|
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 ... |
867-1947 |
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: 1479.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 867 TRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDL 946
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 947 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR 1026
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1027 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAK 1106
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1107 KEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQE 1186
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1187 LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAK 1266
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1267 SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE 1346
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1347 TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQK 1426
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1427 LEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALS 1506
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1507 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1586
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1587 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQL 1666
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1667 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAL 1746
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1747 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGS 1826
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1827 VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLE 1906
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 688558694 1907 EAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1947
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-790 |
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: 1434.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP----------------GELERQLLQANPILESFGNAKTVKNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14920 145 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14920 225 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14920 305 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14920 385 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAA 661
Cdd:cd14920 465 FQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 662 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 741
Cdd:cd14920 545 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558694 742 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14920 625 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
102-790 |
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: 1312.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkavklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKK---------------KGTLEDQILQANPILEAFGNAKTVRNNNSSRF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYR-FLSNGNIPIPGQQ 340
Cdd:cd01377 146 GKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd01377 226 DAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd01377 306 KVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTH- 579
Cdd:cd01377 385 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKs 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 580 GKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgldqvagmnETAFG 659
Cdd:cd01377 463 KNFKKPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGG 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 660 AAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 739
Cdd:cd01377 532 GKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRII 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 688558694 740 FQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd01377 612 FAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-790 |
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: 1244.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS------------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14932 149 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14932 229 KELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14932 309 VGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14932 389 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGaA 661
Cdd:cd14932 469 FQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-A 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 662 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 741
Cdd:cd14932 548 FKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558694 742 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14932 628 EFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-790 |
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: 1195.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------------------GELERQLLQANPILEAFGNAKTVKNDNSSRF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14919 142 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14919 222 KDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14919 302 VGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14919 382 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAA 661
Cdd:cd14919 462 FQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 662 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 741
Cdd:cd14919 542 FKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQ 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558694 742 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14919 622 EFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
102-790 |
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: 1185.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkavklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----------------TGELEKQLLQANPILEAFGNAKTVKNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14921 145 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14921 225 DEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14921 305 VGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14921 385 LQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAA 661
Cdd:cd14921 465 FQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 662 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 741
Cdd:cd14921 545 SKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558694 742 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14921 625 EFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-790 |
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: 1181.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN------------SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd15896 149 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd15896 229 KDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd15896 309 VGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd15896 389 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNEtaFGAA 661
Cdd:cd15896 469 FFKPKKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 662 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 741
Cdd:cd15896 547 FKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558694 742 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd15896 627 EFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
102-790 |
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: 1165.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPkavklqNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAV------NPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14911 154 GKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14911 234 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14911 314 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14911 394 LQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 582 FQKpRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrIVGLDQVAgMNETAFGAa 661
Cdd:cd14911 471 FMK-TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 662 yKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 741
Cdd:cd14911 547 -RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558694 742 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14911 626 EFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-790 |
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: 1140.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----------------GELERQLLQANPILEAFGNAKTVKNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQd 341
Cdd:cd14930 145 GKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14930 224 RELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14930 304 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd14930 384 LQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 582 FQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAa 661
Cdd:cd14930 464 FQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 662 yKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 741
Cdd:cd14930 543 -RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558694 742 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14930 622 EFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
90-790 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1103.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 90 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 169
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 170 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkavklqngilfYGELERQLLQANPILESFGN 249
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------------------VGRLEEQILQSNPILEAFGN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 250 AKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL 329
Cdd:pfam00063 141 AKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 330 SNGN-IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNV 408
Cdd:pfam00063 221 SQSGcYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 409 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLN 488
Cdd:pfam00063 301 TELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 489 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTF 568
Cdd:pfam00063 381 SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 569 VDKLVQEQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLD 648
Cdd:pfam00063 458 LDKLYSTFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAA 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 649 QvagmNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 728
Cdd:pfam00063 537 A----NESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIR 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 729 ICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:pfam00063 613 IRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
83-802 |
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: 1005.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 83 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 162
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 163 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnippespkavklqngilfyGELERQLLQANP 242
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV----------------------GSVEDQILESNP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 243 ILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEG 322
Cdd:smart00242 139 ILEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 323 FNSYRFLSNGN-IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENT-AAQKL 400
Cdd:smart00242 219 PEDYRYLNQGGcLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 401 CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIA 480
Cdd:smart00242 299 AELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 481 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWF 560
Cdd:smart00242 378 GFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 561 PKATDKTFVDKLVQEQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKD 640
Cdd:smart00242 455 PKGTDQTFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 641 vdrivgldqvagmnetafGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 720
Cdd:smart00242 534 ------------------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRY 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 721 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRTGVLAHLEEE 800
Cdd:smart00242 596 LGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEEL 675
|
..
