAELQAQIDELKIQLAKKEEE--LQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKlkrdlSE 1187
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----AL 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558683 1188 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHEsqIQEMRQRHGTALEEISEQLEQAKRVK 1260
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALK 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1080-1556 |
2.58e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1080 LEERLKKEektRQELEKAKRKLDaetTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQA 1159
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1160 QLAELQEDLEsekaARNKAEKLKRDLSEELEALKtELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR 1239
Cdd:COG4717 120 KLEKLLQLLP----LYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1240 QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAksesehKRKKLEAQLQEVMARFSEGEKVKGEL 1319
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE------ERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1320 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEES 1399
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1400 RKNLEKQLATLQAQLvetkkkleddvgALEGLEEVKRKLQKDMEVTS-QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1478
Cdd:COG4717 349 LQELLREAEELEEEL------------QLEELEQEIAALLAEAGVEDeEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1479 HQRQIVSNLEKKQKKfdQMLAEEKTISARYAEERDRAEAEAREKDTKaLSMARALDEALEAKEEFERLNKQLRAEMED 1556
Cdd:COG4717 417 ELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAE-LEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
980-1206 |
3.24e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 980 QSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEE 1059
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1060 EEKaknLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLAR 1139
Cdd:COG4942 103 KEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1140 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ 1206
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1440-1835 |
5.52e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1440 KDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQmLAEEKTISARYAEERDRAEA-E 1518
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1519 AREKDTKAL--SMARALDEALEAKEEFERLNKQL----RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEL 1592
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1593 EDELQATEDAK-----------------------------------LRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVK 1637
Cdd:COG4717 233 ENELEAAALEErlkearlllliaaallallglggsllsliltiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1638 QVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRkLQAQMKDYQRELEEARTSRDEIFTQSK 1717
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1718 ENEKKLKSLEAEILQLQEDLASSERARRH--AEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1795
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 688558683 1796 --LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQN 1835
Cdd:COG4717 472 aeLLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
925-1306 |
6.24e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 60.68 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 925 QLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEE 1004
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1005 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERL 1084
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1085 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAvlargdeevaqknnALKQLRELQAQLAel 1164
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEA--------------LLEELRSLQERLN-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1165 qedlesekAARNKAEKLKRDLSE---------------ELEALKTELEdTLDTTAAQQELRSKREQEVAELKKAIDDETR 1229
Cdd:pfam07888 248 --------ASERKVEGLGEELSSmaaqrdrtqaelhqaRLQAAQLTLQ-LADASLALREGRARWAQERETLQQSAEADKD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1230 NHESQIQEMRQRHGTALEEISEQleQAKRVKGNLEK--NKQTLESDNKELTNEVKSLQQAKSESEHkrkkLEAQLQEVM 1306
Cdd:pfam07888 319 RIEKLSAELQRLEERLQEERMER--EKLEVELGREKdcNRVQLSESRRELQELKASLRVAQKEKEQ----LQAEKQELL 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1109-1334 |
1.03e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1109 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEE 1188
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1189 LEALK---------------TELEDTLDTTAAQQELRSKREQEVAELKKAIdDETRNHESQIQEMRQRHGTALEEISEQL 1253
Cdd:COG3883 92 ARALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1254 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1333
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
.
gi 688558683 1334 S 1334
Cdd:COG3883 251 A 251
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
922-1303 |
1.12e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.52 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 922 KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEIlhdlESRVEEEEERNQSLQNEKKKMqshiqdleeqld 1001
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA----EKARQAEMDRQAAIYAEQERM------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1002 eeeAARQKLQLEKVTAEAKIKKMEEdillledqnskflkekklledrvgemtsqlAEEEEKAKNLGKVKNKQEMMMvdle 1081
Cdd:pfam17380 343 ---AMERERELERIRQEERKRELER------------------------------IRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1082 ERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDELK--------IQLAKKEEELQAVLARGDEEVAQKNNALKQ 1153
Cdd:pfam17380 386 ERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVER 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1154 LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEElealktELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHES 1233
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1234 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQtlesdNKELTNEVKslqqaksESEHKRKKLEAQLQ 1303
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----EREMMRQIV-------ESEKARAEYEATTP 596
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1007-1324 |
1.18e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1007 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR--VGEMTSQLAEEEEKAKNLgkvknKQEMMMVD-LEER 1083
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELERL-----DASSDDLAaLEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1084 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1163
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1164 LQEDLESEKA-ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQE-----VAELKKAIDDETRNHESQIQ- 1236
Cdd:COG4913 774 RIDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFVADLLs 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1237 EMRQrhgtALEEISEQLEQAKRVKGNLEKNKQT---LESDNKELTnEVKSLQQ--------AKSESEHKRKKLEAQLQEV 1305
Cdd:COG4913 854 KLRR----AIREIKERIDPLNDSLKRIPFGPGRylrLEARPRPDP-EVREFRQelravtsgASLFDEELSEARFAALKRL 928
|
330 340
....*....|....*....|....*
gi 688558683 1306 MARF--SEGEKVKGELAD----RTH 1324
Cdd:COG4913 929 IERLrsEEEESDRRWRARvldvRNH 953
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1088-1310 |
1.30e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1088 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQ--LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1165
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1166 EDLES--EKAARNKAEKLKRDLSEELEALKTELEDTLDT-TAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRH 1242
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQ-IAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1243 GTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFS 1310
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1579-1791 |
1.48e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1579 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVA 1658
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1659 AKKKLEMDLKDVEAQIEAANKArdEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLA 1738
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 688558683 1739 SSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQS 1791
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1501-1971 |
1.52e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1501 EKTISARYAEERDRAEAEArekdtkALSMARALDEALEAKEEFERLNkqlraemeDLISSKDDVGKNVHELEKSKRTLEQ 1580
Cdd:PRK02224 169 ERASDARLGVERVLSDQRG------SLDQLKAQIEEKEEKDLHERLN--------GLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1581 QVEEMRTQLEELEDELQATEDAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1660
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIE------------DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1661 KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlqedLASS 1740
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE-------LEEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1741 ERARRHAEQERDELADEIsnsasgkaalldekRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELageRSA 1820
Cdd:PRK02224 376 REAVEDRREEIEELEEEI--------------EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL---RTA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1821 AQKSENARQQLERQNkdLKSKLQELEGS----VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVrRTEKKLKEVF 1896
Cdd:PRK02224 439 RERVEEAEALLEAGK--CPECGQPVEGSphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLE 515
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1897 MQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1971
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1262-1861 |
2.07e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.53 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1262 NLEKNKQTLESDNKELTNEVKSLQQAK---SESEHKRKKLEAQLQEVMarfsegekvkgelaDRTHKIQTELDNVSCLLE 1338
Cdd:PRK01156 184 NIDYLEEKLKSSNLELENIKKQIADDEkshSITLKEIERLSIEYNNAM--------------DDYNNLKSALNELSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1339 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIrqleeeknnlleqqeeeeESRKNLEKQLATLQAQLVETK 1418
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPV------------------YKNRNYINDYFKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1419 KKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1498
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV--------LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1499 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEAleaKEEFERLNKQLRAemedLISSKDDVGKNVHEL------- 1571
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI---SSKVSSLNQRIRA----LRENLDELSRNMEMLngqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1572 --------EKSKRTLEQQVEE---MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVR 1640
Cdd:PRK01156 457 vcgttlgeEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-RADLEDIK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1641 EMEAELEDERKQRALAVAAKKklEMDLKDVEAQ---------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1705
Cdd:PRK01156 536 IKINELKDKHDKYEEIKNRYK--SLKLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1706 RTSRDEIFtqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELAdeisnsasGKAALLDEKRRLEARIAQleee 1785
Cdd:PRK01156 614 KSYIDKSI---REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSIIPDLKEITSRIND---- 678
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1786 leeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvksKFKASIAALE 1861
Cdd:PRK01156 679 ----------IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK-----KIKKAIGDLK 739
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
887-1307 |
2.20e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 887 QVTRQEEEMQAKDEELIKVKERQVKVENELVEME---RKHQQLLEEKNILAEQLQAETELFAEAEEMRaRLVAKKQELEE 963
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELReelEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 964 ILHDLESRVEEEEERNQSLQNEKKK----MQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1039
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1040 KEKKLLEDR-----VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1114
Cdd:COG4717 241 LEERLKEARlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1115 LQAQIDELKIQLAKKEEELQAVLARgdeevaqknnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKT 1194
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDR-----------IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1195 ELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1274
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
410 420 430
....*....|....*....|....*....|...
gi 688558683 1275 keltnevkSLQQAKSESEHKRKKLEAQLQEVMA 1307
Cdd:COG4717 470 --------ELAELLQELEELKAELRELAEEWAA 494
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1612-1779 |
2.45e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.86 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1612 AMKAQFDR--DLQARD---EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIK 1686
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1687 QLRKLQA--QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsg 1764
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL-- 158
|
170
....*....|....*
gi 688558683 1765 kAALLDEKRRLEARI 1779
Cdd:COG1579 159 -EELEAEREELAAKI 172
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1450 |
2.72e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 850 KQQQLSALKVLQRNCAAYLKLRHWqwwRLFTKVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELvemerkhqQLLEE 929
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL--------SKAEK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 930 KNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK 1009
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1010 LQLEKV--TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNkQEMMMVDLEERLKKE 1087
Cdd:TIGR00606 573 KQLEDWlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKEEIEKS 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1088 EKTRQELE----------------------------KAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLAR 1139
Cdd:TIGR00606 652 SKQRAMLAgatavysqfitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1140 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRS---KREQE 1216
Cdd:TIGR00606 732 APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDverKIAQQ 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1217 VAELKKAIDDETRnheSQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRK 1296
Cdd:TIGR00606 812 AAKLQGSDLDRTV---QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEE 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1297 KLEAQLQEVMARFSE--------------GEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1362
Cdd:TIGR00606 889 QLVELSTEVQSLIREikdakeqdspletfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK 968
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1363 E--LLQEETrqklNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLveTKKKLEDDVGALEGLEEVKRK 1437
Cdd:TIGR00606 969 DdyLKQKET----ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNL--TLRKRENELKEVEEELKQHLK 1042
|
650
....*....|...
gi 688558683 1438 LQKDMEVTSQKLE 1450
Cdd:TIGR00606 1043 EMGQMQVLQMKQE 1055
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
900-1855 |
3.11e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 59.29 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 900 EELIKVKERQVKVENELVEMERKHQQLLEEKniLAEQLQAETELFAEAEEMRARLVAK-KQELEEILHDLESRVEEEEER 978
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMETATVELH--LSNIENKKNELLDIIVEIKKHIHGEiNKDLNKILEDFKNKEKELSNK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 979 NQSLQNEK---KKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQ 1055
Cdd:TIGR01612 771 INDYAKEKdelNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1056 LAEEEEKAKNlgKVKNKQEMMmVDLEERLKKEEKTRQeLEKAKRKLDaettDLQDQIAELQAQIDE--LKIQLAKKEEEL 1133
Cdd:TIGR01612 851 FINFENNCKE--KIDSEHEQF-AELTNKIKAEISDDK-LNDYEKKFN----DSKSLINEINKSIEEeyQNINTLKKVDEY 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1134 QAVLARGDEEVAQKNNALKQLRE-LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTlDTTAAQQEL--- 1209
Cdd:TIGR01612 923 IKICENTKESIEKFHNKQNILKEiLNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLN-DYEAKNNELiky 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1210 ------------RSKREQEVAELKKAIDD---ETRNHESQIQEMRQRHGTALEEISEQLEqaKRVKGNLEK-NKQTLESD 1273
Cdd:TIGR01612 1002 fndlkanlgknkENMLYHQFDEKEKATNDieqKIEDANKNIPNIEIAIHTSIYNIIDEIE--KEIGKNIELlNKEILEEA 1079
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1274 NKELTNEVKSLQQAK----------------SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNvsclL 1337
Cdd:TIGR01612 1080 EINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQIND----L 1155
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1338 EDAEKKGIKlTKDVSSLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNNLLEQQEEEEESRKNLEKqlaTLQ 1411
Cdd:TIGR01612 1156 EDVADKAIS-NDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGK---LFL 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1412 AQLVETKKKLEDDVGALEG----LEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDD----LMVDLDHQRQI 1483
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEAyiedLDEIKEK--------SPEIENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI 1300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1484 vSNLEKKQKKFDQMLAEEKTISARYAE-ERDRAEAEAREKDT--------------KALSMARALDEALEAKEEFERLNK 1548
Cdd:TIGR01612 1301 -SDIREKSLKIIEDFSEESDINDIKKElQKNLLDAQKHNSDInlylneianiynilKLNKIKKIIDEVKEYTKEIEENNK 1379
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1549 QLRAEM---EDLISS-KDDVgknvhELEKSKRTLEQQVEEmrTQLEELEDELQATEDAKLRLEVNMqamkaqfDRDLQAR 1624
Cdd:TIGR01612 1380 NIKDELdksEKLIKKiKDDI-----NLEECKSKIESTLDD--KDIDECIKKIKELKNHILSEESNI-------DTYFKNA 1445
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1625 DEQNEEKKrALVKQVremeaELEDERKQRALAVA---AKKKLEMDLKDVEAQIEAANKARDEA---IKQLRKLQAQMKDY 1698
Cdd:TIGR01612 1446 DENNENVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQY 1519
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1699 QRELEE------ARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK 1772
Cdd:TIGR01612 1520 KKDVTEllnkysALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQ 1599
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1773 RRLEA------RIAQLEEELEEEQSNMELLNDRFrkTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1846
Cdd:TIGR01612 1600 LSLENfenkflKISDIKKKINDCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD 1677
|
....*....
gi 688558683 1847 gSVKSKFKA 1855
Cdd:TIGR01612 1678 -ELDSEIEK 1685
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
881-1306 |
3.13e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 881 KVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRarlvaKKQE 960
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 961 leeilhdlesrveeeeernqslqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1040
Cdd:PTZ00121 1631 ------------------------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1041 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAElqaQID 1120
Cdd:PTZ00121 1687 EKKAAE--------ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEE 1755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1121 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRDLSEELEAlkTELE 1197
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiieGGKEGNLVINDSKEMED--SAIK 1833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1198 DTLDTTAAQQElRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1277
Cdd:PTZ00121 1834 EVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDL----KEDDEEEIEEADEIEKIDKDDIEREIPNNNMA 1908
|
410 420
....*....|....*....|....*....
gi 688558683 1278 TNEVKSLQQAKSESEHKRKKLEAQLQEVM 1306
Cdd:PTZ00121 1909 GKNNDIIDDKLDKDEYIKRDAEETREEII 1937
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1058-1234 |
3.25e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1058 EEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVL 1137
Cdd:COG3883 17 QIQAKQKELSELQAELE----AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1138 A-----------------------------RGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1188
Cdd:COG3883 93 RalyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 688558683 1189 LEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQ 1234
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1100-1253 |
3.82e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.09 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1100 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAV---LARGDEEVAQKNNALKQLRELQA-------------QLAE 1163
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteLEDLEKEIKRLELEIEEVEARIKkyeeqlgnvrnnkEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1164 LQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHG 1243
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
170
....*....|
gi 688558683 1244 TALEEISEQL 1253
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1587-1971 |
3.99e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1587 TQLEELEDELQATEDAKLRLevnmqamkaqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAL--AVAAKKKLE 1664
Cdd:COG4717 71 KELKELEEELKEAEEKEEEY------------AELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1665 MDLKDVEAQIEAAnkarDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ-SKENEKKLKSLEAEILQLQEDLASSERA 1743
Cdd:COG4717 139 AELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1744 RRHAEQERDELADEISNSASGKAALLDEKRRLEARI------------AQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1811
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1812 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1891
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1892 --LKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEASEGLSREVNTLKN 1967
Cdd:COG4717 374 alLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELRE 453
|
....
gi 688558683 1968 RLRR 1971
Cdd:COG4717 454 ELAE 457
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1107-1703 |
4.67e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1107 DLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLS 1186
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1187 EELEALK--TELEDTLDTTAAQQELRSKRE-QEVAELKKAIDDETR---NHESQIQEMRQRHGTA--LEEISEQLEQAKR 1258
Cdd:PRK01156 267 MELEKNNyyKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKKQilsNIDAEINKYHAIIKKLsvLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1259 VKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSclle 1338
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS---- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1339 daekkgikltKDVSSLESQLQDTQELLQEETRQKLNLSSRIR------QLEEEKNNLLEQQEEEEESRknlekqlatlqa 1412
Cdd:PRK01156 423 ----------SKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSNHIINHYNEKKSR------------ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1413 qLVETKKKLEDDVGAlegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKnrlQQELDDLMVDLdhqrqivSNLEKKQK 1492
Cdd:PRK01156 481 -LEEKIREIEIEVKD---IDEKIVDLKKRKEYLESEEINKSINEYNKIESA---RADLEDIKIKI-------NELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1493 KFDQMLAEEKTISARYAEER----------------DRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1556
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSKrtswlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1557 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQ---LEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEqneekKR 1633
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKIDNYKKQiaeIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR-----LE 701
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1634 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIkqLRK-----LQAQMKDYQRELE 1703
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAM--IRKsasqaMTSLTRKYLFEFN 774
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1499-1762 |
5.04e-08 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 58.11 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1499 AEEKTISARYAEERDRaeaeaREKDTKALS-MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1577
Cdd:pfam05667 226 WNSQGLASRLTPEEYR-----KRKRTKLLKrIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1578 L----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQ---NEEKKRALVKQVREMEAELEDER 1650
Cdd:pfam05667 301 ThtekLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLE-DLESSIQElekEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1651 KQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-EEARTSRDEIFTQSKENEKKL---KSL 1726
Cdd:pfam05667 380 EELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLiEEYRALKEAKSNKEDESQRKLeeiKEL 459
|
250 260 270
....*....|....*....|....*....|....*.
gi 688558683 1727 EAEILQLQEDLASSERARRHAEQERDELADEISNSA 1762
Cdd:pfam05667 460 REKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSA 495
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1354-1906 |
5.38e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.21 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1354 LESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEE 1433
Cdd:pfam05557 32 LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLAD-------ARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1434 VKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERD 1513
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1514 RAEaearekdtkalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQvEEMRTQLEELE 1593
Cdd:pfam05557 185 DSE------------IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-EKYREEAATLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1594 DELQATEdAKLRLEVNMQAMKAQFDR---DLQARDEQNEEKKRALVKQVREMEAELEDERKQRalavaakKKLEMDLKDV 1670
Cdd:pfam05557 252 LEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR-------RELEQELAQY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1671 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEART---SRDEIFTQSKENEKKLKSLE--AEILQLQEDLASSERARR 1745
Cdd:pfam05557 324 LKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQAHNEEMEAQL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1746 HAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELL--NDRFR--KTTMQVDTLNTELAGERSAA 1821
Cdd:pfam05557 404 SVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLEleRQRLReqKNELEMELERRCLQGDYDPK 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1822 -----QKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK---LK 1893
Cdd:pfam05557 484 ktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKnqrLK 563
|
570
....*....|...
gi 688558683 1894 EVFMQVEDERRHA 1906
Cdd:pfam05557 564 EVFQAKIQEFRDV 576
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1293-1966 |
6.29e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 58.31 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1293 HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSslesqlQDTQELLQEETRQK 1372
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1373 LNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE--------VKRKLQKDMEV 1444
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAkynrrrskIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1445 TSQKLE--------EKAIAFDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQMLAEEKTISARyaEERDRA 1515
Cdd:pfam12128 395 IKDKLAkireardrQLAVAEDDLQALESELREQLEAGKLEFnEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1516 EAEAREKDTKAL-SMARALDEALEAKEEFERLNKQLRAEmedlisskddvgknvhelekskrtlEQQVEEMRTQLEELED 1594
Cdd:pfam12128 473 IERAREEQEAANaEVERLQSELRQARKRRDQASEALRQA-------------------------SRRLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1595 ELQA---TEDAKLRLEVNM--QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA-ELEDERKQRALAVAAKKKLEMDLK 1668
Cdd:pfam12128 528 QLFPqagTLLHFLRKEAPDweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1669 DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSrdeiFTQSKENEKKLKS-LEAEILQLQEdlaSSERARRHA 1747
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1748 EQERDELADEISNSASGKAALLDEKRR--LEARIAQLeeeleeeQSNMELLNDRfrktTMQVDTLNTELAGERSAAQKSE 1825
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL----DAQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1826 NArqqLERQNK-DLKSKlqELEGSVKSKFKASIAALEAKIlqleeqleqeakERAAankiVRRTEKKLKEVFMQvEDERR 1904
Cdd:pfam12128 750 KA---LETWYKrDLASL--GVDPDVIAKLKREIRTLERKI------------ERIA----VRRQEVLRYFDWYQ-ETWLQ 807
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1905 HADQYKEQMEKANSRMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLS---REVNTLK 1966
Cdd:pfam12128 808 RRPRLATQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRcemSKLATLK 876
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1007-1221 |
9.61e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1007 RQKLQlekvTAEAKIK--KMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEErL 1084
Cdd:COG3206 188 RKELE----EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-S 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1085 KKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAkkeEELQAVLARGDEEVAQknnALKQLRELQAQL 1161
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREASLQAQL 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1162 AELQEDLESEKAARNKAEKLKRDlseeLEALKTELEDTLdttAAQQELRSKREQEVAELK 1221
Cdd:COG3206 337 AQLEARLAELPELEAELRRLERE----VEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1177-1894 |
1.00e-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: 57.42 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1177 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR-QRHGTAL--EEISEQL 1253
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNaTRHLCNLlkETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1254 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRTHKIQTELDNV 1333
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE------DHEKIQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1334 SCLLEDAEKKgikltkdvsslESQLQDTQELLqEETRQKLNlssrirQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQ 1413
Cdd:pfam05483 243 SLLLIQITEK-----------ENKMKDLTFLL-EESRDKAN------QLEEKTKLQDENLKELIEKKDHLTKELEDIKMS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1414 L---VETKKKLEDDVG-ALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQ----ELDDLMVDLDHQRQIVS 1485
Cdd:pfam05483 305 LqrsMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1486 NLEKKQKKFDQMlaeektisaryAEERDRAEAEAREKDTKALSMARALDEaleaKEEFERLNKQLRAEMEDLISSKDDVG 1565
Cdd:pfam05483 385 ELQKKSSELEEM-----------TKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1566 KNVHELE-------KSKRTLEQQVEEMRTQLE-ELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ--------NE 1629
Cdd:pfam05483 450 KEIHDLEiqltaikTSEEHYLKEVEDLKTELEkEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQediinckkQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1630 EKKRALVKQVREMEAELEDE--------RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE 1701
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDElesvreefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1702 LEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASserARRHAEQERDELADEISNSASGKAALLDEKRRLEARIaq 1781
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA-- 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1782 leeeleeeqsnmellnDRFRKTTMQVDTLNTELAGERSAAQKSENAR--QQLERQNKDL---KSKLQElEGSVKSKFKAS 1856
Cdd:pfam05483 685 ----------------DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydKIIEERDSELglyKNKEQE-QSSAKAALEIE 747
|
730 740 750
....*....|....*....|....*....|....*...
gi 688558683 1857 IAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1894
Cdd:pfam05483 748 LSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1362-1605 |
1.07e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1362 QELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1440
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1441 DMEVTSQKLEEKAIAFDKLEktknrlQQELDDLMVDLDHQRQIVSNLEkkqkKFDQMLAEEKTISARYAEERDRAEAEAR 1520
Cdd:COG4942 98 ELEAQKEELAELLRALYRLG------RQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1521 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1600
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 688558683 1601 DAKLR 1605
Cdd:COG4942 248 FAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1019-1441 |
1.19e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1019 AKIKKMEEDILLLEDQNSKF---LKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM---------MVDLEERLKK 1086
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1087 EEKTRQELEKAKRKLDAettdLQDQIAELQAQIDELKIQL-AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1165
Cdd:COG4717 151 LEERLEELRELEEELEE----LEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1166 EDLESEKAARNKAEKLKRDLSEE-----------LEALKTELEDTLDTTAA------------QQELRSKREQEVAELKK 1222
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1223 AIDDETRN--HESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELtnEVKSLQQAKSESEHKRK-KLE 1299
Cdd:COG4717 307 LQALPALEelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGvEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1300 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLNLSSRI 1379
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1380 RQLEEEKNNLleqqeeeeesrkNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1441
Cdd:COG4717 463 EQLEEDGELA------------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
928-1150 |
1.20e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 928 EEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDE--EEA 1005
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1006 ARQKLQLEKVTAEA-KIKKMEEDILLLEDQN-SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEER 1083
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1084 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAVLARGDEEVAQKNNA 1150
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
887-1452 |
1.26e-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: 57.04 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 887 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELE 962
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 963 EILHDLESRVEEEEernQSLQNEKKKMQSHiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1042
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKN--------------EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1043 KLLedrvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERlkkeektrqelEKAKRKLDAETTDLQDQIAELQAQIDEL 1122
Cdd:pfam05483 412 KIL----AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR-----------EKEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1123 KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldt 1202
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE----- 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1203 tAAQQELRSKREqevaELKKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVK 1282
Cdd:pfam05483 552 -SVREEFIQKGD----EVKCKLDKSEENARSIEYEVLKKE-KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1283 SLQQAKSESEHKRKKLEAQLQEVMARFsegekvkGELADRTHK-IQTELDNVSCLLEDAEK------KGIKLTKDVsSLE 1355
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKF-------EEIIDNYQKeIEDKKISEEKLLEEVEKakaiadEAVKLQKEI-DKR 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1356 SQlQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDvgaleglEEVK 1435
Cdd:pfam05483 698 CQ-HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIE-------KEEK 769
|
570
....*....|....*..
gi 688558683 1436 RKLQKDMEVTSQKLEEK 1452
Cdd:pfam05483 770 EKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1619-1830 |
1.30e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1619 RDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1698
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1699 QRELEEA-RTSRDEIFTQSKENEKKLKSLE----------AEILQLQEDLASSERARRHAEQERDELADEISNSASGKAA 1767
Cdd:COG4942 110 LRALYRLgRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558683 1768 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQ 1830
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1320-1556 |
1.49e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1320 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeees 1399
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1400 rKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH 1479
Cdd:COG4942 86 -AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA---LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1480 QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1556
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1081-1291 |
1.52e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1081 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRE-LQA 1159
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREeLGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1160 QLAELQED----------LESE----------------KAARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQELRSKR 1213
Cdd:COG3883 91 RARALYRSggsvsyldvlLGSEsfsdfldrlsalskiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1214 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1291
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1545-1971 |
1.60e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1545 RLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnmqamkAQFDRDLQAR 1624
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1625 DEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV----EAQIEAANKARDEAIKQLRKLQAQMKDYQR 1700
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1701 ELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL-----DEKRRL 1775
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLflllaREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1776 EARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKskLQELEGSVKSKFKA 1855
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1856 SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVfmqvedERRHADQYKEQMEKansRMKQLKRQLEEAEEEAT 1935
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL------EELLEALDEEELEE---ELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 688558683 1936 RANASRRKLQRELDDATEASE--GLSREVNTLKNRLRR 1971
Cdd:COG4717 450 ELREELAELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
983-1736 |
2.26e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 56.60 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 983 QNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQ-NSKFLKEKKLLEDRVGEMTSQLaEEEE 1061
Cdd:TIGR01612 532 QNIKAKLYKEIEAGLKESYELAKNWKKLIHE---IKKELEEENEDSIHLEKEiKDLFDKYLEIDDEIIYINKLKL-ELKE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1062 KAKNLGKvKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI-AELQAQIDEL-KIQLAKKEEELQAVLAR 1139
Cdd:TIGR01612 608 KIKNISD-KNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIySTIKSELSKIyEDDIDALYNELSSIVKE 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1140 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELEDTLDTTAaqQELRSKR 1213
Cdd:TIGR01612 687 NAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVElhlsniENKKNELLDIIVEIKKHIHGEINKDLNKIL--EDFKNKE 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1214 EQEVAELK--KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRvkgNLEKNKQTL------ESDNKELTNEVKSLQ 1285
Cdd:TIGR01612 765 KELSNKINdyAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQ---NYDKSKEYIktisikEDEIFKIINEMKFMK 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1286 QAKSESEHKRKKLEAQLQEVM----ARFSE-GEKVKGELADR-------------------THKIQTELDNVSCLLEDAE 1341
Cdd:TIGR01612 842 DDFLNKVDKFINFENNCKEKIdsehEQFAElTNKIKAEISDDklndyekkfndskslineiNKSIEEEYQNINTLKKVDE 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1342 KkgIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKl 1421
Cdd:TIGR01612 922 Y--IKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIE--KSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNN- 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1422 eddvGALEGLEEVKRKLQKDMEVTSQKleekaiAFDKLEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEE 1501
Cdd:TIGR01612 997 ----ELIKYFNDLKANLGKNKENMLYH------QFDEKEKATNDIEQKIEDA-------NKNIPNIEIAIHTSIYNIIDE 1059
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1502 ktISARYAEERDRAEAEAREKDTKALSMARALDEALE-------AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKS 1574
Cdd:TIGR01612 1060 --IEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKhynfddfGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1575 KRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFDRDLQARDEQNEekkraLVKQVREMEAELEDERK 1651
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEE 1211
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1652 QRALAVA---------------AKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMkDYQRELEEARTSRDEI---F 1713
Cdd:TIGR01612 1212 VKGINLSygknlgklflekideEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEMETFNISHDDDkdhH 1290
|
810 820
....*....|....*....|...
gi 688558683 1714 TQSKENEKKLKSLEAEILQLQED 1736
Cdd:TIGR01612 1291 IISKKHDENISDIREKSLKIIED 1313
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1648-1970 |
2.49e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1648 DERKQRALAvaakkklemDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDeifTQSKENEKKLKSLE 1727
Cdd:TIGR02169 169 DRKKEKALE---------ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKRE---YEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1728 AEILQLQEDLASSERARRHAEQERDELADEIsnsasgkAALLDEKRRLEARIaqleeeleeeqsnMELLNDRFRKTTMQV 1807
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRL-------EEIEQLLEELNKKI-------------KDLGEEEQLRVKEKI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1808 DTLNTELAgersaaqksenarqQLERQNKDLKSKLQELEGSVKsKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRR 1887
Cdd:TIGR02169 297 GELEAEIA--------------SLERSIAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1888 TEKKLKEVFMQVEDE-------RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSR 1960
Cdd:TIGR02169 362 LKEELEDLRAELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
330
....*....|
gi 688558683 1961 EVNTLKNRLR 1970
Cdd:TIGR02169 442 EKEDKALEIK 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1561-1781 |
2.83e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1561 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVR 1640
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAK-LLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1641 EMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIK-------QLRKLQAQMKDYQREL-EEARTSRD 1710
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558683 1711 EIFTQSKENEKKLKSLEAEILQLQEDLAS-SERARRHAEQERD-ELADEISNSasgkaaLLdeKRRLEARIAQ 1781
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1132-1304 |
2.86e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1132 ELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtlDTTAAQQELRS 1211
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1212 KREQEvaelkkAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1291
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|...
gi 688558683 1292 EHKRKKLEAQLQE 1304
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1077-1954 |
3.38e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1077 MVDLEERLKKEEKT---RQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlakkEEELQAVLARgdeeVAQKNNAL-- 1151
Cdd:PRK04863 275 MRHANERRVHLEEAlelRRELYTSRRQLAAEQYRLVEMARELAELNEAESDL----EQDYQAASDH----LNLVQTALrq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1152 -KQLRELQAQLAELQEDLESEKAARNKAeklkRDLSEELEALKTELEDTLDTTAAQqelrskreqeVAELKKAID-DETR 1229
Cdd:PRK04863 347 qEKIERYQADLEELEERLEEQNEVVEEA----DEQQEENEARAEAAEEEVDELKSQ----------LADYQQALDvQQTR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1230 NheSQIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarf 1309
Cdd:PRK04863 413 A--IQYQQAVQ----ALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV---- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1310 segekvkgeladrtHKIQTELDNvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEKN 1387
Cdd:PRK04863 483 --------------RKIAGEVSR-----SEAWDVARELLRRLREQRHLAEQLQQLRMRlsELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1388 NLLEQQEeeeesrkNLEKQLATLQAQLVEtkkkleddvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK---- 1463
Cdd:PRK04863 544 KRLGKNL-------DDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawl 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1464 ------NRLQ----------QELDDLMVD-LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKA 1526
Cdd:PRK04863 607 aaqdalARLReqsgeefedsQDVTEYMQQlLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1527 LSMARAlDEALEAKEEFERLNKQLR---------------AEMEDL----------ISSKDDVGKNVHELEK------SK 1575
Cdd:PRK04863 687 LSEIYD-DVSLEDAPYFSALYGPARhaivvpdlsdaaeqlAGLEDCpedlyliegdPDSFDDSVFSVEELEKavvvkiAD 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1576 RTL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDLQ-----ARDEQNEEKKR 1633
Cdd:PRK04863 766 RQWrysrfpevplfgraarEKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELR 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1634 ALVKQVREMEAELED----ERKQRALAVAAKKKL--------EMDLKDVEAQIEAANKARDEaIKQLRKLQAQMKDYQRE 1701
Cdd:PRK04863 841 QLNRRRVELERALADhesqEQQQRSQLEQAKEGLsalnrllpRLNLLADETLADRVEEIREQ-LDEAEEAKRFVQQHGNA 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1702 LEeartsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAllDEKRRLEARIAq 1781
Cdd:PRK04863 920 LA-----------QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAKNSD- 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1782 leeeleeeqsnmelLNDRFRkttmqvdtlntelagersaaQKSENARQQLERQNKDLKSKLQELegsvkSKFKASIAALE 1861
Cdd:PRK04863 986 --------------LNEKLR--------------------QRLEQAEQERTRAREQLRQAQAQL-----AQYNQVLASLK 1026
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1862 AkilqleeqleqeakERAAANKIVRRTEKKLKEVFMQVEDE-----RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR 1936
Cdd:PRK04863 1027 S--------------SYDAKRQMLQELKQELQDLGVPADSGaeeraRARRDELHARLSANRSRRNQLEKQLTFCEAEMDN 1092
|
970
....*....|....*...
gi 688558683 1937 ANASRRKLQRELDDATEA 1954
Cdd:PRK04863 1093 LTKKLRKLERDYHEMREQ 1110
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1411-1629 |
3.58e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1411 QAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1490
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1491 QKKFDQMLAEEKTI--SARYAEERDRAEAEAREKDtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknv 1568
Cdd:COG3883 95 LYRSGGSVSYLDVLlgSESFSDFLDRLSALSKIAD----ADADLLEELKADKAELEAKKAELEAKLAELEALKA------ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 1569 hELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNE 1629
Cdd:COG3883 165 -ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1488-1971 |
3.83e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1488 EKKQKKFDQMLAEEKTISARYAEERDRAEA----EAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDD 1563
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1564 VGKNVHELEKSKRTLEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRAL 1635
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1636 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1715
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1716 SKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1788
Cdd:TIGR02169 415 LQRLseeladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1789 EQSNMELLNDRFRKTTMQVDTLNTEL------------------------AGERSAAQKSEN------ARQQLERQN--- 1835
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgeryataievaAGNRLNNVVVEDdavakeAIELLKRRKagr 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1836 ------KDLKSKLQELE--------------------------------------------------------------- 1846
Cdd:TIGR02169 575 atflplNKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtlegelfeksga 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1847 ---GSVKSKFKASIAA-LEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQ 1922
Cdd:TIGR02169 655 mtgGSRAPRGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1923 LKRQLEEAEEE-------ATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1971
Cdd:TIGR02169 735 LKERLEELEEDlssleqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
892-1418 |
3.87e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.44 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 892 EEEMQAKDEELIKVKERQVKVENELVEMER-KHQQLLEEKNILAEQLQAETELFAeaeemrarlVAKKQELEEILHDLES 970
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQnKNHINNELESKEEQLSSYEDKLFD---------VCGSQDEESDLERLKE 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 971 RVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVG 1050
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRD 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1051 EMTS----QLAEEEEKAKNLGKVKNKQEMMMVD-------LEERLKKEEKTRQELEKAK---------RKLDAETTDLQD 1110
Cdd:TIGR00606 727 EMLGlapgRQSIIDLKEKEIPELRNKLQKVNRDiqrlkndIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDVER 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1111 QIAELQAQID---------ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQedleSEKAARNKAEKL 1181
Cdd:TIGR00606 807 KIAQQAAKLQgsdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK----SEKLQIGTNLQR 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1182 KRDLSEELEALKTELEDTLdttaaqQELRSKREQEVAELKKAIDDETRNHE--SQIQEMRQRHGTALEEISEQLEQAKRV 1259
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLI------REIKDAKEQDSPLETFLEKDQQEKEEliSSKETSNKKAQDKVNDIKEKVKNIHGY 956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1260 KGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSegekvkgeladrTHKIQTELDNVSCLLE 1338
Cdd:TIGR00606 957 MKDIENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID------------TQKIQERWLQDNLTLR 1024
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1339 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETK 1418
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKL--EENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1223-1465 |
3.94e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1223 AIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQL 1302
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1303 QEVMARFsegEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1382
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1383 EEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKT 1462
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 688558683 1463 KNR 1465
Cdd:COG4942 250 ALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1352-1776 |
4.05e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1352 SSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEkQLATLQAQLVETKKKLEDDVGALEG 1430
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1431 LEEVKRKLQKDMEVTSQ---------KLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkfDQMLAEE 1501
Cdd:COG4717 124 LLQLLPLYQELEALEAElaelperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1502 KTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR-----AEMEDLISSKDDVGKNVHE------ 1570
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaAALLALLGLGGSLLSLILTiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1571 ------------LEKSKRTLEQQVEEMR--TQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDL-----QARDEQNEEK 1631
Cdd:COG4717 281 lvlgllallfllLAREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1632 KRALVKQVREMEAEL--------EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRK--LQAQMKDYQRE 1701
Cdd:COG4717 361 EELQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1702 LEEARTSRDEIftqskenEKKLKSLEAEILQLQED--LASSERARRHAEQERDELADEISNSASGKAALLDEKRRLE 1776
Cdd:COG4717 441 LEELEEELEEL-------REELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
969-1180 |
4.86e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 969 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIlllEDQNSKFLKEKKLLEDR 1048
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1049 VGEM-----TSQLAEEEEKAKNLGKVKNKQEMMMVDLE---ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1120
Cdd:COG3883 92 ARALyrsggSVSYLDVLLGSESFSDFLDRLSALSKIADadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1121 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1180
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1380-1969 |
5.46e-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: 55.12 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1380 RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKL 1459
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV---HEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1460 EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDR-AEAEAREKDTKALSMARALD---- 1534
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmSTMHFRSLGSAISKILRELDteis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1535 -------------EAL--EAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTleqQVEEMRTQLEELEDELQAT 1599
Cdd:pfam15921 235 ylkgrifpvedqlEALksESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARS---QANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1600 EDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELE----------------DERKQRALAVAAKKKL 1663
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTearterdqfsqesgnlDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1664 EMDLKDVEAQ------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAE-- 1729
Cdd:pfam15921 392 ELSLEKEQNKrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQle 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1730 -----ILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNmellNDRFRKTT 1804
Cdd:pfam15921 472 stkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQ 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1805 MQVDTLNTELAGERSAA----QKSENARQ-----------------QLERQNKDLKSKLQELEgSVKSKFKASIAALEAK 1863
Cdd:pfam15921 548 TECEALKLQMAEKDKVIeilrQQIENMTQlvgqhgrtagamqvekaQLEKEINDRRLELQEFK-ILKDKKDAKIRELEAR 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1864 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQME--KANSRMK---------QLKRQLEEAEE 1932
Cdd:pfam15921 627 VSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKseemetttnKLKMQLKSAQS 706
|
650 660 670
....*....|....*....|....*....|....*..
gi 688558683 1933 EATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1969
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI 743
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1061-1193 |
6.37e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.83 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1061 EKAK-NLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLakkEEELQAVLAR 1139
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1140 GDEEVAQknnALKQLRELQAQLA------ELQEDLESEKAARNKAEKLKRDLSEELEALK 1193
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYasvkahELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1405-1971 |
6.80e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.84 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1405 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEekaiafDKLEKTKNRLQQELDDLMVDLDHQRQIV 1484
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1485 SNLEKKQKKFDQMLAEEKtisARYAEERD--RAEAEAREKDTKALsmaraLDEALEAKEEFERLnKQLRAEmedliSSKD 1562
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKAL-----TGKHQDVTAKYNRR-RSKIKE-----QNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1563 DVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlEVNMQamkaqfdrdlQARDEQNEEKKRALVKQVREM 1642
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL-EFNEE----------EYRLKSRLGELKLRLNQATAT 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1643 EAELEDERKQRALAVAAKKKLEMDLKDVE-AQIE--AANKARDEAIKQLRKLQAQMKDYQRELEEARTsrdEIFTQSKEN 1719
Cdd:pfam12128 460 PELLLQLENFDERIERAREEQEAANAEVErLQSElrQARKRRDQASEALRQASRRLEERQSALDELEL---QLFPQAGTL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1720 EKKLKSLEAEILQLQEDLASSE---RARRHAEQERDELADEISNSASGkaalLDEKR-----------RLEARIAQLEEE 1785
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPEllhRTDLDPEVWDGSVGGELNLYGVK----LDLKRidvpewaaseeELRERLDKAEEA 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1786 LEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKiL 1865
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ-L 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1866 QLEEQLEQEAKERAAANKIVRRTEK--KLKEVfmqVEDERRHADQYKEQMEKANSrmkQLKRQLEEAEEEATRANASRrk 1943
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKqaYWQVV---EGALDAQLALLKAAIAARRS---GAKAELKALETWYKRDLASL-- 763
|
570 580
....*....|....*....|....*...