gi 688558694 801 RD 802
Cdd:smart00242 676 RE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
39-1363 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 911.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 39 VWVPSERHGFEAASIREERGEEVLVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 113
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 114 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 193
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 194 VIQYLAHVASSHkgrkdhniPPESpkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 273
Cdd:COG5022 172 IMQYLASVTSSS--------TVEI-------------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 274 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQETMEAM 352
Cdd:COG5022 231 EICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 353 HIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQT 432
Cdd:COG5022 311 KTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 433 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 512
Cdd:COG5022 390 LEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 513 LEQEEYQREGIEWSFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVDKLVQ--EQGTHGKFQKPRQLKD 590
Cdd:COG5022 469 LEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 591 KadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVgldqvagmnetafgaayktKKGMFR 670
Cdd:COG5022 547 K--FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFP 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 671 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 750
Cdd:COG5022 606 TLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 751 TPNA----IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDIIIYFQSVCRGYLARKAFA 826
Cdd:COG5022 686 SPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYL 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 827 KKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVkerQVKVENELVEMERKHQQLLE 906
Cdd:COG5022 766 QALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFSL 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 907 EKNILAEQlqaetelFAEAEEMRARLVAKKQelEEILHDLESRVEEEEERNQSLQNEKKKMQShiqdleeqldeeeAARQ 986
Cdd:COG5022 843 KAEVLIQK-------FGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDVKSISS-------------LKLV 900
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 987 KLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEdrvgemTSQLaeEEEKAKNLGKVKNKQEMMMVDleerlKKEE 1066
Cdd:COG5022 901 NLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLN------NIDL--EEGPSIEYVKLPELNKLHEVE-----SKLK 967
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1067 KTRQELEKAKRKLDAETTDLQDQIAELQAQIDElkiqLAKKEEELQAVlargdeevaqkNNALKQLRELQAQLAELQEDL 1146
Cdd:COG5022 968 ETSEEYEDLLKKSTILVREGNKANSELKNFKKE----LAELSKQYGAL-----------QESTKQLKELPVEVAELQSAS 1032
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1147 E------SEKAARNKAEKLKRD-------LSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQI 1213
Cdd:COG5022 1033 KiissesTELSILKPLQKLKGLlllennqLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPA 1112
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1214 QEMR-----QRHGTALEEISEQLEQA----KRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEV- 1283
Cdd:COG5022 1113 NVLQfivaqMIKLNLLQEISKFLSQLvntlEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKs 1192
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1284 MARFSEGEKVKGELADRTHKIQTElDNVSCLLEDAEKKGIKLT------KDVSSLESQLQDTQELLQEETRQKLNLSSRI 1357
Cdd:COG5022 1193 KLSSSEVNDLKNELIALFSKIFSG-WPRGDKLKKLISEGWVPTeystslKGFNNLNKKFDTPASMSNEKLLSLLNSIDNL 1271
|
....*.
gi 688558694 1358 RQLEEE 1363
Cdd:COG5022 1272 LSSYKL 1277
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
102-790 |
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: 853.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-----------------ASSIEQQILQSNPILEAFGNAKTVRNDNSSR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL-----SNGNIP 335
Cdd:cd00124 144 FGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 336 IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNT--DQASMPENTAAQKLCHLLGMNVMEFTR 413
Cdd:cd00124 224 IDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFQLNSFEQ 492
Cdd:cd00124 304 ALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 493 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKL 572
Cdd:cd00124 384 LCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 573 VQEQGTHGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkdvdrivgldqvag 652
Cdd:cd00124 461 YSAHGSHPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 653 mnetafgaayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 732
Cdd:cd00124 519 -----------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRA 575
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 733 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd00124 576 GYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
102-790 |
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: 779.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKAvklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTG----------GTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQ 339
Cdd:cd14927 151 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14927 230 DDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14927 310 VKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 578
Cdd:cd14927 389 EKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 579 HGKFQKPR---QLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdriVGLDQVAgmnE 655
Cdd:cd14927 466 SPNFQKPRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDSTE---D 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 656 TAFGAAYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 734
Cdd:cd14927 540 PKSGVKEKRKKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGF 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 735 PNRIVFQEFRQRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14927 620 PNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
103-790 |
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: 761.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASShkgrkdhnIPPESPKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT--------GDLAKKKDSKMK------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQ 340
Cdd:cd14913 148 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASID 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14913 227 DAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14913 307 KVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTH 579
Cdd:cd14913 386 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 580 GKFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqVAGMNETA 657
Cdd:cd14913 463 NNFQKPKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FATADADS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 658 FGAAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 736
Cdd:cd14913 534 GKKKVAKKKGsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPN 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 737 RIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14913 614 RILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
102-790 |
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: 742.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKAvklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKT------DEAAKSK----------GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQ 340
Cdd:cd14909 145 GKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14909 225 DGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14909 305 KVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 579
Cdd:cd14909 384 KLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 580 GKFQKPRQLK---DKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivGLDQVAGMNET 656
Cdd:cd14909 461 APFQKPKPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 657 AFGAAykTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 736
Cdd:cd14909 536 KGGRG--KKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPN 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 737 RIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14909 614 RMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
102-790 |
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: 723.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK------------------GSLEDQIIQANPVLEAFGNAKTTRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHL-RSDLLLEGFNSYRFLSNGNIPIPGQQ 340
Cdd:cd14934 143 GKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14934 223 DGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14934 303 KVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 579