gi 688558683 1944 lqrelDDATEASEGLSREVNTLKNRLRR 1971
Cdd:pfam12128 764 -----GVDPDVIAKLKREIRTLERKIER 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1007-1163 |
7.82e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1007 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknLGKVKNKQEMmmvdleERLKK 1086
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEY------EALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1087 EEKTrqeLEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1163
Cdd:COG1579 97 EIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1284-1949 |
9.17e-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: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1284 LQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADrthKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQE 1363
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE---EIQENKDLIK--ENNATRHLCNLLKETCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1364 LLQEETRQ-KLNLSSRIrqleeEKNNLLEQQEEEEESRKNLEKQLatlqaqlvetkkKLEDDVGALEGLEEVKRKLQKDm 1442
Cdd:pfam05483 176 YEREETRQvYMDLNNNI-----EKMILAFEELRVQAENARLEMHF------------KLKEDHEKIQHLEEEYKKEIND- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1443 evtsqklEEKAIAFDKLEKTKNrlQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEARek 1522
Cdd:pfam05483 238 -------KEKQVSLLLIQITEK--ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1523 dtKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAted 1601
Cdd:pfam05483 307 --RSMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI--- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1602 aklrlevnmqamkaqFDRDLQARDEQNEEkkraLVKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKAR 1681
Cdd:pfam05483 382 ---------------ITMELQKKSSELEE----MTKFKNNKEVELEELKK----ILAEDEKLLDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1682 DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNS 1761
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1762 ASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1841
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1842 LQELEGSVKSKFKasiaaleaKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMK 1921
Cdd:pfam05483 596 CNNLKKQIENKNK--------NIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
650 660
....*....|....*....|....*...
gi 688558683 1922 QLKRQLEEAEEEATRANASRRKLQRELD 1949
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1548-1764 |
9.60e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1548 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdlQARDEQ 1627
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1628 NEEKKR-------------ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQ 1694
Cdd:COG3883 97 RSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1695 MKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1764
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1671-1894 |
1.00e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1671 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLasserarrhaEQE 1750
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1751 RDELADEI------SNSASGKAALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAqks 1824
Cdd:COG3883 85 REELGERAralyrsGGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1825 ENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1894
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
892-1381 |
1.05e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 892 EEEMQAKDEELIKVKErqvkvenELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVA---KKQELEEILHDL 968
Cdd:PRK01156 189 EEKLKSSNLELENIKK-------QIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSledMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 969 ESRVEEEEERN---QSLQNEKKKMQS--------HIQDLEEQLDEEEAARQKLQ---LEKVTAEAKIKKMEEdillLEDQ 1034
Cdd:PRK01156 262 ESDLSMELEKNnyyKELEERHMKIINdpvyknrnYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1035 NSKFLKEKKLLEDRVGEMT----------SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAE 1104
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1105 TTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG----------------------------DEEVAQKNNALKQLRE 1156
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhiinhynekksrlEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1157 LQAQLAELQEDLESEKAARNKAEKLKrdlseeLEALKTELEDTLDTTAAQQELRSKREQEVAELKKA-IDDETRNHESQI 1235
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1236 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN-----------KELTNEVKSLQQAKSESEHKRKKLEA---- 1300
Cdd:PRK01156 572 NALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFpddksyidksiREIENEANNLNNKYNEIQENKILIEKlrgk 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1301 --QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDA-------EKKGIKLTKDVSSLESQLQDTQELLQ--EET 1369
Cdd:PRK01156 652 idNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTIEILRTRINELSDRINDINETLEsmKKI 731
|
570
....*....|..
gi 688558683 1370 RQKLNLSSRIRQ 1381
Cdd:PRK01156 732 KKAIGDLKRLRE 743
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
835-1297 |
1.14e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.82 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 835 QSVCRGYLARkafAKKQQQLSALKVLQRNCAAY-----LKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVKErq 909
Cdd:TIGR00618 419 FRDLQGQLAH---AKKQQELQQRYAELCAAAITctaqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL-- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 910 vKVENELVEMER---KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEK 986
Cdd:TIGR00618 494 -ARLLELQEEPCplcGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 987 KKMQSHIQDLEEQLDEEEAARQKLQLE-KVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1065
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLtEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1066 LGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAKKEEELQAVLARGDE 1142
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEmlaQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1143 EVAQKNNALKQ-LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1221
Cdd:TIGR00618 733 DLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1222 KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKK 1297
Cdd:TIGR00618 813 PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----QLTQEQAKIIQLSDKLNGINQI 884
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1277-1659 |
1.14e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 53.15 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1277 LTNEVKSLQQAKSESEhkrkKLEAQLQEVMArfsEGEKVKGELADRTHKIQT---ELDNVSCLLEDAEKKGIKLTKDVSS 1353
Cdd:pfam19220 36 IEAILRELPQAKSRLL----ELEALLAQERA---AYGKLRRELAGLTRRLSAaegELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1354 LESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeeesRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE 1433
Cdd:pfam19220 109 LRIELRDKTAQAEALERQLAAETEQNRALEEE--------------NKALREEAQAAEKALQRAEGELATARERLALLEQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1434 VKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERD 1513
Cdd:pfam19220 175 ENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQ-----------------AERERAEAQLEEAVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1514 RAEAEARekdtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE 1593
Cdd:pfam19220 238 AHRAERA-------SLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1594 DELQATEDAKLRLEVNMQAM-KAQFDRD------------LQARDEQ----NEEKKRALVKQVREMEAELEDERKQRALA 1656
Cdd:pfam19220 311 QQFQEMQRARAELEERAEMLtKALAAKDaaleraeeriasLSDRIAEltkrFEVERAALEQANRRLKEELQRERAERALA 390
|
...
gi 688558683 1657 VAA 1659
Cdd:pfam19220 391 QGA 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1457-1670 |
1.49e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1457 DKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1520
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1521 EKDTKALSMARALDEALEAKEEFERLNKQLR---------AEMEDLISSKDDVGKnvhelekskrtLEQQVEEMRTQLEE 1591
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITK-----------IKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1592 LEDELQatEDAKLRLEVNMQAMKAqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1670
Cdd:PHA02562 318 LDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1441-1660 |
1.69e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1441 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEA 1519
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1520 REKDT----KALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1595
Cdd:COG3883 97 RSGGSvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1596 LQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1660
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1020-1228 |
1.81e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.01 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1020 KIKKMEEDILL-LEDQNSKFLKE-------------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK--------QEMMM 1077
Cdd:PRK05771 2 APVRMKKVLIVtLKSYKDEVLEAlhelgvvhiedlkEELSNERLRKLRSLLTKLSEALDKLRSYLPKlnplreekKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1078 VDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK------------------------IQLAKKEEEL 1133
Cdd:PRK05771 82 KSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfkyvsvfvgtVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1134 QAVLARGDEEVAQKNN---------------ALKQLRELQAQLAELQEDLESEKAARNKAEKLKR------DLSEELEAL 1192
Cdd:PRK05771 162 LESDVENVEYISTDKGyvyvvvvvlkelsdeVEEELKKLGFERLELEEEGTPSELIREIKEELEEiekereSLLEELKEL 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 688558683 1193 KTELEDTLdtTAAQQELRSKREQEVAELKKAIDDET 1228
Cdd:PRK05771 242 AKKYLEEL--LALYEYLEIELERAEALSKFLKTDKT 275
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
891-1114 |
1.96e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 891 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELEEILH 966
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 967 DLESRVEEEEERNQSLQneKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE--AKIKKMEEDILLLEDQNSKFLKEKKL 1044
Cdd:COG4942 98 ELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArrEQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1045 LEdrvgemtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1114
Cdd:COG4942 176 LE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1133-1362 |
2.53e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1133 LQAVLARGDEEVAQKNNALKQLRE----LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQE 1208
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA------EAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1209 LRSKREQevaeLKKaiddetRNHESQIQEMRQRHGTAL---EEISEQLEQAKRVKGNLEKNKQTLE---SDNKELTNEVK 1282
Cdd:COG3883 81 IEERREE----LGE------RARALYRSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADADLLEelkADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1283 SLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1362
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1080-1648 |
2.57e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.88 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1080 LEERLKKEEKTRQELEKAKRKLDAETT-------DLQDQIAELQAQIDELKIQLAKKE--EELQAVLARGDEEVAQKNNA 1150
Cdd:PRK10246 299 IQEQSAALAHTRQQIEEVNTRLQSTMAlrarirhHAAKQSAELQAQQQSLNTWLAEHDrfRQWNNELAGWRAQFSQQTSD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1151 LKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE---LEDTLDTTAAQQELRSKREQEVAELKKAIDDE 1227
Cdd:PRK10246 379 REQLRQWQQQLTHAEQKLNALPAI---TLTLTADEVAAALAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1228 TRNHESQIQEMRQRHGTALEEISEQ---LEQAKRVKgNLEKNKQTLESDNK-----ELTNEVKSLQQAKSESEHKRKkLE 1299
Cdd:PRK10246 456 QTQRNAALNEMRQRYKEKTQQLADVktiCEQEARIK-DLEAQRAQLQAGQPcplcgSTSHPAVEAYQALEPGVNQSR-LD 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1300 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELL-----QEETRQKLN 1374
Cdd:PRK10246 534 ALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldaQEEHERQLR 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1375 LSSRIRQLEEEKNNLleqqeeeeesrknlEKQLATLQAQLVETKKKLEDDVGAL------EGLEEvkrKLQKDMEVTSQK 1448
Cdd:PRK10246 614 LLSQRHELQGQIAAH--------------NQQIIQYQQQIEQRQQQLLTALAGYaltlpqEDEEA---SWLATRQQEAQS 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1449 LEEKAIAFDKLEKTKNRLQQELDDL--MVDLDHQRQIVSnLEKKQKKFDQML---AEEKTISARYAEERDRAeAEAREKD 1523
Cdd:PRK10246 677 WQQRQNELTALQNRIQQLTPLLETLpqSDDLPHSEETVA-LDNWRQVHEQCLslhSQLQTLQQQDVLEAQRL-QKAQAQF 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1524 TKALSMARALDealeaKEEFerlnkqLRAEMEDlisskddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA----- 1598
Cdd:PRK10246 755 DTALQASVFDD-----QQAF------LAALLDE---------ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQhqqhr 814
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1599 ------TEDAKlRLEVNMQAMKAQFdRDLQAR----------DEQNEEKKRALVKQVREMEAELED 1648
Cdd:PRK10246 815 pdgldlTVTVE-QIQQELAQLAQQL-RENTTRqgeirqqlkqDADNRQQQQALMQQIAQATQQVED 878
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1570-1746 |
3.14e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1570 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDlqaRDEQNEEKKralVKQVREMEAELEDE 1649
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRN---NKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1650 RKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAqmkdyqrELEEARTSRDEIFTQSKENEKKLKSLEAE 1729
Cdd:COG1579 102 KRRIS-------DLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|....*....
gi 688558683 1730 ILQL--QEDLASSERARRH 1746
Cdd:COG1579 168 LAAKipPELLALYERIRKR 186
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1076-1457 |
3.19e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1076 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLR 1155
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1156 ELQAQLAELQEDLESekaarnkaeklkrdLSEELEALKTELEDTLDTtaAQQELRSKREQEvaELKKAIDDETRNHESQI 1235
Cdd:pfam07888 126 AHEARIRELEEDIKT--------------LTQRVLERETELERMKER--AKKAGAQRKEEE--AERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1236 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTL------ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1309
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1310 SEGE-----------KVKGELADRTHKIQTELDNVS----CLLEDAEKKGIKLTKdvssLESQLQDTQELLQEETRQKLN 1374
Cdd:pfam07888 268 DRTQaelhqarlqaaQLTLQLADASLALREGRARWAqereTLQQSAEADKDRIEK----LSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1375 LSSrirQLEEEKnnlLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKdmeVTSQKLEEKAI 1454
Cdd:pfam07888 344 LEV---ELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET---VADAKWSEAAL 414
|
...
gi 688558683 1455 AFD 1457
Cdd:pfam07888 415 TST 417
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1470-1848 |
3.27e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1470 LDDLMVDLDHQRQIvsNLEKKQKKFDQMlaeektisaryAEERDRAEaeaREKDTKALSMARALDEALEAKEEFERLNKQ 1549
Cdd:pfam17380 271 LNQLLHIVQHQKAV--SERQQQEKFEKM-----------EQERLRQE---KEEKAREVERRRKLEEAEKARQAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1550 LRAEMEDLisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlevnmqamkaQFDRDLQARDEQNE 1629
Cdd:pfam17380 335 IYAEQERM------------AMERERELERIRQEERKRELERIRQEEIAMEISRMR----------ELERLQMERQQKNE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1630 ekkralvkQVREmeaELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1709
Cdd:pfam17380 393 --------RVRQ---ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1710 DEIFTQsKENEKKLKSLEAEILQLQEDLASSERaRRHAEQERDEladeisnsasGKAALLDEKRR---LEARIAQLEEEL 1786
Cdd:pfam17380 462 VERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEE----------RKQAMIEEERKrklLEKEMEERQKAI 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1787 EEEQSNMELLNDRFRKTTM----QVDTLNTELAGERSAAQKSENARQQLeRQNKDLKSKLQELEGS 1848
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
1079-1192 |
3.39e-06 |
|
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.
Pssm-ID: 464151 [Multi-domain] Cd Length: 295 Bit Score: 51.10 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1079 DLEERLK--KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL----------------------- 1133
Cdd:pfam14362 107 EIDRELLeiQQEEADAAKAQLAAAYRARLAELEAQIAALDAEIDAAEARLDALQAEArceldgtpgtgtgvpgdgpvakt 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 1134 -QAVLARGDEEVAQ-KNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1192
Cdd:pfam14362 187 kQAQLDAAQAELAAlQAQNDARLAALRAELARLTAERAAARARSQAAIDGDDGLLARLEAL 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1724-1968 |
3.49e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1724 KSLEAEILQLQEDLASSERARRHAEQERDeladeisnsasgKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1803
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDARE------------QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1804 tmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEeqleqeaKERAAANK 1883
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE-------RELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1884 IVRRTEKKLKEVFMQVEDErrhADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDateasegLSREVN 1963
Cdd:COG4913 360 RRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 688558683 1964 TLKNR 1968
Cdd:COG4913 430 SLERR 434
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1013-1522 |
4.03e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.05 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1013 EKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQ 1092
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK----------YLEALNKKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1093 ELEKAKRKLDAettdLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE------ 1166
Cdd:pfam05557 98 QLADAREVISC----LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrik 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1167 -----------------DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETR 1229
Cdd:pfam05557 174 elefeiqsqeqdseivkNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1230 NH--ESQIQE---MRQRHGTAL---EEISEQLEQakrvkgnLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1301
Cdd:pfam05557 254 KEklEQELQSwvkLAQDTGLNLrspEDLSRRIEQ-------LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1302 LQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLED------AEKKGIKLTKDVSSLESQLQDTQ-----------EL 1364
Cdd:pfam05557 327 IEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydkeltMSNYSPQLLERIEEAEDMTQKMQahneemeaqlsVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1365 LQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR-KNLEKQLATLQAQLvetkKKLEDDVGALEgLEEVKRKLQKDME 1443
Cdd:pfam05557 407 EEELGGYKQQAQTLERELQALRQQESLADPSYSKEEvDSLRRKLETLELER----QRLREQKNELE-MELERRCLQGDYD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1444 VTSQK---LEEKAIAfdkleKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERdRAEAEAR 1520
Cdd:pfam05557 482 PKKTKvlhLSMNPAA-----EAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL-RKELESA 555
|
..
gi 688558683 1521 EK 1522
Cdd:pfam05557 556 EL 557
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1734-1972 |
4.58e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1734 QEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTE 1813
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1814 LAGERSAAQKSENARQQLERQNKdLKSKLQeleGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLK 1893
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1894 EVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRRG 1972
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1112-1351 |
5.01e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 52.14 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1112 IAELQAQIDELKIQLAKKEEELQAvlaRGDEEVAQKNNA-LKQlrELQAQLAEL---QEDLES-EKAARNKAEKLKRD-L 1185
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNA---LADKERAEADRQrLEQ--EKQQQLAAIsgsQSQLEStDQNALETNGQAQRDaI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1186 SEELEALKTELE------DTLDTTAAQQELRSK--REQEVAELKKAID---DETRNHES-QIQEMRQRHGTALEEISEQL 1253
Cdd:NF012221 1612 LEESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQeqlDDAKKISGkQLADAKQRHVDNQQKVKDAV 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1254 EQAKRVKGNLEKNKQTLESDnkeltnevksLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1333
Cdd:NF012221 1692 AKSEAGVAQGEQNQANAEQD----------IDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENK 1761
|
250
....*....|....*...
gi 688558683 1334 SCLLEdAEKKGIKLTKDV 1351
Cdd:NF012221 1762 ANQAQ-ADAKGAKQDESD 1778
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
925-1383 |
5.29e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 925 QLLEEKNILaEQLQAETELfAEAEEMRARLvakkqELEEILHDLESRVEEEEERNQSLQNEKKKMQshiQDLEEQLDEEE 1004
Cdd:pfam05557 3 ELIESKARL-SQLQNEKKQ-MELEHKRARI-----ELEKKASALKRQLDRESDRNQELQKRIRLLE---KREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1005 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMmmvdLEERL 1084
Cdd:pfam05557 73 EQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL----LKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1085 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEE-----ELQAVLARGDEEVAQKNNALKQLRELQA 1159
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSElaripELEKELERLREHNKHLNENIENKLLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1160 QLAELQEDLESEKAARNKAEKL---KRDLSEELEALKTELEDTLDTTAAQQELRSK------REQEVAELKKAIDDETRN 1230
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLeleKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqREIVLKEENSSLTSSARQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1231 HESQIQEMRQRHGTALEEISE---QLEQAKRVKGNLEKN-----------KQTLESDNKELTNEVKSLQQAK--SESEHK 1294
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDlnkKLKRHKALVRRLQRRvllltkerdgyRAILESYDKELTMSNYSPQLLEriEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1295 RKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLN 1374
Cdd:pfam05557 389 TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNE 466
|
....*....
gi 688558683 1375 LSSRIRQLE 1383
Cdd:pfam05557 467 LEMELERRC 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1523-1767 |
6.82e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1523 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL------ 1596
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1597 -QATEDAKLRLEV------------NMQAMKAQFDRDLQARDEQNEEKKralvkQVREMEAELEDERKQralAVAAKKKL 1663
Cdd:COG3883 95 lYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKA-----ELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1664 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1743
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260
....*....|....*....|....
gi 688558683 1744 RRHAEQERDELADEISNSASGKAA 1767
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1059-1193 |
7.79e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1059 EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL--KIQLAKKEEELQav 1136
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLerELSEARSEERRE-- 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 1137 lARGDEEVAQKNNALKQLR----ELQAQLAELQEDLESEKAARNKaeklkrDLSEELEALK 1193
Cdd:COG2433 461 -IRKDREISRLDREIERLEreleEERERIEELKRKLERLKELWKL------EHSGELVPVK 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
905-1201 |
8.54e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 905 VKERQVKVEnelvEMERKHQQLLEEKNILAEQLQAETELfAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQN 984
Cdd:PRK02224 470 IEEDRERVE----ELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 985 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIllledqnskflkekklleDRVGEMTSQLAEEEEKAK 1064
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI------------------ESLERIRTLLAAIADAED 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1065 NLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDlqDQIAELQAQIDELKIQLAKKEEELQAVLARGDE-- 1142
Cdd:PRK02224 607 EIERLREKRE----ALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDlq 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1143 -EVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLK---RDLSEEL-----EALKTELEDTLD 1201
Cdd:PRK02224 681 aEIGAVENELEELEELRERREALENRVEALEALYDEAEELEsmyGDLRAELrqrnvETLERMLNETFD 748
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
938-1176 |
9.24e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 938 QAETELFAEAEEMRArLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTA 1017
Cdd:COG3883 13 FADPQIQAKQKELSE-LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1018 EAKIKKMEE-------------------DILLLEDQNSKFLKEKKLLeDRVGEMTSQLAEEEEKAKNlgKVKNKQEmmmv 1078
Cdd:COG3883 78 EAEIEERREelgeraralyrsggsvsylDVLLGSESFSDFLDRLSAL-SKIADADADLLEELKADKA--ELEAKKA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1079 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQ 1158
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|....*...
gi 688558683 1159 AQLAELQEDLESEKAARN 1176
Cdd:COG3883 231 AAAAAAAAAAAAAASAAG 248
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1571-1775 |
9.48e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1571 LEKSK-RTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1649
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1650 RKQRALAVAAKKKLEMDLKDVEAQIEAANK----------------ARDEAIKQLRKLQAQMKDYQRELEEARTSRDE-- 1711
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1712 -IFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRL 1775
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1088-1364 |
9.70e-06 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 50.08 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1088 EKTRQELEKAkRKLDAETTD----LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1163
Cdd:pfam04108 17 TDARSLLEEL-VVLLAKIAFlrrgLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1164 LQE-----------DLESEKAARNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKreQEVAELKKAIDDETRNH 1231
Cdd:pfam04108 96 PPGeekqktlldfiDEDSVEILRDALKELIDELQAAQESLDSDLKRfDDDLRDLQKELESL--SSPSESISLIPTLLKEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1232 ESQIQEMRQRhgtaLEEIS---EQLEQAKRV-KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA 1307
Cdd:pfam04108 174 ESLEEEMASL----LESLTnhyDQCVTAVKLtEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNS 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1308 RFSEGEKVKGELADrthkIQTELDN-VSCLLEDAEkkgiKLTKDVSSLESQLQDTQEL 1364
Cdd:pfam04108 250 LIDELLSALQLIAE----IQSRLPEyLAALKEFEE----RWEEEKETIEDYLSELEDL 299
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1075-1348 |
1.03e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1075 MMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQL 1154
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1155 RELQAQLAELQEDLESEKAARNKAEKLKRD---LSEELEALKTELEDTLDTTAAQQEL--RSKR-EQEVAELKKAID--D 1226
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEknE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1227 ETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE---LTNEVKSLQQAKSESEHKRKKLEAQLQ 1303
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEadeLHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 688558683 1304 EVMArfSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLT 1348
Cdd:COG1340 241 ELRK--ELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLT 283
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1080-1255 |
1.04e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 48.03 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1080 LEERLKKEEKTRQELEK-----AKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLArgdeevaqknnalKQL 1154
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLG-------------QNV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1155 RELQAQLAELQEDLesEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ-----QELRSKREQEVAELKKAIDDETR 1229
Cdd:pfam01442 69 EELRQRLEPYTEEL--RKRLNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*.
gi 688558683 1230 NHESQIQEMRQRHGTALEEISEQLEQ 1255
Cdd:pfam01442 147 EVQAQLSQRLQELREKLEPQAEDLRE 172
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1038-1384 |
1.10e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 50.34 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1038 FLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQA 1117
Cdd:COG5185 171 ELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1118 QIDELKIQLAKKEEELQAVLARGDEEVA----QKNNALKQLRELQAQLAELQEDLESEKA------------ARNKAEKL 1181
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGENAESSKrlneNANNLIKQFENTKEKIAEYTKSIDIKKAtesleeqlaaaeAEQELEES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1182 KRDLSEELEALKTELEDTLDT-TAAQQELRSKREQEVAELKKAIDDET-RNHESQIQEMRQRHGTALEEiseQLEQAKRV 1259
Cdd:COG5185 331 KRETETGIQNLTAEIEQGQESlTENLEAIKEEIENIVGEVELSKSSEElDSFKDTIESTKESLDEIPQN---QRGYAQEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1260 KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKiqteldnvSCLLED 1339
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEIN--------RSVRSK 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 688558683 1340 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1384
Cdd:COG5185 480 KEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAE 524
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1101-1316 |
1.23e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1101 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1180
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY---DELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1181 LKRDLSEELEALKTEL----EDTLDTTAAQQ-----ELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRhgtaLEEISE 1251
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQisegpDRITKIKDKLKELQHSLEKL----DTAIDELEEI----MDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1252 QLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1316
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLitlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1626-1778 |
1.23e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1626 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE--------AANKARD----EAIKQLRKLQA 1693
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREdlarEALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1694 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK- 1772
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK----KDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174
|
....*.
gi 688558683 1773 RRLEAR 1778
Cdd:COG1842 175 EEMEAR 180
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
698-722 |
1.31e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.31e-05
10 20
....*....|....*....|....*
gi 688558683 698 YKESLTKLMATLRNTNPNFVRCIIP 722
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
942-1578 |
1.32e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 942 ELFAEAEEMRaRLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKI 1021
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1022 KKMEEDILLLED---QNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqemmmvDLEERLKKEEKTRQeleKAK 1098
Cdd:PRK01156 228 NNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYK-----------ELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1099 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ--AVLARGDEEVAQKNnalKQLRELQAQLAELQEDLESEKAARN 1176
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKK---SRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1177 KAEKLK---RDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQL 1253
Cdd:PRK01156 371 SIESLKkkiEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNM 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1254 ------------------EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA-QLQEVMARFSEGEK 1314
Cdd:PRK01156 447 emlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1315 VKGELADRTHKIQTeldnvsclLEDAEKKGIKLTKDVSSLEsqlqdtQELLQEETRQKLNLSSRIRQLEEEknnlleqqe 1394
Cdd:PRK01156 527 ARADLEDIKIKINE--------LKDKHDKYEEIKNRYKSLK------LEDLDSKRTSWLNALAVISLIDIE--------- 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1395 eeeesrknlekqlaTLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNrlqqELDDLM 1474
Cdd:PRK01156 584 --------------TNRSRSNEIKKQLND---LESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN----EIQENK 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1475 VDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEaearekdtkalSMARALDEALEAKEEFERLNKQLRAEM 1554
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLK-----------KSRKALDDAKANRARLESTIEILRTRI 711
|
650 660
....*....|....*....|....
gi 688558683 1555 EDLISSKDDVGKNVHELEKSKRTL 1578
Cdd:PRK01156 712 NELSDRINDINETLESMKKIKKAI 735
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1094-1250 |
1.40e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 49.34 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1094 LEKAKRKLDAETTDLQDQIAELQAQIDelkiQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKA 1173
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1174 ARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQE-LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEIS 1250
Cdd:pfam00529 132 LAPIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1511-1953 |
1.60e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1511 ERDRAEAEAREKDTKALsmARALDEALEAKEEFERLNKQLRAEMEDLisskdDVGKNVHELEKSKRTLEQQVEEMRTQLE 1590
Cdd:COG4717 77 EEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1591 ELEDELQATEDaklrLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1670
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1671 EAQIEA-ANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEK--------------KLKSLEAEILQLQE 1735
Cdd:COG4717 226 EEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1736 DLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELA 1815
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1816 GERSAAQKSEnARQQLERQNKDLKSKLQELEGSVKSKFKA-SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKe 1894
Cdd:COG4717 386 ELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELE- 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1895 vfmQVEDERRHADQYKEQmekansrmKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1953
Cdd:COG4717 464 ---QLEEDGELAELLQEL--------EELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1163-1423 |
1.68e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1163 ELQEDLESEK--AARNKAEKLK-RDLSEELEALKTELEDTLDTTAAQQ----ELRSKREQEVAELKKAIDD---ETRNHE 1232
Cdd:PHA02562 154 KLVEDLLDISvlSEMDKLNKDKiRELNQQIQTLDMKIDHIQQQIKTYNknieEQRKKNGENIARKQNKYDElveEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1233 SQIqemrqrhgtalEEISEQLEqakrvkgNLEKNKQTLESDNKELTNEvkslqQAKSESEHKRKKLEAQLQE-------V 1305
Cdd:PHA02562 234 AEI-----------EELTDELL-------NLVMDIEDPSAALNKLNTA-----AAKIKSKIEQFQKVIKMYEkggvcptC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1306 MARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI---KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1382
Cdd:PHA02562 291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDefnEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 688558683 1383 EEEknnlleqqeeeeesRKNLEKQLATLQAQLVETKKKLED 1423
Cdd:PHA02562 371 QAE--------------FVDNAEELAKLQDELDKIVKTKSE 397
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
960-1600 |
1.86e-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: 50.05 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 960 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEqldeeeaarQKLQLEKVTAEA-------KIKKMEEDILLLE 1032
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA---------QINDLEDVADKAisnddpeEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1033 DQNSKFLKEKKLLEDRVGEM-TSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1111
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIeKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEI 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1112 IAELQAQIDelkiqlAKKEEELQAVLARGDEE---VAQKNNalkqlrelqaqlaelqedlESEKAARNKAEKLKRDLSEE 1188
Cdd:TIGR01612 1263 ENEMGIEMD------IKAEMETFNISHDDDKDhhiISKKHD-------------------ENISDIREKSLKIIEDFSEE 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1189 --LEALKTELEDTLDTTAAQQELRSKREQEVAELK--------KAIDDETRNHESQIQEMRQRHGTALEEiSEQLEQAKR 1258
Cdd:TIGR01612 1318 sdINDIKKELQKNLLDAQKHNSDINLYLNEIANIYnilklnkiKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLIKKIK 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1259 VKGNLEKNKQTLES--DNKELTNEVKSLQQAKSEsehkrkkleaqlqevmarfsegekvkgeladrthkIQTELDNVSCL 1336
Cdd:TIGR01612 1397 DDINLEECKSKIEStlDDKDIDECIKKIKELKNH-----------------------------------ILSEESNIDTY 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1337 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQlatlqaqlv 1415
Cdd:TIGR01612 1442 FKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNdHDFNINELKEHIDKSKGCKDEADKNAKAIEKN--------- 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1416 etkkkleddvgaleglEEVKRKLQKDMEVTSQKLEEKAIAfDKLEKTKNRLQQELDDLMvdlDHQRQIVSNLEKKQKKFD 1495
Cdd:TIGR01612 1513 ----------------KELFEQYKKDVTELLNKYSALAIK-NKFAKTKKDSEIIIKEIK---DAHKKFILEAEKSEQKIK 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1496 QMLAEEKTISARYAEERDRAEA------EAREKDTKALSMARALDEALEAKEEFERLNKQLRA----EMEDLISSKDDVG 1565
Cdd:TIGR01612 1573 EIKKEKFRIEDDAAKNDKSNKAaidiqlSLENFENKFLKISDIKKKINDCLKETESIEKKISSfsidSQDTELKENGDNL 1652
|
650 660 670
....*....|....*....|....*....|....*
gi 688558683 1566 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1600
Cdd:TIGR01612 1653 NSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
903-1924 |
2.11e-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: 50.05 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 903 IKVKERQVKVENELVEMERKHQQLLEEKNILAEQLqAETELFAEAEEMRAR---LVAKKQELEEILHD--------LESR 971
Cdd:TIGR01612 605 LKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDEL-AKISPYQVPEHLKNKdkiYSTIKSELSKIYEDdidalyneLSSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 972 VEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlekvtaeAKIKKMEEDILLLEDQNSKFLKEKklLEDRVGE 1051
Cdd:TIGR01612 684 VKENAIDNTEDKAKLDDLKSKIDKEY---------------------DKIQNMETATVELHLSNIENKKNE--LLDIIVE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1052 MTSQLAEE--EEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAelqaqIDELKIQLAK- 1128
Cdd:TIGR01612 741 IKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN-----IDNIKDEDAKq 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1129 ---KEEELQAVLARGDEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDtldttaa 1205
Cdd:TIGR01612 812 nydKSKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD------- 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1206 qqELRSKREQEVAELKKAIDDETRNHESQIQEMrqrhgTALEEISEQLEQAKRVKGNLEK--NKQTL--ESDNKEL---- 1277
Cdd:TIGR01612 883 --DKLNDYEKKFNDSKSLINEINKSIEEEYQNI-----NTLKKVDEYIKICENTKESIEKfhNKQNIlkEILNKNIdtik 955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1278 -TNEVK---------SLQQAKSESEHKRKKL-----EAQLQEVMARFSEGEKVKGElaDRTHKIQTELDNVSCLLEDAEK 1342
Cdd:TIGR01612 956 eSNLIEksykdkfdnTLIDKINELDKAFKDAslndyEAKNNELIKYFNDLKANLGK--NKENMLYHQFDEKEKATNDIEQ 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1343 KGIKLTKDVSS---------------LESQLQDTQELLQEETRQKLNLS----SRIRQ----------LEEEKNNLLEQQ 1393
Cdd:TIGR01612 1034 KIEDANKNIPNieiaihtsiyniideIEKEIGKNIELLNKEILEEAEINitnfNEIKEklkhynfddfGKEENIKYADEI 1113
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1394 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVgaleglEEVKRKLQKDMEVTsqkleEKAIAFDKLEKTKNRLQqeldDL 1473
Cdd:TIGR01612 1114 NKIKDDIKNLDQKIDHHIKALEEIKKKSENYI------DEIKAQINDLEDVA-----DKAISNDDPEEIEKKIE----NI 1178
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1474 MVDLDHQRQIVSNLEK------KQKKFDQMLAEEKTISARYAE-------ERDRAEAEAREKDTKAL-SMARALDEALEA 1539
Cdd:TIGR01612 1179 VTKIDKKKNIYDEIKKllneiaEIEKDKTSLEEVKGINLSYGKnlgklflEKIDEEKKKSEHMIKAMeAYIEDLDEIKEK 1258
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1540 KEEFER---LNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNM-QAMKA 1615
Cdd:TIGR01612 1259 SPEIENemgIEMDIKAEMETFNISHDDD-KDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLlDAQKH 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1616 QFDRDLQARDEQN------EEKKRALVKQVREMEAELEDERKQ------RALAVAAKKKLEMDLKDVEAQIEAA--NKAR 1681
Cdd:TIGR01612 1338 NSDINLYLNEIANiynilkLNKIKKIIDEVKEYTKEIEENNKNikdeldKSEKLIKKIKDDINLEECKSKIESTldDKDI 1417
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1682 DEAIKQLRKLQAQMkdyqreLEEaRTSRDEIFTQSKENEKKL----KSLE------AEILQLQEDLASSERARRHAE-QE 1750
Cdd:TIGR01612 1418 DECIKKIKELKNHI------LSE-ESNIDTYFKNADENNENVlllfKNIEmadnksQHILKIKKDNATNDHDFNINElKE 1490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1751 RDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN--DRFRKTTMQVD----------TLNTELAGER 1818
Cdd:TIGR01612 1491 HIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNkfAKTKKDSEIIIkeikdahkkfILEAEKSEQK 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1819 SAAQKSENARQQLERQNKDLKSK----LQELEGSVKSKFkASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK--- 1891
Cdd:TIGR01612 1571 IKEIKKEKFRIEDDAAKNDKSNKaaidIQLSLENFENKF-LKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKeng 1649
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 688558683 1892 -----LKEVFMQVEDERRHADQYKEQMEKANSRMKQLK 1924
Cdd:TIGR01612 1650 dnlnsLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1428-1925 |
2.14e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.75 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1428 LEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK-KQKKFD--QMLAEEKTI 1504
Cdd:pfam07111 75 LRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEgSQRELEeiQRLHQEQLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1505 SARYAEERDRA----EAEAREKDTKALSMARA--LDEALEAKEEFERLNKQLRAEMEDLISS------------------ 1560
Cdd:pfam07111 155 SLTQAHEEALSsltsKAEGLEKSLNSLETKRAgeAKQLAEAQKEAELLRKQLSKTQEELEAQvtlveslrkyvgeqvppe 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1561 ---------KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEK 1631
Cdd:pfam07111 235 vhsqtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1632 KRALVKQVREMEAELEDERKQRALAVAAKKK-----------LEMDLKDVEAQIEA--------------ANKAR----- 1681
Cdd:pfam07111 315 VFALMVQLKAQDLEHRDSVKQLRGQVAELQEqvtsqsqeqaiLQRALQDKAAEVEVermsakglqmelsrAQEARrrqqq 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1682 --DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL----------KSLEAEILQLQEDLASSERARRHAEQ 1749
Cdd:pfam07111 395 qtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQESCPPPPPAPP 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1750 ERDELADEISNSASGKAALlDEKRRLEARIAQLEEELEEEQSNMELLndRFRKTTMQVDT---------------LNTEL 1814
Cdd:pfam07111 475 VDADLSLELEQLREERNRL-DAELQLSAHLIQQEVGRAREQGEAERQ--QLSEVAQQLEQelqraqeslasvgqqLEVAR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1815 AGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqlEEQLEQEAKERAAANKIVRRT--EKKL 1892
Cdd:pfam07111 552 QGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQIQHRAtqEKER 628
|
570 580 590
....*....|....*....|....*....|...
gi 688558683 1893 KEVFMQVEDERRhadqyKEQMEKANSRMKQLKR 1925
Cdd:pfam07111 629 NQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
892-1260 |
2.58e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 49.37 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 892 EEEMQAKDEELIKVKERQV----KVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRAR--------LVAKKQ 959
Cdd:pfam09731 51 LGEDPPLAPKPKTFRPLQPsvvsAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE--KEATKDAAEakaqlpksEQEKEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 960 ELEEILHDLESRVEEEEERNQSLQNEKKK-MQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEDILLLEDQNSK 1037
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQaVKAHTDSLKEASDTAEISREKaTDSALQKAEALAEKLKEVINLAKQSEEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1038 FLKEKKLLEDRVGEMTS----QLAEEEEKAKNLGKVKNKqemmMVDLEErlKKEEKTRQELEK--------AKRKLDAET 1105
Cdd:pfam09731 209 AAPPLLDAAPETPPKLPehldNVEEKVEKAQSLAKLVDQ----YKELVA--SERIVFQQELVSifpdiipvLKEDNLLSN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1106 TDLQDQIAELQAQIDELKIQLA--KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLA--ELQEDLESEKAARNKAEKL 1181
Cdd:pfam09731 283 DDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRESY 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1182 KRDLSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNHESQIQEMRQRHG---TALEEISEQLEQAKR 1258
Cdd:pfam09731 363 EEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANLKgleKATSSHSEVEDENRK 441
|
..
gi 688558683 1259 VK 1260
Cdd:pfam09731 442 AQ 443
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1681-1846 |
2.68e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1681 RDEAIKQLRKLQAQMKDyQRELEEARTSrdeiftqskenekklkSLEAEILQLQEDLASSERARRHAEQERDELADEISn 1760
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGAGA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1761 SASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS 1840
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKIADLGR 179
|
170
....*....|....
gi 688558683 1841 KL--------QELE 1846
Cdd:PRK09039 180 RLnvalaqrvQELN 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1015-1219 |
2.96e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1015 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNL-GKVKNKQEmmmvDLEERLKKEEKTRQE 1093
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALqAEIDKLQA----EIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1094 LEKAKRK--------------LDAETTD-----------LQDQIAELQAQIDELKIQLAKKEEELQAVLArgdEEVAQKN 1148
Cdd:COG3883 88 LGERARAlyrsggsvsyldvlLGSESFSdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLA---ELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558683 1149 NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1219
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1512-1777 |
3.05e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1512 RDRAEAEAREKDTKALSMARALDEA---LEAKEEFERLNKQLRAEMEdlISSKDDVGKnvhELEKSKRTLEQQVEEMRTQ 1588
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEAldkLRSYLPKLNPLREEKKKVS--VKSLEELIK---DVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1589 LEELEDELQATEDAKLRLEVnmqaMKAqFDRDLQARDEQ----------NEEKKRALVKQVREMEAELEDERKQRALAVA 1658
Cdd:PRK05771 109 ISELENEIKELEQEIERLEP----WGN-FDLDLSLLLGFkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1659 AKKKlemdlkdveaqieaanKARDEAIKQLRKLqaqmkDYQR-ELEEARTSRDEIftqsKENEKKLKSLEAEILQLQEDL 1737
Cdd:PRK05771 184 VVLK----------------ELSDEVEEELKKL-----GFERlELEEEGTPSELI----REIKEELEEIEKERESLLEEL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 688558683 1738 ASSerarrhaeqeRDELADEISNSasgKAALLDEKRRLEA 1777
Cdd:PRK05771 239 KEL----------AKKYLEELLAL---YEYLEIELERAEA 265
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
886-1117 |
3.18e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 886 LQVTRQE------EEMQAKDEELIKVKERQVKVENELVEMERkhqqlleeknILAEQLQAETELFAEAEEMRARlvakkq 959
Cdd:pfam17380 383 LQMERQQknervrQELEAARKVKILEEERQRKIQQQKVEMEQ----------IRAEQEEARQREVRRLEEERAR------ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 960 ELEEI-LHDLESRVEEEEERNQSLQNEKKKMQshIQDLEEQLDEEEAARQKLqLEKVTAEAKIKKMEEDillledqnskf 1038
Cdd:pfam17380 447 EMERVrLEEQERQQQVERLRQQEEERKRKKLE--LEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEE----------- 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1039 lKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEM---MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAEL 1115
Cdd:pfam17380 513 -RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeerRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
..
gi 688558683 1116 QA 1117
Cdd:pfam17380 592 EA 593
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
890-1310 |
3.21e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 890 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL------LEEKNILAEQLQAETE-LFAEAEEMRARLVAKKQELE 962
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYnsylksIESLKKKIEEYSKNIErMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 963 EILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDillledqnskFLKEK 1042
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINH----------YNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1043 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVD-LEERLKKEEKTRQELEKAKRKLdAETTDLQDQIAELQAQIDE 1121
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKS 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1122 LKIQL--AKKEEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE 1195
Cdd:PRK01156 558 LKLEDldSKRTSWLNALAVISLIDIetnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSY---IDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1196 LEDTLDTTAAQQELRSKRE---QEVAElKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLES 1272
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDnykKQIAE-IDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRARLESTIEILRT 709
|
410 420 430
....*....|....*....|....*....|....*...
gi 688558683 1273 DNKELTNEVKSLQQaKSESEHKRKKLEAQLQEVMARFS 1310
Cdd:PRK01156 710 RINELSDRINDINE-TLESMKKIKKAIGDLKRLREAFD 746
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1433-1684 |
3.21e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1433 EVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisaryaeER 1512
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---------EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1513 DRAEAEAREKDTKALsMARALDEAleakeefERLNKQLRAEMedLISSKDdvgknVHELEKSKRTLEQQVEEMRTQLEEL 1592
Cdd:COG4942 91 EIAELRAELEAQKEE-LAELLRAL-------YRLGRQPPLAL--LLSPED-----FLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1593 E---DELQATEdaklrlevnmQAMKAQFDRDLQARDEQNEEKKR--ALVKQVREMEAELEDERKQRALAVAAKKKLEMDL 1667
Cdd:COG4942 156 RadlAELAALR----------AELEAERAELEALLAELEEERAAleALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*..
gi 688558683 1668 KDVEAQIEAANKARDEA 1684
Cdd:COG4942 226 EALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1225-1455 |
3.84e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1225 DDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQE 1304
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1305 VmarFSEGEKVK-----------GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEetrqkl 1373
Cdd:COG3883 95 L---YRSGGSVSyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1374 nLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKA 1453
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
..
gi 688558683 1454 IA 1455
Cdd:COG3883 245 SA 246
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1021-1248 |
4.16e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1021 IKKMEEDILLLE-------DQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMvDLEERLKKEEKTRQE 1093
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILE-EQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1094 LEKA-KRKLDAETTDLQDQIAELQAQIDELKIQLA--KKEEELQAVLargdeevaQKNNAL--KQLRELQAQLAELQEDL 1168
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIevAETEERVFKL--------EKERSLldASLRELESKFIVAQEDV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1169 esekaarNKAEKLKRD-LSEELEalktELEDTLDTTAAQ-----------QELRSKREQEVAELKKAiddETRNHESQIQ 1236
Cdd:PLN02939 288 -------SKLSPLQYDcWWEKVE----NLQDLLDRATNQvekaalvldqnQDLRDKVDKLEASLKEA---NVSKFSSYKV 353
|
250
....*....|..
gi 688558683 1237 EMRQRHGTALEE 1248
Cdd:PLN02939 354 ELLQQKLKLLEE 365
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1020-1334 |
4.31e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1020 KIKKMEEDILLLEDQNSK--FLKEKKLL----------EDRVGEMTSQLAE----EEEKAKNLGKVKNKQEMMMVD---- 1079
Cdd:PRK04778 80 SLPDIEEQLFEAEELNDKfrFRKAKHEIneieslldliEEDIEQILEELQEllesEEKNREEVEQLKDLYRELRKSllan 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1080 ----------LEERLKKEEKTRQELEKAK------------RKLDAETTDLQDQIA-----------ELQAQIDELKIQL 1126
Cdd:PRK04778 160 rfsfgpaldeLEKQLENLEEEFSQFVELTesgdyveareilDQLEEELAALEQIMEeipellkelqtELPDQLQELKAGY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1127 AKKEEE--------LQAVLARGDEEVAQKNNALKQLR--ELQAQLAELQED-------LESEKAARNKAEKLKRDLSEEL 1189
Cdd:PRK04778 240 RELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDldEAEEKNEEIQERidqlydiLEREVKARKYVEKNSDTLPDFL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1190 EALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---IDDETRNHE---SQIQEMrqrhgtaLEEISEQL 1253
Cdd:PRK04778 320 EHAKEQNKELKEEIDrvkqsytlNESELESVRqlEKQLESLEKQydeITERIAEQEiaySELQEE-------LEEILKQL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1254 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKL----------------EAQLQEVMARFSEG----E 1313
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSnlpglpedylemffevSDEIEALAEELEEKpinmE 472
|
410 420
....*....|....*....|.
gi 688558683 1314 KVKGELadrtHKIQTELDNVS 1334
Cdd:PRK04778 473 AVNRLL----EEATEDVETLE 489
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1337-1542 |
5.35e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1337 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVE 1416
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1417 TKKKLEDDVGA-----------------------LEGLEEVKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELDDL 1473
Cdd:COG3883 84 RREELGERARAlyrsggsvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKA----ELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1474 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEE 1542
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1480-1971 |
5.46e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1480 QRQIVSNLEKKQKkFDQMLAEEKTISAryaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIS 1559
Cdd:TIGR00618 165 KKELLMNLFPLDQ-YTQLALMEFAKKK---SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1560 SKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrDLQARDEQNEEKKRALVKQV 1639
Cdd:TIGR00618 241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA---AHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1640 REMEAELEDERKQRALAVAAKKKLEmdlkdveaqieaankardEAIKQLRKLQAQMKDYQRELEEArTSRDEIFTQSKEN 1719
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIE------------------EQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1720 EKKLKSLEA--EILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN 1797
Cdd:TIGR00618 378 TQHIHTLQQqkTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1798 DRFRKTTMQvdtlntELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSvKSKFKASIAALEAKILQLEEQLEQEAKE 1877
Cdd:TIGR00618 458 KIHLQESAQ------SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1878 RAAANKiVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeaeeeATRANASRRKLQRELDDATEASEG 1957
Cdd:TIGR00618 531 QRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNLQNITVRLQDLTEK 602
|
490
....*....|....
gi 688558683 1958 LSREVNTLKNRLRR 1971
Cdd:TIGR00618 603 LSEAEDMLACEQHA 616
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1151-1495 |
6.05e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1151 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTaaQQELRSKREQEVAELKKAIDDETRN 1230
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1231 HESQIQEMRQRHGtalEEISEQLEQAKRVKgNLEKNKQtlesdnKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfs 1310
Cdd:pfam17380 379 ELERLQMERQQKN---ERVRQELEAARKVK-ILEEERQ------RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1311 EGEKVKGELADRTHKIQTELDnvscllEDAEKKGIKLTKDvsslesqlqdtqellQEETRQKLnlssrirqLEEEKnnll 1390
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQ------QEEERKRKKLELE---------------KEKRDRKR--------AEEQR---- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1391 eqqeeeeesRKNLEKQLATLQAQLVETKKK-------LEDDVGALegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK 1463
Cdd:pfam17380 494 ---------RKILEKELEERKQAMIEEERKrkllekeMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKAT 562
|
330 340 350
....*....|....*....|....*....|..
gi 688558683 1464 NRlQQELDDLMVDLDHQRQIVSNlEKKQKKFD 1495
Cdd:pfam17380 563 EE-RSRLEAMEREREMMRQIVES-EKARAEYE 592
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1108-1755 |
6.16e-05 |
|
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: 48.28 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1108 LQDQIAELQAQIDELKIQLAKKEEELQAVLargdeevaqknNALKQLRElqaqlAELQEDLESEKAARNKAEKLK---RD 1184
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSM-----------NSIKTFWS-----PELKKERALRKEEAARISVLKeqyRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1185 LSEELEALKTELEDTLDTTAAQQELRSKREQEV------AELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQakr 1258
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFttspvdGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1259 VKGNLEKNKQTLESDNKELTN-----EVKSLQQAKSESEHKRKK----LEAQLQEVMARFSEGEKVKGELADRTHK---I 1326
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKllemlQSKGLPKKSGEEDWERTRriaeAEMQLGHLEVLLDQKEKENIHLREELHRrnqL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1327 QTELDNVSCLLEDAEKKGIKltkdVSSLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKN-----NLLEQQEEEE 1397
Cdd:pfam10174 222 QPDPAKTKALQTVIEMKDTK----ISSLERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKShskfmKNKIDQLKQE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1398 ESRKN-----LEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1472
Cdd:pfam10174 298 LSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1473 LMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMArALDEALEAKEE-FERLN 1547
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1548 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ------ATEDAKLR-LEVNMQAMKAQFDR- 1619
Cdd:pfam10174 457 EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSKl 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1620 DLQARDEQNEE----KKRALVKQVREMEAELEDERKQRALAVA-------AKKKLEMDLKDVEAQIEAANKARDEAIKQL 1688
Cdd:pfam10174 537 ENQLKKAHNAEeavrTNPEINDRIRLLEQEVARYKEESGKAQAeverllgILREVENEKNDKDKKIAELESLTLRQMKEQ 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1689 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKlkslEAEILQLQEDLASSERARRHAEQERDELA 1755
Cdd:pfam10174 617 NKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD----NSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1118-1286 |
6.50e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 47.32 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1118 QIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELqaqLAELQEDLESEKAARNKAEKLKrdlSEELEALKTELE 1197
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDR---KDALEEELRQLKQLEDELEDCD---PTELDRAKEKLK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1198 DTLDTTAAQQELRSKREQEVAELKKAIDDETrnhesqiqemrqrhgtalEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1277
Cdd:smart00787 215 KLLQEIMIKVKKLEELEEELQELESKIEDLT------------------NKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276
|
....*....
gi 688558683 1278 TNEVKSLQQ 1286
Cdd:smart00787 277 KEQLKLLQS 285
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1510-1737 |
7.11e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1510 EERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL 1589
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1590 EELEDELQATEDAKLRLEvNMQAMKAQFDRDLQARDeQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKD 1669
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRA-ELKE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1670 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDL 1737
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1526-1767 |
7.83e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1526 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtleQQVEEMRTQLEELEDELQATEDAKLR 1605
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----EEYNELQAELEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1606 LEVNMQAMKAQFDRdlQARDEQNEEKKRALVKQVreMEAELEDERKQRALAV-----AAKKKLEmDLKDVEAQIEAANKA 1680
Cdd:COG3883 77 AEAEIEERREELGE--RARALYRSGGSVSYLDVL--LGSESFSDFLDRLSALskiadADADLLE-ELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1681 RDEAIKQLRKLQAQMKDYQRELEeartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISN 1760
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELE----------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
....*..
gi 688558683 1761 SASGKAA 1767
Cdd:COG3883 222 AAAAAAA 228
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1626-1749 |
7.88e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 45.83 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1626 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE------------AANKARDEAIKQLRKLQA 1693
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKkleekaqaaltkGNEELAREALAEKKSLEK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1694 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQ 1749
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK----KNLLKARLKAAKAQEA 149
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1181-1311 |
8.10e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1181 LKRDLSEELEALKTELEDTLDttAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtalEEISEQLEQAKRVK 1260
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR-------NELQKLEKRLLQKE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 688558683 1261 GNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1311
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1077-1173 |
8.79e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.77 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1077 MVDLEERLKKEEKTRQELEKAKRKLDAET-TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNnalkQLR 1155
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG----KIP 488
|
90
....*....|....*...
gi 688558683 1156 ELQAQLAELQEDLESEKA 1173
Cdd:COG0542 489 ELEKELAELEEELAELAP 506
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1146-1449 |
8.83e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1146 QKNNALKQLRELQA-QLAELQEDLESEKAarNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEVAELKKAI 1224
Cdd:PRK05771 17 YKDEVLEALHELGVvHIEDLKEELSNERL--RKLRSLLTKLSEALDKLRSYLP------KLNPLREEKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1225 DDetrnhesqiqemrqrhgtaLEEISEQLEqaKRVKGnleknkqtLESDNKELTNEVKSLQQAKSESEhkrkKLEAqLQE 1304
Cdd:PRK05771 89 KD-------------------VEEELEKIE--KEIKE--------LEEEISELENEIKELEQEIERLE----PWGN-FDL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1305 VMARFSEGEKVKGELAdRTHKIQTE----LDNVSCLLEDAEKKG------IKLTKDVSSLESQLQDTqELLQEETRQKLN 1374
Cdd:PRK05771 135 DLSLLLGFKYVSVFVG-TVPEDKLEelklESDVENVEYISTDKGyvyvvvVVLKELSDEVEEELKKL-GFERLELEEEGT 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1375 LSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGL--EEVKRKLQKDMEVTSQKL 1449
Cdd:PRK05771 213 PSELIREIKEEL--------------EEIEKERESLLEELKELAKKYLEELLALYEYleIELERAEALSKFLKTDKT 275
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1113-1367 |
8.99e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1113 AELQAQIDELKiqlakKEEELQAvlargDEEVAQKNnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1192
Cdd:PRK11281 39 ADVQAQLDALN-----KQKLLEA-----EDKLVQQD--LEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1193 KTELEDTLDTTAAQQELRSkREQEVAELkkaiddetrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEs 1272
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQ-LESRLAQT-----------LDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1273 dnkELTNEVKSLQQAKSESEHKRK-KLEAQLQEVMARFSEGekvkgeladrthkiQTELDNVSCLLEDAEKKGIKLTKDV 1351
Cdd:PRK11281 174 ---QIRNLLKGGKVGGKALRPSQRvLLQAEQALLNAQNDLQ--------------RKSLEGNTQLQDLLQKQRDYLTARI 236
|
250
....*....|....*.
gi 688558683 1352 SSLESQLQDTQELLQE 1367
Cdd:PRK11281 237 QRLEHQLQLLQEAINS 252
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1037-1473 |
9.49e-05 |
|
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: 47.16 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1037 KFLKEKKLLEDRVGEMTSQ-LAEEEEKAKNLGkvknkqemMMVDLEERLKKEEKTRQELEkakrklDAETTDLQDQIAEL 1115
Cdd:pfam06160 7 KIYKEIDELEERKNELMNLpVQEELSKVKKLN--------LTGETQEKFEEWRKKWDDIV------TKSLPDIEELLFEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1116 QAQIDELKIQLAKKE-EELQAVLARGDEEVAQKNNALKQLrelqaqlaelqedLESEKAARNKAEKLK---RDLSEELEA 1191
Cdd:pfam06160 73 EELNDKYRFKKAKKAlDEIEELLDDIEEDIKQILEELDEL-------------LESEEKNREEVEELKdkyRELRKTLLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1192 LKTELEDTLDTTAAQ-QELRSKREQEVaELKKAID-DETRNHESQIQEMrqrhgtaLEEISEQLEqakRVKGNLEKNKQT 1269
Cdd:pfam06160 140 NRFSYGPAIDELEKQlAEIEEEFSQFE-ELTESGDyLEAREVLEKLEEE-------TDALEELME---DIPPLYEELKTE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1270 LESDNKELTNEVKSLQQAKSESEH-----KRKKLEAQLQEVMARFSEGE--KVKGELADrthkIQTELDNVSCLLE---D 1339
Cdd:pfam06160 209 LPDQLEELKEGYREMEEEGYALEHlnvdkEIQQLEEQLEENLALLENLEldEAEEALEE----IEERIDQLYDLLEkevD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1340 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQkLNLSSRIRQLEEEKNnlleqqeeeeesrKNLEKQLATLQAQLVETKK 1419
Cdd:pfam06160 285 AKKYVEKNLPEIEDYLEHAEEQNKELKEELER-VQQSYTLNENELERV-------------RGLEKQLEELEKRYDEIVE 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 688558683 1420 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1473
Cdd:pfam06160 351 RLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEF 404
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1019-1299 |
1.10e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 47.46 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1019 AKIKKMEEDILLLEDqnskFLKEKKLLEDRVGEMTSQLAEEEEKAkNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKak 1098
Cdd:pfam18971 567 AKGLSLQEANKLIKD----FLSSNKELAGKALNFNKAVAEAKSTG-NYDEVKKAQK----DLEKSLRKREHLEKEVEK-- 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1099 rKLDAETTDLQDQIAELQA--QIDELkIQLAKKEEElqavlaRGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARN 1176
Cdd:pfam18971 636 -KLESKSGNKNKMEAKAQAnsQKDEI-FALINKEAN------RDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFD 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1177 KAEKLK-RDLS---EELEALKTELED----------TLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqeMRQRH 1242
Cdd:pfam18971 708 EFKNGKnKDFSkaeETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVI--INQKV 785
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1243 GTALEEISEQLEQAKRVkGNLEKNKQTLeSDNKELTNEVKSLQQAKSESEHKRKKLE 1299
Cdd:pfam18971 786 TDKVDNLNQAVSVAKAM-GDFSRVEQVL-ADLKNFSKEQLAQQAQKNEDFNTGKNSE 840
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1506-1825 |
1.10e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1506 ARYAEERDRaEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1585
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1586 RTQLEELEDELQATEDAKLRLEVNMQAMKaqfdrdlqardeqneEKKRALVKQVREMEAElederkqralavaaKKKLEM 1665
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAE--------------RKQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1666 DLKDVEAQIEAANKardeAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERArr 1745
Cdd:pfam07888 179 KLQQTEEELRSLSK----EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1746 hAEQERDELADEISNSASGKAALldEKRRLEAR----------------IAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1809
Cdd:pfam07888 253 -VEGLGEELSSMAAQRDRTQAEL--HQARLQAAqltlqladaslalregRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330
....*....|....*.
gi 688558683 1810 LNTELAGERSAAQKSE 1825
Cdd:pfam07888 330 LEERLQEERMEREKLE 345
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1447-1971 |
1.21e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1447 QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKD 1523
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1524 TKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR-----------------TLEQQVEEMR 1586
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1587 TQLEELEDELQATEDAKLRLEVnMQAMKAQFDRDLQARDEQN---------EEKKRALVKQVREMEAELEDERKQR---- 1653
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNnqilelegyEMDYNSYLKSIESLKKKIEEYSKNIerms 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1654 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQS----------------- 1716
Cdd:PRK01156 391 AFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhi 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1717 -KENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1795
Cdd:PRK01156 471 iNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1796 LNDRFRKTTMQ-VDTLNTELAgeRSAAQKS----ENARQQLERQNK---DLKSKLQELEGS---VKSKFKASIAALEAKI 1864
Cdd:PRK01156 551 IKNRYKSLKLEdLDSKRTSWL--NALAVISlidiETNRSRSNEIKKqlnDLESRLQEIEIGfpdDKSYIDKSIREIENEA 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1865 LQLEEQLEQEAKERAAANKIvRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEeaeeeatRANASRRKL 1944
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKL-RGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-------DAKANRARL 700
|
570 580
....*....|....*....|....*..
gi 688558683 1945 QRELDDATEASEGLSREVNTLKNRLRR 1971
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLES 727
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1100-1781 |
1.31e-04 |
|
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: 47.12 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1100 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNnalkQLRELQAQLAELQEDLESEKAARNKAE 1179
Cdd:pfam10174 175 KSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHL----REELHRRN----QLQPDPAKTKALQTVIEMKDTKISSLE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1180 KLKRDLSEELEALKTELEdtLDTTAAQQELRSkreqevAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEqakrv 1259
Cdd:pfam10174 247 RNIRDLEDEVQMLKTNGL--LHTEDREEEIKQ------MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLE----- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1260 kgnleknkqTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVkgeLADRTHKIQteldnvsclled 1339
Cdd:pfam10174 314 ---------TLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESF---LNKKTKQLQ------------ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1340 aekkgiKLTKDVSSLESQLQDTQELLQEETRqKLNLssrirqleeeknnlleqqeeeeesrknLEKQLATLQAQLVETKK 1419
Cdd:pfam10174 370 ------DLTEEKSTLAGEIRDLKDMLDVKER-KINV---------------------------LQKKIENLQEQLRDKDK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1420 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDlmvDLDHQRQIVSNLEKKQKKFDQMLA 1499
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELT 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1500 EEKTISARYAEERDRAEAEAREKDTKALSMARALDealEAKEEFERLNKQLraemedlisskddvgKNVHELEKSKRTLE 1579
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE---QKKEECSKLENQL---------------KKAHNAEEAVRTNP 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1580 QQVEemRTQLEELEDELQATEDAKLRLEVnmqamkaqfDRDLQA-RDEQNEekKRALVKQVREMEAELEDERKQRALAVA 1658
Cdd:pfam10174 555 EIND--RIRLLEQEVARYKEESGKAQAEV---------ERLLGIlREVENE--KNDKDKKIAELESLTLRQMKEQNKKVA 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1659 AKKKLEMDLK------DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL- 1731
Cdd:pfam10174 622 NIKHGQQEMKkkgaqlLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRk 701
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 688558683 1732 QLQEDLASSERARRHAEQERDELADEISNSASGK-------AALLDEKRRLEARIAQ 1781
Cdd:pfam10174 702 QLEEILEMKQEALLAAISEKDANIALLELSSSKKkktqeevMALKREKDRLVHQLKQ 758
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1668-1864 |
1.34e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1668 KDVEAQIEAANKARDeaikqlrkLQAQMKDYQRELEEARTSRDEIFTQSKENE---KKLKSLEAEILQLQEDLASSERAr 1744
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETEqlkQQLAQAPAKLRQAQAELEALKDD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1745 rhaeqerdelADEISNSASGKAALldekRRLEARIAQLEEELEEEQSNMELLNDrfrkttmQVDTLNTelAGERSAAQKS 1824
Cdd:PRK11281 110 ----------NDEETRETLSTLSL----RQLESRLAQTLDQLQNAQNDLAEYNS-------QLVSLQT--QPERAQAALY 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 688558683 1825 ENAR--QQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKI 1864
Cdd:PRK11281 167 ANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQN 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1670-1924 |
1.42e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1670 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFT--QSKENEKKLKSLEAEILQLQEDLASSERARRHA 1747
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1748 EQERDELADEISNSASGKAAlldekRRLEARIAQleeeleeeqsnmellndrfrkttmqvdtLNTELAGERSAAQKSENA 1827
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVI-----QQLRAQLAE----------------------------LEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1828 RQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqleeqleqeakerAAANKIVRRTEKKLKEvFMQVEDE----R 1903
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQARE--------------ASLQAQLAQLEARLAE-LPELEAElrrlE 357
|
250 260
....*....|....*....|.
gi 688558683 1904 RHADQYKEQMEKANSRMKQLK 1924
Cdd:COG3206 358 REVEVARELYESLLQRLEEAR 378
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
887-1366 |
1.52e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 887 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETEL---FAEAEEMRARLVAKKQELEE 963
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 964 IlHDLESRVeeeeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKL-QLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1042
Cdd:pfam05557 199 I-PELEKEL-------ERLREHNKHLNENIENKLLLKEEVEDLKRKLeREEKYREEAATLELEKEKLEQELQSWVKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1043 KLLEDRVGE-MTSQLAEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDE 1121
Cdd:pfam05557 271 TGLNLRSPEdLSRRIEQLQQREIVLKEENS-------SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1122 L--KIQLAKKEEE-LQAVLARGDEEVAQKN---NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTE 1195
Cdd:pfam05557 344 LqrRVLLLTKERDgYRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1196 LedTLDTTAAQQELRSKREQEVAELKKAIDDetrnhesqIQEMRQRhgtaLEEISEQLEqakrvkgnLEKNKQTLESDNK 1275
Cdd:pfam05557 424 L--QALRQQESLADPSYSKEEVDSLRRKLET--------LELERQR----LREQKNELE--------MELERRCLQGDYD 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1276 ELTNEVKSLQQ-AKSESEHKRKKLEAQLQEVMARfsegekvkgeLADRTHKIQTELDNVSCL----LEDAEKKGIKLTKD 1350
Cdd:pfam05557 482 PKKTKVLHLSMnPAAEAYQQRKNQLEKLQAEIER----------LKRLLKKLEDDLEQVLRLpettSTMNFKEVLDLRKE 551
|
490
....*....|....*.
gi 688558683 1351 VSSLESQLQDTQELLQ 1366
Cdd:pfam05557 552 LESAELKNQRLKEVFQ 567
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1528-1881 |
1.54e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.21 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1528 SMARALDEALEAKEEFERLNKQLRAEMEDLISSKddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLe 1607
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELPQAK----SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1608 vnmQAMKAQFDRDLQARDEQNEEKK---RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEA 1684
Cdd:pfam19220 89 ---VARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1685 IKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASS----ERARRHAEQERDELADEISN 1760
Cdd:pfam19220 166 RERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEqaerERAEAQLEEAVEAHRAERAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1761 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQ------ 1834
Cdd:pfam19220 246 LRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraelee 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1835 -----NKDLKSKLQELEGSVKS-------------KFKASIAALEAKILQLEEQLEQEAKERAAA 1881
Cdd:pfam19220 326 raemlTKALAAKDAALERAEERiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
955-1137 |
1.61e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 955 VAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 1034
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1035 NSKFLKEKklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1114
Cdd:COG1579 82 LGNVRNNK--------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|...
gi 688558683 1115 LQAQIDELKIQLAKKEEELQAVL 1137
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPEL 176
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1618-1741 |
2.04e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1618 DRDLQARDEQNEEKKRALVKQVREMEAELEDE---RKQRALAVAAKKKLEMDLKDVEAQIEAANK------ARDEAIKQL 1688
Cdd:COG1566 78 PTDLQAALAQAEAQLAAAEAQLARLEAELGAEaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgavsqqELDEARAAL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 688558683 1689 RKLQAQMKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAEILQLQEDLASSE 1741
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLREE-EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1399-1607 |
2.13e-04 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 46.37 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1399 SRKNLEKQLATLQAQ------LVETKKKLEDDVgalEGLEEVKRK--LQK-DMEVTSQKLEEKaiafdkLEKTKNRLQQE 1469
Cdd:pfam15066 340 SNLYLEKKVKELQMKitkqqvFVDIINKLKENV---EELIEDKYNviLEKnDINKTLQNLQEI------LANTQKHLQES 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1470 lddlmvdldhqrqivsnleKKQKKFDQMlaEEKTISARYAEERDRAEAEAREKDtKALSMARALDEALEAKE-EFERLnK 1548
Cdd:pfam15066 411 -------------------RKEKETLQL--ELKKIKVNYVHLQERYITEMQQKN-KSVSQCLEMDKTLSKKEeEVERL-Q 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1549 QLRAEMEDLISSKDDVgknvheLEKSKRTLEQQVEEMRTQLEELEDE-LQATEDAKLRLE 1607
Cdd:pfam15066 468 QLKGELEKATTSALDL------LKREKETREQEFLSLQEEFQKHEKEnLEERQKLKSRLE 521
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1440-1684 |
2.15e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.75 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1440 KDMEVTSQKLEEKAIAfdklEKTKNRLQQELDDLmvdLDHqrqiVSNLEKKQKKFDQmLAEEKTISAryaeERDRAEAEA 1519
Cdd:NF012221 1552 KQDDAAQNALADKERA----EADRQRLEQEKQQQ---LAA----ISGSQSQLESTDQ-NALETNGQA----QRDAILEES 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1520 REKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIssKDDVGKnvhELEKSKRTLEQQVEEMRTQLE----ELEDE 1595
Cdd:NF012221 1616 RAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQE---QLDDAKKISGKQLADAKQRHVdnqqKVKDA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1596 LQATEDAKLRLEVNMQAMKAQFDrdlQARDEQNEEKKRALVKQVREMEAElederkQRALAVAAKKKLEMDlKDVEAQIE 1675
Cdd:NF012221 1691 VAKSEAGVAQGEQNQANAEQDID---DAKADAEKRKDDALAKQNEAQQAE------SDANAAANDAQSRGE-QDASAAEN 1760
|
....*....
gi 688558683 1676 AANKARDEA 1684
Cdd:NF012221 1761 KANQAQADA 1769
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1101-1255 |
2.25e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1101 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEK 1180
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDL----QDSVANLRASLSAAEAERSRLQALLAELA---GAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1181 LKRDLSEELEALKTELEDTLDTTAA-QQELRSKREQeVAELKKAIDD-ETRNHESQ--IQEMRQRHGTALEEISEQLEQ 1255
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELlNQQIAALRRQ-LAALEAALDAsEKRDRESQakIADLGRRLNVALAQRVQELNR 194
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1660-1841 |
2.50e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1660 KKKLEMDLKDVEAqieAANKARDEAIKQL---------RKLQAQ-MKDYQRELEE----ARTSRDEIFTQSKE-----NE 1720
Cdd:PRK10929 25 EKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEprsvpPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1721 KKLKSLEAEILQLQEDLAssERARRhAEQERDElADEISNSASGKAALLDEKRRL----EARI-AQLEEELEEEQSNMEL 1795
Cdd:PRK10929 102 MSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLAQAQLTA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 688558683 1796 LNDRFRKTTMQVDTLntELagersaAQKSENARQQLERQNKDLKSK 1841
Cdd:PRK10929 178 LQAESAALKALVDEL--EL------AQLSANNRQELARLRSELAKK 215
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1092-1320 |
2.67e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1092 QELEKAKRKLD------AETTDLQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQKNNALkQLRELQAQLAELQ 1165
Cdd:PRK11281 63 QDLEQTLALLDkidrqkEETEQLKQQLAQAPAKLRQAQ-------AELEALKDDNDEETRETLSTL-SLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1166 EDLESekaarnkaekLKRDLSE---ELEALKTELEDtldttaAQQEL--RSKREQEVAELKKAIDDETRNHESQIQEMRQ 1240
Cdd:PRK11281 135 DQLQN----------AQNDLAEynsQLVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1241 RHGTALEEISEQLEQakrvkgNLEKNKQTLESDNKELtnEVKSLQQAKSESE---------HKRKKL------EAQLQEV 1305
Cdd:PRK11281 199 AEQALLNAQNDLQRK------SLEGNTQLQDLLQKQR--DYLTARIQRLEHQlqllqeainSKRLTLsektvqEAQSQDE 270
|
250
....*....|....*
gi 688558683 1306 MARFSEGEKVKGELA 1320
Cdd:PRK11281 271 AARIQANPLVAQELE 285
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1591-1863 |
3.04e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1591 ELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElederkqrALAVAAKKKLEMDLKDV 1670
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAAEARAAKDKDAVAA--------ALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1671 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskENEKKlKSLEAEIlqlqedlassERAR-RHAEQ 1749
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAA------------ADPKK-AAVAAAI----------ARAKaKKAAQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1750 ErDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmqvdtlnTELAGERSAAQKSENARQ 1829
Cdd:PRK05035 565 Q-AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA---------VAAAIARAKAKKAEQQAN 634
|
250 260 270
....*....|....*....|....*....|....
gi 688558683 1830 QLERQNKDLKsklqelegsvKSKFKASIAALEAK 1863
Cdd:PRK05035 635 AEPEEPVDPR----------KAAVAAAIARAKAR 658
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
954-1330 |
3.32e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.45 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 954 LVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK----------LQLEKVTAEA---- 1019
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKylllqkqleqLQEENFRLETardd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1020 ---KIKKMEEDILLLEDQNSKFLK---EKKLLED----------RVGEMTSQLAEEEEKAKNLG----KVKNKQEMMM-- 1077
Cdd:pfam05622 85 yriKCEELEKEVLELQHRNEELTSlaeEAQALKDemdilressdKVKKLEATVETYKKKLEDLGdlrrQVKLLEERNAey 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1078 ----VDLEERLKKEEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNN---A 1150
Cdd:pfam05622 165 mqrtLQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTlreT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1151 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLseeleaLKTELEDTLdttaaqqeLRSKREQEVAELKKAIDDETRn 1230
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI------MPAEIREKL--------IRLQHENKMLRLGQEGSYRER- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1231 hesqiqemrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE-------SEHKRKKLEAQLQ 1303
Cdd:pfam05622 306 ---------------LTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEqgskaedSSLLKQKLEEHLE 370
|
410 420
....*....|....*....|....*..
gi 688558683 1304 EVMARFSEGEKVKGELADRTHKIQTEL 1330
Cdd:pfam05622 371 KLHEAQSELQKKKEQIEELEPKQDSNL 397
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1498-1654 |
3.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1498 LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED----LISSKDDVGKNVHELEK 1573
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1574 SKRTLEQQVEEMRTQLEELE------DELQATEDAKLRLEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELE 1647
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEkkeeelEELIEEQLQELERISGLTAEEAK----EILLEKVEEEARHEAAVLIKEIEEEAK 183
|
....*..
gi 688558683 1648 DERKQRA 1654
Cdd:PRK12704 184 EEADKKA 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
920-1253 |
3.47e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 920 ERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQ--SLQNEKKkmqsHIQDLE 997
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELE----RLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 998 EQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknlgkvknkqemmm 1077
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--------------- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1078 vDLEERLKKEEKTRQELEKAKRkldaettdLQDQIAELQAQIDELKIQLAKKEEELQ----AVLARGDEEVAQKNNALKQ 1153
Cdd:COG4913 750 -LLEERFAAALGDAVERELREN--------LEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLAL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1154 LRELQAQ-LAELQEDLESEKAARNKAEK--LKRDLSEELEALKTELE---DTL------DTTAAQQELRSKREQEVAELK 1221
Cdd:COG4913 821 LDRLEEDgLPEYEERFKELLNENSIEFVadLLSKLRRAIREIKERIDplnDSLkripfgPGRYLRLEARPRPDPEVREFR 900
|
330 340 350
....*....|....*....|....*....|..
gi 688558683 1222 KAIDDETRNHESQIQEMRQRHGTALEEISEQL 1253
Cdd:COG4913 901 QELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1084-1384 |
3.75e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.80 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1084 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAqlae 1163
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTR---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1164 lQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQElrskreqevaelkkaiddetrNHESQIQEMrQRHg 1243
Cdd:pfam15905 137 -VNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQE---------------------GMEGKLQVT-QKN- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1244 taLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLeAQLQEVMArfsegekvkgELADRT 1323
Cdd:pfam15905 193 --LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDI-AQLEELLK----------EKNDEI 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1324 HKIQTELDNVSCLLEdaekkgiKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEE 1384
Cdd:pfam15905 260 ESLKQSLEEKEQELS-------KQIKDLNEKCKLLEsEKEELLREYEEKEQTLNAELEELKE 314
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
986-1367 |
3.85e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 986 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVT----------------------AEAKIKKMEEDILLLEDQNSK--FLKE 1041
Cdd:PRK04778 24 RKRNYKRIDELEERKQELENLPVNDELEKVKklnltgqseekfeewrqkwdeiVTNSLPDIEEQLFEAEELNDKfrFRKA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1042 KKLLedrvGEMTSQLAEEEEKAKNLgkvknKQEMM-MVDLEERLKKE-EKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1119
Cdd:PRK04778 104 KHEI----NEIESLLDLIEEDIEQI-----LEELQeLLESEEKNREEvEQLKDLYRELRKSLLANRFSFGPALDELEKQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1120 DELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDT 1199
Cdd:PRK04778 175 ENLEEEFSQFVELTES----GDYVEAR-----EILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1200 ---LDTTAAQQELRSKREQeVAELKKAID----DETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEKNKQTLES 1272
Cdd:PRK04778 246 gyhLDHLDIEKEIQDLKEQ-IDENLALLEeldlDEAEEKNEEIQE-------RIDQLYDILEREVKARKYVEKNSDTLPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1273 D-------NKELTNEVKSLQQAK--SESE-HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK 1342
Cdd:PRK04778 318 FlehakeqNKELKEEIDRVKQSYtlNESElESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEK 397
|
410 420
....*....|....*....|....*
gi 688558683 1343 KGIKLTKDVSSLESQLQDTQELLQE 1367
Cdd:PRK04778 398 EQEKLSEMLQGLRKDELEAREKLER 422
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1117-1227 |
4.54e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1117 AQIDELKIQLAKKEEELQAVLARGDEEVAQKnnalkqLRELQAQLAELQEDLESEKaARNKAEKlkrDLSEELEALKTEL 1196
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALK-ARWEAEK---ELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 688558683 1197 EDTLDTTAAQQELRSKREQEVAELKKAIDDE 1227
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1619-1828 |
4.55e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1619 RDLQARDEQNEEKKRALVKQVREMEAELEDerkqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1698
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1699 QRELEEARTSRD--EIFTQSKENEKKLKSLEA----------EILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1766
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSESFSDFLDRLSAlskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1767 ALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENAR 1828
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1081-1301 |
4.98e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1081 EERLKKEEKTRQEleKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQ 1160
Cdd:PRK05035 459 QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAE 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1161 LAELQEDLESEKA-----ARNKAEKLKR-----DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRN 1230
Cdd:PRK05035 537 KQAAAAADPKKAAvaaaiARAKAKKAAQqaanaEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1231 HESQIQEMR-QRHGTALEEISEQLEQAK--RVKGNLEKNK-----QTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1301
Cdd:PRK05035 617 VAAAIARAKaKKAEQQANAEPEEPVDPRkaAVAAAIARAKarkaaQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1008-1208 |
5.47e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.51 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1008 QKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqemmMVDLEERLKKE 1087
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA----------LTKGNEELARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1088 EKTR-QELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARgdEEVAQKNNALKQLR---------EL 1157
Cdd:pfam04012 88 ALAEkKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTSLgslstssatDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 688558683 1158 QAQLAELQEDLESEKAARNKAEKlKRDLSEELEALKTELEDTLDTTAAQQE 1208
Cdd:pfam04012 166 FERIEEKIEEREARADAAAELAS-AVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
899-1197 |
6.09e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 899 DEELIKVKERQVKVENELVEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLVAKkqELEEILHDLESRVEE 974
Cdd:PRK05771 27 ELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklRSYLPKLNPLREEKKKVSVKSLEELIK--DVEEELEKIEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 975 EEERNQSLQNEKKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDIllledqnsKFLKEKKLLEDRVGEMTS 1054
Cdd:PRK05771 105 LEEEISELENEIKELEQEIE----------------RLEPW------GNFDLDL--------SLLLGFKYVSVFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1055 QLAEEEEKAKNLGKV----KNKQEMMMV---------DLEERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDE 1121
Cdd:PRK05771 155 DKLEELKLESDVENVeyisTDKGYVYVVvvvlkelsdEVEEELKKLGFERLELE-EEGTPSELIREIKEELEEIEKERES 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1122 LK---IQLAKKEEELQAVLARGDEEVAQKNNALKQLRE------LQA-----QLAELQEDLesEKAARNKAEKLKRDLSE 1187
Cdd:PRK05771 234 LLeelKELAKKYLEELLALYEYLEIELERAEALSKFLKtdktfaIEGwvpedRVKKLKELI--DKATGGSAYVEFVEPDE 311
|
330
....*....|
gi 688558683 1188 ELEALKTELE 1197
Cdd:PRK05771 312 EEEEVPTKLK 321
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1076-1215 |
6.19e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1076 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLR 1155
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLA-------TERSARREAEAELE 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1156 ELQAQLAELQEDLESEKAARnkaEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ 1215
Cdd:pfam09787 118 RLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQ 174
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1045-1129 |
6.20e-04 |
|
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467481 [Multi-domain] Cd Length: 103 Bit Score: 40.99 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1045 LEDRVGEMTSQLAEEEEKAKNLGKVKNkqEMMMVDLEERLK----------KEEKTRQELEKAKRKLDAETTDLQDQIAE 1114
Cdd:cd23165 11 LNARLHELKEELKAKKKELENLEDASD--ELELADDDEPVPykigevfvhlSLEEAQERLEKAKEELEEEIEKLEEEIDE 88
|
90
....*....|....*
gi 688558683 1115 LQAQIDELKIQLAKK 1129
Cdd:cd23165 89 IEEEMKELKVQLYAK 103
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1726-1864 |
6.65e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.95 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1726 LEAEILQLQEDLASSERARRHAEQERD---ELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1802
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDrlqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1803 TTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS---KLQELEGSVKSKFKASIAALEAKI 1864
Cdd:pfam00529 136 GGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQsaaENQAEVRSELSGAQLQIAEAEAEL 200
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1234-1385 |
7.05e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 44.65 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1234 QIQEMR----QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1309
Cdd:pfam10168 540 ATQVFReeylKKHDLAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1310 -------SEGEKvkgELADRTHKIQTELDNVSCLLEDAEKK------------GIKLTKDVSSLESQLQDTQELLQEETR 1370
Cdd:pfam10168 620 nsqlpvlSDAER---EMKKELETINEQLKHLANAIKQAKKKmnyqryqiaksqSIRKKSSLSLSEKQRKTIKEILKQLGS 696
|
170
....*....|....*
gi 688558683 1371 QKLNLSSRIRQLEEE 1385
Cdd:pfam10168 697 EIDELIKQVKDINKH 711
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1570-1755 |
7.41e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1570 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDE 1649
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1650 RKQRALAVAAKKKLEmdlkdveaqiEAANKARDEAIKqlrKLQAQMKdyqRELEEARTSRDEIFTQSKENEKKLKSLEAE 1729
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 688558683 1730 ILQLQEDLASSERARRHAEQERDELA 1755
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1074-1208 |
7.49e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 44.07 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1074 EMMMVDLEERLKKE--EKTRQELEKAKRKLDAETTDLQD------------QIAELQAQIDELKIQLAKKEEELQAVLAR 1139
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1140 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLkrdlsEELEALKTEL---EDTLDTTAAQQE 1208
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1684-1971 |
7.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1684 AIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAE---QERDELADEISN 1760
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1761 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttmqvdtlntelAGERSAAQKSENARQQLERQNKDLKS 1840
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1841 KLQELEgSVKSKFKASIAALEAKIlqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANsRM 1920
Cdd:PRK03918 308 ELREIE-KRLSRLEEEINGIEERI-----------KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-EL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 688558683 1921 KQLKRQLeeaeeeatrANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1971
Cdd:PRK03918 375 ERLKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1298-1647 |
8.54e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1298 LEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKgikLTKDVSSLESQLQDTQELLQEETRQKLNLSS 1377
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE---LESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1378 RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE------DDVGALEGLEEVKRK-LQKDMEVTSQKLE 1450
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELErmkeraKKAGAQRKEEEAERKqLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1451 EKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1530
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1531 RALDEALEAKEEFERLNKQL--------------RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1596
Cdd:pfam07888 269 RTQAELHQARLQAAQLTLQLadaslalregrarwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVEL 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1597 QATEDAKL----RLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELE 1647
Cdd:pfam07888 349 GREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1054-1192 |
9.86e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1054 SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEEL 1133
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-APAWLAA 607
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1134 QAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1192
Cdd:COG3096 608 QDALERLREQSGE---ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1653-1862 |
1.02e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.51 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1653 RALAVAAKKKLEMDLKD-----VEAQIEAANKARDEA---IKQLRKLQAQMKDYQRELEEARTSRDEIFTQ--SKENEKK 1722
Cdd:cd22656 101 DDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAakvVDKLTDFENQTEKDQTALETLEKALKDLLTDegGAIARKE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1723 LKSLEAEILQLQEDLAsserarRHAEQERDELADEISNsasgkaalLDEKRRLEARIaqleeeleeeQSNMELLNDrfrk 1802
Cdd:cd22656 181 IKDLQKELEKLNEEYA------AKLKAKIDELKALIAD--------DEAKLAAALRL----------IADLTAADT---- 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1803 ttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEA 1862
Cdd:cd22656 233 ---DLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1059-1603 |
1.07e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.97 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1059 EEEKAKNLGKVKNKQEMMMVDL----EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ 1134
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1135 A-----------VLARGDEEVAQKNNALKQlRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELE 1197
Cdd:pfam07111 215 AqvtlveslrkyVGEQVPPEVHSQTWELER-QELLDTMQHLQEDRADLQATvellqvRVQSLTHMLALQEEELTRKIQPS 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1198 DTLD---TTAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1274
Cdd:pfam07111 294 DSLEpefPKKCRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1275 ---KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKK--GIK-LT 1348
Cdd:pfam07111 373 msaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhTIKgLM 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1349 KDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeeSRKNLEKQLATLQAQLvETKKKLEDDVGAL 1428
Cdd:pfam07111 453 ARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREER------------NRLDAELQLSAHLIQQ-EVGRAREQGEAER 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1429 EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSnlekkqKKFDQMLAEEKTISARY 1508
Cdd:pfam07111 520 QQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYG------QALQEKVAEVETRLREQ 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1509 AEERDRAEAEAREKDTKALSMARALDEalEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR----TLEQQVEE 1584
Cdd:pfam07111 594 LSDTKRRLNEARREQAKAVVSLRQIQH--RATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNlmlaTLQQEGLL 671
|
570
....*....|....*....
gi 688558683 1585 MRTQLEELEDELQATEDAK 1603
Cdd:pfam07111 672 SRYKQQRLLAVLPSGLDKK 690
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
902-1132 |
1.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 902 LIKVKERQVKVENELVEMERKH--QQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERN 979
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 980 QSLQNEKKKMQShiqdleeqldeeEAARQKLQLEKVTAEAK--------------IKKMEEDILLLEDQNSKFLKEKKLL 1045
Cdd:PHA02562 251 EDPSAALNKLNT------------AAAKIKSKIEQFQKVIKmyekggvcptctqqISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1046 EDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQ 1125
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKIS----TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
....*..
gi 688558683 1126 LAKKEEE 1132
Cdd:PHA02562 395 KSELVKE 401
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
985-1187 |
1.15e-03 |
|
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: 43.69 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 985 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVtaEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAK 1064
Cdd:pfam06160 231 EHLNVDKEIQQLEEQLEENLALLENLELDEA--EEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1065 NLgkvknKQEMMMVDLEERLKKEEKTRQElekakrkldaettDLQDQIAELQAQIDELKIQLAKKE---EELQAVLargd 1141
Cdd:pfam06160 309 EL-----KEELERVQQSYTLNENELERVR-------------GLEKQLEELEKRYDEIVERLEEKEvaySELQEEL---- 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 688558683 1142 eevaqkNNALKQLRELQAQLAELQEDLES----EKAARNKAEKLKRDLSE 1187
Cdd:pfam06160 367 ------EEILEQLEEIEEEQEEFKESLQSlrkdELEAREKLDEFKLELRE 410
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1088-1374 |
1.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1088 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQED 1167
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1168 LESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE 1247
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1248 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHkRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ 1327
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL-SALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 688558683 1328 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN 1374
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1648-1838 |
1.36e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1648 DERKQRALAVAAKKKLEMDLK---DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN----- 1719
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrq 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1720 -EKKLKSLEAEILQLQEDLAS-----------SERARR---HAEQERDELADEISNSASGKAALLDEKR-RLEARIAQle 1783
Cdd:PRK11281 126 lESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQAEQAL-- 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1784 eeleeeqsnMELLNDrFRKTTMQVDTLNTELaGERSAAQKSENArQQLERQNKDL 1838
Cdd:PRK11281 204 ---------LNAQND-LQRKSLEGNTQLQDL-LQKQRDYLTARI-QRLEHQLQLL 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1039-1710 |
1.39e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1039 LKEKKLLEDRVGEMTSQLAE----------EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL 1108
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSEleqrlrqqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1109 QDQIAELQAQIDELKiQLAKKEEELQAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1188
Cdd:PRK04863 585 RQQLEQLQARIQRLA-ARAPAWLAAQDALARLREQSGE---EFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1189 LEALkteledTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISeqleqakRVKGNLEK 1265
Cdd:PRK04863 661 IERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLS-------DAAEQLAG 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1266 NKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE--GEKVKGELA--DRTHKIQTELDNVSCLLEdae 1341
Cdd:PRK04863 728 LEDCPE-DLYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRfpEVPLFGRAAreKRIEQLRAEREELAERYA--- 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1342 kkgiKLTKDVSSLESQLQDTQELLQ-----------EETRQKLNlsSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1410
Cdd:PRK04863 804 ----TLSFDVQKLQRLHQAFSRFIGshlavafeadpEAELRQLN--RRRVELERALADHESQEQQQRSQLEQAKEGLSAL 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1411 QAQLVETKKKLEDDVGalEGLEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQ---QELDDLMVDLDHQRQIVSNL 1487
Cdd:PRK04863 878 NRLLPRLNLLADETLA--DRVEEIREQL-DEAEEAKRFVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDA 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1488 ekKQKKFDqmlaeektisarYAEERDRAEAEAREKDTKALSMARALDEALEAK-EEFERLNKQLRAEMEDLISSKDDVGK 1566
Cdd:PRK04863 955 --KQQAFA------------LTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRlEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1567 NVHELEKSKRTLEQQVEEMRTQLEELedELQATEDAklrlevnmqAMKAQFDRD-LQARDEQNEEKKRALVKQVREMEAE 1645
Cdd:PRK04863 1021 VLASLKSSYDAKRQMLQELKQELQDL--GVPADSGA---------EERARARRDeLHARLSANRSRRNQLEKQLTFCEAE 1089
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1646 LEDERKQralavaaKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-----EEARTSRD 1710
Cdd:PRK04863 1090 MDNLTKK-------LRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELaylsaDELRSMSD 1152
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
935-1341 |
1.40e-03 |
|
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: 43.69 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 935 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshiqdleeqldeeeaarqklqlek 1014
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT----------------------------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1015 vtaeakikkmeedillLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEE--------KAKnlgKVKNKQEMMMVDLEERLkk 1086
Cdd:pfam06160 137 ----------------LLANRFSYGPAIDELEKQLAEIEEEFSQFEEltesgdylEAR---EVLEKLEEETDALEELM-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1087 eEKTRQELEKAKRKLDAETTDLQDQIAELQAQ---IDELKI-----QLAKKEEELQAVLARGDEEVAQKNNalkqlRELQ 1158
Cdd:pfam06160 196 -EDIPPLYEELKTELPDQLEELKEGYREMEEEgyaLEHLNVdkeiqQLEEQLEENLALLENLELDEAEEAL-----EEIE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1159 AQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---ID 1225
Cdd:pfam06160 270 ERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELErvqqsytlNENELERVRglEKQLEELEKRydeIV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1226 DETRNHE---SQIQEMrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKseSEHKRKKLEAQL 1302
Cdd:pfam06160 350 ERLEEKEvaySELQEE-------LEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL--REIKRLVEKSNL 420
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 688558683 1303 ----QEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1341
Cdd:pfam06160 421 pglpESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQ 463
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1119-1301 |
1.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1119 IDELKIQLAKKEEELQAvlargdEEVAQKNNALKQLRELQAQ--LAELQEDLESE-KAARNKAEKLKRDLSEELEALKTE 1195
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIL------EEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1196 LEDTLDTTA---AQQELRSKREQEVAELKKaiddetrnhesQIQEMRQRHGTALEEISE-QLEQAKRVKgnLEKNKQTLE 1271
Cdd:PRK12704 102 LELLEKREEeleKKEKELEQKQQELEKKEE-----------ELEELIEEQLQELERISGlTAEEAKEIL--LEKVEEEAR 168
|
170 180 190
....*....|....*....|....*....|
gi 688558683 1272 SDNKELTNEVKslQQAKSESEHKRKKLEAQ 1301
Cdd:PRK12704 169 HEAAVLIKEIE--EEAKEEADKKAKEILAQ 196
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1079-1234 |
1.51e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.29 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1079 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLREL 1157
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAAL 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558683 1158 QAQLAELQEDLESeKAARNKAEKLKRDL-SEELEALKTELEdtldttAAQQELRSKREQEVAELKKAIDDETRNHESQ 1234
Cdd:pfam12795 162 KAQIDMLEQELLS-NNNRQDLLKARRDLlTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1688-1851 |
1.55e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1688 LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEisnsasgKAA 1767
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE-------KDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1768 LLDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEG 1847
Cdd:pfam07888 120 LLAQRAAHEARIRE--------------LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
....
gi 688558683 1848 SVKS 1851
Cdd:pfam07888 186 ELRS 189
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1464-1898 |
1.62e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1464 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaeEKTISARYAEERDRAEAEAREKDTKALsMARALDEALEAKEEF 1543
Cdd:COG5278 89 DELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRARLLLLALAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1544 ERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQA 1623
Cdd:COG5278 166 AALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1624 RDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE 1703
Cdd:COG5278 246 LAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAAL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1704 EARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLE 1783
Cdd:COG5278 326 AALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1784 EELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAK 1863
Cdd:COG5278 406 AAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALA 485
|
410 420 430
....*....|....*....|....*....|....*
gi 688558683 1864 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQ 1898
Cdd:COG5278 486 EAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1570-1781 |
1.80e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1570 ELEKSKRTLEQQVEEMRTQLEELED-ELQATEDAKLRLEVNMQAmkaqfdrdlqardeqNEEKKRALVKQVREMeaeL-E 1647
Cdd:COG0497 176 ELRADEAERARELDLLRFQLEELEAaALQPGEEEELEEERRRLS---------------NAEKLREALQEALEA---LsG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1648 DERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE---------EARTSR--------- 1709
Cdd:COG0497 238 GEGGALDLLGQALRALE-RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdperleevEERLALlrrlarkyg 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1710 ---DEIFTQSKENEKKLKSLEAeilqLQEDLASSERARRHAEQERDELADEISNsASGKAAlldekRRLEARIAQ 1781
Cdd:COG0497 317 vtvEELLAYAEELRAELAELEN----SDERLEELEAELAEAEAELLEAAEKLSA-ARKKAA-----KKLEKAVTA 381
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1629-1902 |
1.90e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1629 EEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTS 1708
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1709 RDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1788
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1789 EQSNMELLNDRFRKTTMQ-VDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQL 1867
Cdd:COG4372 190 KEANRNAEKEEELAEAEKlIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270
....*....|....*....|....*....|....*
gi 688558683 1868 EEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDE 1902
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1038-1193 |
1.91e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1038 FLKEKKLLEDRvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELqa 1117
Cdd:PRK12705 24 LLKKRQRLAKE-AERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1118 qiDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQ---LRELQAQ---LAELQEDLESEKAARNKAEKLKRDLSEELEA 1191
Cdd:PRK12705 101 --DNLENQLEEREKALSARELELEELEKQLDNELYRvagLTPEQARkllLKLLDAELEEEKAQRVKKIEEEADLEAERKA 178
|
..
gi 688558683 1192 LK 1193
Cdd:PRK12705 179 QN 180
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1555-1729 |
1.94e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.44 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1555 EDLISSKDDvGKNVHELEkSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRA 1634
Cdd:pfam09787 24 EKLIASLKE-GSGVEGLD-SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1635 LVKQV---REMEAEL-----------EDERKQRALAVAAKKKLEMDLKDVEAQIEA---ANKARDEAIKQLRKLQAQMKD 1697
Cdd:pfam09787 102 LATERsarREAEAELerlqeelryleEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQ 181
|
170 180 190
....*....|....*....|....*....|..
gi 688558683 1698 YQRELEEARTSRDEIFTQSKENEKKLKSLEAE 1729
Cdd:pfam09787 182 KQTMLEALSTEKNSLVLQLERMEQQIKELQGE 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
887-1072 |
1.96e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 887 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERK----HQQLLEEKNILAEQLQA--------------ETELFAEAE 948
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 949 EMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQShiqdleeQLDEEEAARQKLQLEKVTAEAKIKKMEEDI 1028
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 688558683 1029 LLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1072
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1082-1191 |
2.25e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1082 ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEELQAvlARGDEEVAQKNNALKQLRELQAQL 1161
Cdd:COG2268 220 NREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEAAYEIAE--ANAEREVQRQLEIAEREREIELQE 296
|
90 100 110
....*....|....*....|....*....|...
gi 688558683 1162 AELQEDLESEKA---ARNKAEKLKRDLSEELEA 1191
Cdd:COG2268 297 KEAEREEAELEAdvrKPAEAEKQAAEAEAEAEA 329
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1244-1742 |
2.32e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 43.01 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1244 TALEEISEQLEQAKRVKGNLEKN-------KQTLESDNKELTNEVKSLQQAKSESEHKRKKleaQLQEVMARFSEgEKVK 1316
Cdd:pfam15818 7 TSLLEALEELRMRREAETQYEEQigkiiveTQELKWQKETLQNQKETLAKQHKEAMAVFKK---QLQMKMCALEE-EKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1317 GELADRTHkiQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQdTQELLQEETRQKLNlssrirQLEEEKNNLLEQQEEE 1396
Cdd:pfam15818 83 YQLATEIK--EKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQ-LHLLAKEDHHKQLN------EIEKYYATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1397 EESRKNLEKQLA---TLQAQLVETKKKLEDDVGAL-EGLEEVKRKLQKDmEVTSQ-KLEEKAIAFDKLEKTKNRLQQELD 1471
Cdd:pfam15818 154 KENHGKLEQNVQeaiQLNKRLSALNKKQESEICSLkKELKKVTSDLIKS-KVTCQyKMGEENINLTIKEQKFQELQERLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1472 -DLMVDLDHQRQIVSNLEKKQKKFdqmlaeektISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERlnKQL 1550
Cdd:pfam15818 233 mELELNKKINEEITHIQEEKQDII---------ISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQR--EKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1551 RAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrdlqarDEQNEE 1630
Cdd:pfam15818 302 KENEEKFLNLQN-------EHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQ--------KKFEED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1631 KKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQReLEeaRTSRD 1710
Cdd:pfam15818 367 KKFQNVPEVNNENSEMSTEKSENLIIQKYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQV-LE--KSFKN 443
|
490 500 510
....*....|....*....|....*....|..
gi 688558683 1711 EIFTQSKENEKKLKSLEAEILQLQEDLASSER 1742
Cdd:pfam15818 444 EIDTSVPQDKNQSEISLSKTLCTDKDLISQGQ 475
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1342-1607 |
2.43e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1342 KKGIKLTKDVSSLESQlqdTQELLQEETRQklnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKL 1421
Cdd:pfam15905 66 QKNLKESKDQKELEKE---IRALVQERGEQ----DKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1422 E--DDVGALEGLEEVKRKLQKDMEVTSQKLEEKA-IAFDKLEKTKNRLQQelddLMVDLDHQRQIVSNLEKKQKKFDQML 1498
Cdd:pfam15905 139 EllKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMkEVMAKQEGMEGKLQV----TQKNLEHSKGKVAQLEEKLVSTEKEK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1499 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtl 1578
Cdd:pfam15905 215 IEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK--- 291
|
250 260
....*....|....*....|....*....
gi 688558683 1579 EQQVEEMRTQLEELEDELQATEDaKLRLE 1607
Cdd:pfam15905 292 EELLREYEEKEQTLNAELEELKE-KLTLE 319
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1529-1657 |
2.64e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1529 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVgknVHELEKSKRTLEQQVEEMRTQLEELEDEL---QATEDAKLR 1605
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQ---VERLEAEVEELEAELEEKDERIERLERELseaRSEERREIR 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1606 LEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAV 1657
Cdd:COG2433 463 KDREISRLDREIER-LERELEEERERIEELKRKLERLKELWKLEHSGELVPV 513
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1663-1833 |
2.67e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1663 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQ---RELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLAs 1739
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1740 seRARRHAEQE---RDELADEISNSASGKAALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELag 1816
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL-- 200
|
170
....*....|....*..
gi 688558683 1817 ersaaqksENARQQLER 1833
Cdd:pfam00529 201 --------KLAKLDLER 209
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1042-1205 |
2.75e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.97 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1042 KKLLEDRVGEMTSQLAEEEEKAKnlgKVKNKqemmMVDLEERLKKEEKTRQELEKA-KRKLDAETTDL-QDQIAELQAQI 1119
Cdd:cd22656 116 KKTIKALLDDLLKEAKKYQDKAA---KVVDK----LTDFENQTEKDQTALETLEKAlKDLLTDEGGAIaRKEIKDLQKEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1120 DELK----IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLK---RDLSEELEAL 1192
Cdd:cd22656 189 EKLNeeyaAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIG---PAIPALEKLQgawQAIATDLDSL 265
|
170
....*....|...
gi 688558683 1193 KTELEDTLDTTAA 1205
Cdd:cd22656 266 KDLLEDDISKIPA 278
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1087-1219 |
2.76e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1087 EEKTRQELEKAKrKLDAE-TTDLQDQIAELQAqidELKIQLAKKEEELQAVLARGDEEvaqknNALKQLRELQAQLAELQ 1165
Cdd:PTZ00491 642 DERTRDSLQKSV-QLAIEiTTKSQEAAARHQA---ELLEQEARGRLERQKMHDKAKAE-----EQRTKLLELQAESAAVE 712
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1166 ---------------EDLESE---KAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1219
Cdd:PTZ00491 713 ssgqsraealaeaeaRLIEAEaevEQAELRAKALRIEAEAELEKLRKRQELELEYEQAQNELEIAKAKELAD 784
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1169-1386 |
2.84e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.68 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1169 ESEKAARNKAEKLKRdlSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNhESQIQEMRQRHGTALEE 1248
Cdd:TIGR00927 637 EAEHTGERTGEEGER--PTEAEGENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEG-EGEIEAKEADHKGETEA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1249 ISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGEL-ADRTHKIQ 1327
Cdd:TIGR00927 713 EEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIqAGEDGEMK 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1328 TElDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1386
Cdd:TIGR00927 793 GD-EGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEK 850
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1093-1193 |
3.21e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1093 ELEKAKRKLDAETTDLQ---DQIAELQAQIDELKiQLAKK----EEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1165
Cdd:COG0497 276 ELEEAASELRRYLDSLEfdpERLEEVEERLALLR-RLARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAE 354
|
90 100 110
....*....|....*....|....*....|....
gi 688558683 1166 EDLEsEKAA------RNKAEKLKRDLSEELEALK 1193
Cdd:COG0497 355 AELL-EAAEklsaarKKAAKKLEKAVTAELADLG 387
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1081-1260 |
3.39e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.34 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1081 EERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKI------QLAKKEEEL---QAVLARGDEEVaqknnal 1151
Cdd:pfam10168 546 EEYLKKHDLAREEIQKRVKLLKLQK---EQQLQELQSLEEERKSlseraeKLAEKYEEIkdkQEKLMRRCKKV------- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1152 kqLRELQAQLAELqedLESEkaarnkaeklkRDLSEELEALKTELEdTLDttAAQQELRSKREQEVAELKKAIDDETRN- 1230
Cdd:pfam10168 616 --LQRLNSQLPVL---SDAE-----------REMKKELETINEQLK-HLA--NAIKQAKKKMNYQRYQIAKSQSIRKKSs 676
|
170 180 190
....*....|....*....|....*....|....*.
gi 688558683 1231 ------HESQIQEMRQRHGtalEEISEQLEQAKRVK 1260
Cdd:pfam10168 677 lslsekQRKTIKEILKQLG---SEIDELIKQVKDIN 709
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
986-1382 |
3.45e-03 |
|
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: 42.15 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 986 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVTA----------------------EAKIKKMEEDILLLEDQNSK--FLKE 1041
Cdd:pfam06160 5 RKKIYKEIDELEERKNELMNLPVQEELSKVKKlnltgetqekfeewrkkwddivTKSLPDIEELLFEAEELNDKyrFKKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1042 KKLLEdrvgEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ-------IAE 1114
Cdd:pfam06160 85 KKALD----EIEELLDDIEEDIKQILE----------ELDELLESEEKNREEVEELKDKYRELRKTLLANrfsygpaIDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1115 LQAQIDELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALK- 1193
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTES----GDYLEAR-----EVLEKLEEETDALEELMEDIPPL---YEELKTELPDQLEELKe 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1194 --TELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEK 1265
Cdd:pfam06160 219 gyREMEeegyalEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1266 NKQTLESD-------NKELTNEVKSLQQ----AKSESEHKR------KKLEAQLQEVMARFSEGEKVKGELADRTHKIQT 1328
Cdd:pfam06160 292 NLPEIEDYlehaeeqNKELKEELERVQQsytlNENELERVRglekqlEELEKRYDEIVERLEEKEVAYSELQEELEEILE 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 688558683 1329 ELDNVsclledaEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1382
Cdd:pfam06160 372 QLEEI-------EEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1042-1224 |
3.63e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1042 KKLLEDRVGEMTSQLAE-EEEKAKNLGKVKnKQEMMMVDLEERLKK-EEKTRQELEKA-----------KRKLDAETTDL 1108
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEaRQALAQVIANQK-RLERQLEELEAEAEKwEEKARLALEKGredlarealerKAELEAQAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1109 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNAlkqlrELQAQLAELQEDLESEKAAR--NKAEKLKRDLS 1186
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-----KAQEKVNEALSGIDSDDATSalERMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 688558683 1187 EELEALKT-ELEDTLDTTAAQQELRSKREQEVAELKKAI 1224
Cdd:COG1842 179 ARAEAAAElAAGDSLDDELAELEADSEVEDELAALKAKM 217
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1428-1937 |
3.82e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1428 LEGLEEVKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISAR 1507
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHG----KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1508 YaeerdraeaearekdtkalsmaRALDEALEAKEEFERLNKQLRAEMEDLISSKddvgkNVHELEKSKRTLEQQVEEMRT 1587
Cdd:TIGR00618 245 L----------------------TQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1588 QLEELEDELQATEDAKLRLEVNMQAM-KAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKK---L 1663
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1664 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1743
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1744 RRHAEQERDELADEISNSASGKAALLDEKRRLEARIAqleeELEEEQSNMELLNDRFRKTTMQVdTLNTELAGERSAAQK 1823
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMQR 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1824 SENARQQLERQNKDLKSKLQELE---GSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1900
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510
....*....|....*....|....*....|....*..
gi 688558683 1901 DERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRA 1937
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1351-1571 |
3.85e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1351 VSSLESQLqDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEG 1430
Cdd:PHA02562 190 IDHIQQQI-KTYNKNIEEQRKK---NGENIARKQNKYDELVEEA------KTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1431 LEEVKRKLQKDME----------------VTSQKLEEKAiafDKLEKTKNR---LQQELDDLMVDLDHQRQIVSNLEKKQ 1491
Cdd:PHA02562 260 LNTAAAKIKSKIEqfqkvikmyekggvcpTCTQQISEGP---DRITKIKDKlkeLQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1492 KKFDQMLAEEKTISARYAEERDRAeaeareKDTKALsMARALDEALEAKEEFERLNKQLraemEDLISSKDDVGKNVHEL 1571
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKA------KKVKAA-IEELQAEFVDNAEELAKLQDEL----DKIVKTKSELVKEKYHR 405
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1531-1965 |
4.20e-03 |
|
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: 42.15 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1531 RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELqatedaklrlEVNM 1610
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDEL----------EKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1611 QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQ-RALAVAAKKKLEMDLKDVEA---QIEAANKA--RDEA 1684
Cdd:pfam06160 156 AEIEEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyrEMEEEGYAleHLNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1685 IKQLRKLQAQMKDYQRELEEARTsrdeiftqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1764
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLEL---------DEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1765 KAALLDEKRRLeariaqleeeleeeQSNMELLND---RFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1841
Cdd:pfam06160 307 NKELKEELERV--------------QQSYTLNENeleRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1842 LQELEGSVKsKFKASIAALEakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEdeRRH----ADQYKEQMEKAN 1917
Cdd:pfam06160 373 LEEIEEEQE-EFKESLQSLR--------------KDELEAREKLDEFKLELREIKRLVE--KSNlpglPESYLDYFFDVS 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 688558683 1918 SRMKQLKRQLeeaeeeatraNASR---RKLQRELDDATEASEGLSREVNTL 1965
Cdd:pfam06160 436 DEIEDLADEL----------NEVPlnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1630-1925 |
4.63e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1630 EKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1709
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1710 DEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKaALLDEKRRLEARIAQLEEELEEE 1789
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1790 QSNMELLNdRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKAsIAALEAKILqlee 1869
Cdd:COG1340 160 EKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK-ADELHEEII---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1870 qleqeakeraAANKIVRRTEKKLKEVFMQVEDERRHADQyKEQMEKANSRMKQLKR 1925
Cdd:COG1340 234 ----------ELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1042-1193 |
4.65e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1042 KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD----AETTDLQDQIAELQA 1117
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEdcdpTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1118 QIDELKIQLAKKEEELQAVlargdEEVAQKNNALKQlrELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALK 1193
Cdd:smart00787 219 EIMIKVKKLEELEEELQEL-----ESKIEDLTNKKS--ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1668-1772 |
4.70e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.34 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1668 KDVEAQIEAANKARDEAIKQLrklqaqmKDYQRELEEARTSRDEIFTQSKENEKKLKslEAEILQLQEDLASS-ERARRH 1746
Cdd:cd06503 33 EKIAESLEEAEKAKEEAEELL-------AEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAE 103
|
90 100
....*....|....*....|....*.
gi 688558683 1747 AEQERDELADEISNSASGKAALLDEK 1772
Cdd:cd06503 104 IEQEKEKALAELRKEVADLAVEAAEK 129
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1040-1196 |
4.73e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1040 KEKKL--LEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKakrkLDAEttdLQDQIAELQA 1117
Cdd:PRK09039 51 KDSALdrLNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERSRLQA----LLAE---LAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558683 1118 QIDELKIQLAkkeeELQAVLARgdeevaqknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTEL 1196
Cdd:PRK09039 117 RAGELAQELD----SEKQVSAR----------ALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1561-1724 |
5.26e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1561 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEdaKLRLEVNMQAmkaqfdrdlqardEQNEEKKRALVkqvr 1640
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE--KLKEELEEKK-------------EKLQEEEDKLL---- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1641 emeAELEDERKQRalavaakkklemdlkdveaqIEAANKARDEAIKQLRKLQA---------QMKDYQRELEEARTSRDE 1711
Cdd:PRK00409 569 ---EEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKggyasvkahELIEARKRLNKANEKKEK 625
|
170
....*....|...
gi 688558683 1712 IFTQSKENEKKLK 1724
Cdd:PRK00409 626 KKKKQKEKQEELK 638
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1068-1191 |
5.29e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1068 KVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQK 1147
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS---FERLAELRDELAELE-------EELEALKARWEAEKELI 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 688558683 1148 NNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1191
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1274-1503 |
5.31e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.55 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1274 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG-----EKVKGELADRTHKIQTELDNVSC---------LLED 1339
Cdd:pfam05667 249 LKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSsttdtGLTKGSRFTHTEKLQFTNEAPAAtsspptkveTEEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1340 AEKKGiklTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQlVETKK 1419
Cdd:pfam05667 329 LQQQR---EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEEL--------------EELKEQNEELEKQ-YKVKK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1420 KLeddVGALEGLEEVKRKLQKDMEVTSQKLEE-------------------KAIAFDKLEKTKNRLQ--QELDDLMvdld 1478
Cdd:pfam05667 391 KT---LDLLPDAEENIAKLQALVDASAQRLVElagqwekhrvplieeyralKEAKSNKEDESQRKLEeiKELREKI---- 463
|
250 260
....*....|....*....|....*
gi 688558683 1479 hqRQIVSNLEKKQKKFDQMLAEEKT 1503
Cdd:pfam05667 464 --KEVAEEAKQKEELYKQLVAEYER 486
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1510-1759 |
5.54e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1510 EERDRAEAEAREKDTKalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKskrtLEQQVEEMRTQL 1589
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEE----AEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1590 EELEDELQATEDAKLRLEVNMQAMKAqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKD 1669
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKE--------IAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1670 V-------EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskenEKKLKSLEAEILQLQEDLASSER 1742
Cdd:pfam00261 153 VgnnlkslEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFA--------------ERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|....*..
gi 688558683 1743 ARRHAEQERDELADEIS 1759
Cdd:pfam00261 219 KYKAISEELDQTLAELN 235
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1619-1754 |
5.62e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1619 RDLQARDEQNEEKKRALVKQVREMEAELEDERkqralavaakkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1698
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEE----------------IRRLEEQVERLEAEVEELEAELEEKDERIERL 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558683 1699 QRELEEARTSRDEiftqSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDEL 1754
Cdd:COG2433 447 ERELSEARSEERR----EIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1091-1197 |
5.72e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.25 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1091 RQELEKAKRKLDAETTDLQDQIAELQAQIDELkIQLAKKEEELQAVLArgdeevAQKNNALKqlrELQAQLAELQEDLES 1170
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAY-AAAQAALATAQKELA------NAQAQALQ---TAQNNLATAQAALAN 329
|
90 100
....*....|....*....|....*..
gi 688558683 1171 EKAARNKAEKLKRDLSEELEALKTELE 1197
Cdd:TIGR04320 330 AEARLAKAKEALANLNADLAKKQAALD 356
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1540-1692 |
6.01e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1540 KEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA--TEDAKLRLEVNMQAMKAQF 1617
Cdd:cd22656 109 DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDllTDEGGAIARKEIKDLQKEL 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1618 DrdlQARDEQNEEKKRALvKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeaankarDEAIKQLRKLQ 1692
Cdd:cd22656 189 E---KLNEEYAAKLKAKI-DELKALIADDEAKLAAALRLIADLTAADTDLDNLLALI-------GPAIPALEKLQ 252
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
1087-1197 |
6.32e-03 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 38.04 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1087 EEKTRQELEKAKRkldaettdlqDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQE 1166
Cdd:pfam16516 1 EELKRKEMEKVYK----------DEIDCLQAQLQAAEEALAAKQREIDEL----KQEIAQKEEDLETISVLKAQAEVYRS 66
|
90 100 110
....*....|....*....|....*....|.
gi 688558683 1167 DLESEKAARNKAEKLKRDLSEELEALKTELE 1197
Cdd:pfam16516 67 DFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
892-1226 |
6.73e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 892 EEEMQAKDEELIKVKERQVKVENELVE--------MERKHQQLLEEKNILAEQLQAETELFAEAEEMRA-RLVAKKQELE 962
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINksineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 963 EILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarqklqlekvtaeakIKKMEEDILLLEDQNSKFLKEK 1042
Cdd:PRK01156 569 SWLNALAVISLIDIETNRSRSNEIKKQLNDL---------------------------ESRLQEIEIGFPDDKSYIDKSI 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1043 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvdleeRLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL 1122
Cdd:PRK01156 622 REIENEANNLNNKYNEIQENKILIEKLRGKID--------NYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1123 KIQLAKKEEELQAVLARgdeevaqknnalkqLRELQAQLAELQEDLESEKaarnKAEKLKRDLSEELEALKTELEDTLDT 1202
Cdd:PRK01156 694 KANRARLESTIEILRTR--------------INELSDRINDINETLESMK----KIKKAIGDLKRLREAFDKSGVPAMIR 755
|
330 340
....*....|....*....|....
gi 688558683 1203 TAAQQELRSKREQEVAELKKAIDD 1226
Cdd:PRK01156 756 KSASQAMTSLTRKYLFEFNLDFDD 779
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1207-1469 |
6.85e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1207 QELRSKREQEVAELK--KAIDDETRN--HESQIQEMRQRHGTA-LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTnEV 1281
Cdd:pfam15905 59 LELKKKSQKNLKESKdqKELEKEIRAlvQERGEQDKRLQALEEeLEKVEAKLNAAVREKTSLSASVASLEKQLLELT-RV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1282 KSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDT 1361
Cdd:pfam15905 138 NELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1362 QELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1441
Cdd:pfam15905 218 KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE 297
|
250 260
....*....|....*....|....*...
gi 688558683 1442 MEVTSQKLEEkaiafdKLEKTKNRLQQE 1469
Cdd:pfam15905 298 YEEKEQTLNA------ELEELKEKLTLE 319
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1575-1729 |
7.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1575 KRTLEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFDRDLQARDEQNEEKKRALVKQVREMEAELED 1648
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1649 ERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE--LEEAR-TSRDEIFTQSKENEKKLKs 1725
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEeEARHEAAVLIKEIEEEAK- 183
|
....
gi 688558683 1726 LEAE 1729
Cdd:PRK12704 184 EEAD 187
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1511-1754 |
7.60e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1511 ERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEmedlisskdDVGKNVHELEKSKRTLEQQVEEmRTQLE 1590
Cdd:COG5022 829 EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYL---------QSAQRVELAERQLQELKIDVKS-ISSLK 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1591 E--LEDELQATEdaklrlevnmqaMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEM-DL 1667
Cdd:COG5022 899 LvnLELESEIIE------------LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVEsKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1668 KDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqsKENEKKLKSLEAEILQLQ--EDLASSERARR 1745
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAL----QESTKQLKELPVEVAELQsaSKIISSESTEL 1042
|
....*....
gi 688558683 1746 HAEQERDEL 1754
Cdd:COG5022 1043 SILKPLQKL 1051
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1031-1423 |
7.82e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1031 LEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGK-----VKNKQEMMMV---------DLEERLKKEEKTRQELEK 1096
Cdd:PRK10246 535 LEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQeeqalTQQWQAVCASlnitlqpqdDIQPWLDAQEEHERQLRL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1097 AKRKLDaettdLQDQIAELQAQIDELKIQLAKKEEELQAVLAR--------GDEEV------------AQKNNALKQLRE 1156
Cdd:PRK10246 615 LSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqeDEEASwlatrqqeaqswQQRQNELTALQN 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1157 LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEalktelEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQ 1236
Cdd:PRK10246 690 RIQQLTPLLETLPQSDDLPHSEETVALDNWRQVH------EQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVF 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1237 EMRQRHGTAL--EEISEQLEQakrvkgnlekNKQTLESDnkeltnevksLQQAKSESEHKRKKLEAQLQevmarfsegek 1314
Cdd:PRK10246 764 DDQQAFLAALldEETLTQLEQ----------LKQNLENQ----------RQQAQTLVTQTAQALAQHQQ----------- 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1315 vkgeladrthkiqteldnvsclledAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqe 1394
Cdd:PRK10246 813 -------------------------HRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNR-------- 859
|
410 420
....*....|....*....|....*....
gi 688558683 1395 eeeesrknleKQLATLQAQLVETKKKLED 1423
Cdd:PRK10246 860 ----------QQQQALMQQIAQATQQVED 878
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1237-1558 |
8.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1237 EMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1316
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1317 GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknNLLEQQEEE 1396
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1397 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1476
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1477 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1556
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
..
gi 688558683 1557 LI 1558
Cdd:COG4372 335 LL 336
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
887-1188 |
8.85e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 887 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 966
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 967 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1046
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1047 DRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQL 1126
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558683 1127 AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1188
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1074-1304 |
8.96e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1074 EMMMVDLEERLkkeekTRQELEKAKRKLDAETTDlQDQIAELQAQIDELKIQLAKKEEELQAvlargdeevaqknnALKQ 1153
Cdd:pfam05622 274 EIMPAEIREKL-----IRLQHENKMLRLGQEGSY-RERLTELQQLLEDANRRKNELETQNRL--------------ANQR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1154 LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTeledtldttaAQQELRSKREQeVAELKKAIDDETRNHES 1233
Cdd:pfam05622 334 ILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHE----------AQSELQKKKEQ-IEELEPKQDSNLAQKID 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558683 1234 QIQEMRQRHgtalEEISEQLEQakRVKGNLEKNK---QTLESD-NKELTNEVKSLQQAKSESEHKRKKLEAQLQE 1304
Cdd:pfam05622 403 ELQEALRKK----DEDMKAMEE--RYKKYVEKAKsviKTLDPKqNPASPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1641-1734 |
8.99e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1641 EMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLR-KLQAQMKDYQRELEEARTSRDEIFT--QSK 1717
Cdd:cd16269 195 EKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKeKMEEERENLLKEQERALESKLKEQEalLEE 274
|
90
....*....|....*..
gi 688558683 1718 ENEKKLKSLEAEILQLQ 1734
Cdd:cd16269 275 GFKEQAELLQEEIRSLK 291
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1668-1772 |
9.23e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 38.62 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1668 KDVEAQIEAANKARDEAikqlrklQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKslEAEILQLQEDLAS-SERARRH 1746
Cdd:COG0711 34 EKIADGLAEAERAKEEA-------EAALAEYEEKLAEARAEAAEIIAEARKEAEAIA--EEAKAEAEAEAERiIAQAEAE 104
|
90 100
....*....|....*....|....*.
gi 688558683 1747 AEQERDELADEISNSASGKAALLDEK 1772
Cdd:COG0711 105 IEQERAKALAELRAEVADLAVAIAEK 130
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1487-1970 |
9.48e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1487 LEKKQKKFDQMLAEEKTISARYAEE-RDRAEAEAREKDTKALSMAR------------ALDEALEAKEEFERLNKQLRAE 1553
Cdd:NF041483 169 LDESRAEAEQALAAARAEAERLAEEaRQRLGSEAESARAEAEAILRrarkdaerllnaASTQAQEATDHAEQLRSSTAAE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1554 medlissKDDVGKNVHELEkskRTLEQQVEEMRTQLEELEdelqaTEDAKLRLEVNMQAMKAqfdrdLQARDEQNEEKKR 1633
Cdd:NF041483 249 -------SDQARRQAAELS---RAAEQRMQEAEEALREAR-----AEAEKVVAEAKEAAAKQ-----LASAESANEQRTR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1634 ALVKQVREMEAELEDErkqralAVAAKKKLEMDLKDVEAQieaANKARDEAIKQLRKLQAQmkDYQRELEEARTSRDEIF 1713
Cdd:NF041483 309 TAKEEIARLVGEATKE------AEALKAEAEQALADARAE---AEKLVAEAAEKARTVAAE--DTAAQLAKAARTAEEVL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1714 TQSKENEKKLKSLEAEilqlqedlaSSERARRHAEQERDELADEISNSASG-KAALLDEKRRLEARIAQleeeleeeqsn 1792
Cdd:NF041483 378 TKASEDAKATTRAAAE---------EAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE----------- 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1793 melLNDRFRKTTMQVDTLNTELA--GERSAAQKSENARQQLERQNKDLKSKLqelegsvkSKFKASIAALEAKILQLEEQ 1870
Cdd:NF041483 438 ---LQEEARRLRGEAEQLRAEAVaeGERIRGEARREAVQQIEEAARTAEELL--------TKAKADADELRSTATAESER 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558683 1871 LEQEAKERAA-----ANKIVRRT----EKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASR 1941
Cdd:NF041483 507 VRTEAIERATtlrrqAEETLERTraeaERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEE 586
|
490 500 510
....*....|....*....|....*....|.
gi 688558683 1942 RKLQRE--LDDATEASEGLSREVNTLKNRLR 1970
Cdd:NF041483 587 RLTAAEeaLADARAEAERIRREAAEETERLR 617
|
|
|