Cdd:cd14934 382 KLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 580 GKFQKPRQLKDK---ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqvagmnET 656
Cdd:cd14934 459 SNFLKPKGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EE 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 657 AFGAAYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 735
Cdd:cd14934 525 APAGSKKQKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFP 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 736 NRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14934 605 NRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
103-790 |
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: 715.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippESpkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET--------------QVEEKVLASNPIMEAFGNAKTTRNDNSSRF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQ 340
Cdd:cd01380 140 GKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd01380 220 DAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd01380 300 VTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYAN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTH 579
Cdd:cd01380 380 EKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 580 GK--FQKPRQLKDKadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKfvaelwkdvdrivgldqvagmneta 657
Cdd:cd01380 456 PNkhFKKPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR------------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 658 fgaayktKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 737
Cdd:cd01380 509 -------KK----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSR 577
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 688558694 738 IVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd01380 578 WTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
103-790 |
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: 703.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippESPKAvklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPGK----------GTLEDQIIQANPALEAFGNAKTVRNDNSSRF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQ 339
Cdd:cd14917 147 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELL-DMLLITNNpyDYAFISQGETTVASI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14917 226 DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14917 306 VKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 578
Cdd:cd14917 385 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 579 HGKFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqVAGMNET 656
Cdd:cd14917 462 SNNFQKPRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 657 AFGAAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 735
Cdd:cd14917 533 IEKGKGKAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFP 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 736 NRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14917 613 NRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
102-790 |
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: 702.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkavKLqngilfyGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKK------------KL-------GALEDQIMQANPVLEAFGNAKTLRNDNSSRF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhLRsDLLLEGFN--SYRFLSNGNIPIPGQ 339
Cdd:cd14929 142 GKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE-LR-DLLLVSANpsDFHFCSCGAVAVESL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14929 220 DDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14929 300 IKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 578
Cdd:cd14929 379 EKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 579 HGKFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivglDQVAGmNET 656
Cdd:cd14929 456 SVHFQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAI 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 657 AFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 736
Cdd:cd14929 528 QFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPN 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 737 RIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14929 608 RLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
104-790 |
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: 686.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 183
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 184 GAGKTENTKKVIQYLAHVASSHKGRKDhnippespKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFGK 263
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKE--------ESGKMQ------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 264 FIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDK 342
Cdd:cd14918 149 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 343 DNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKV 422
Cdd:cd14918 229 EELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 423 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 502
Cdd:cd14918 309 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 503 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGK 581
Cdd:cd14918 388 QQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSAN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 582 FQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdrivgldqVAGMNETAFG 659
Cdd:cd14918 465 FQKPKVVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 660 AAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 739
Cdd:cd14918 537 KGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 688558694 740 FQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14918 617 YGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
103-790 |
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: 684.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEITSGKMQ------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14912 150 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14912 230 QEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14912 310 VGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHG 580
Cdd:cd14912 389 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 581 KFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagmnETAF 658
Cdd:cd14912 466 NFQKPKVVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG--------ASAG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 659 GAAYK--TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 735
Cdd:cd14912 538 GGAKKggKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 736 NRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14912 618 SRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
103-790 |
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: 683.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippespkavklqNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKE--------------NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQ 339
Cdd:cd14916 148 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELL-DMLLVTNNpyDYAFVSQGEVSVASI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14916 227 DDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14916 307 VKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 500 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GT 578
Cdd:cd14916 386 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 579 HGKFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdrivgldQVAGMNET 656
Cdd:cd14916 463 SNNFQKPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 657 AFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 736
Cdd:cd14916 536 GKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPN 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 737 RIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14916 616 RILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
103-790 |
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: 680.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEATSGKMQ------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14910 150 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd14910 230 QEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14910 310 VGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHG 580
Cdd:cd14910 389 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 581 KFQKPRQLKDK--ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdrivgldqVAGMNETAF 658
Cdd:cd14910 466 NFQKPKPAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 659 GAAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 737
Cdd:cd14910 538 GKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 738 IVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14910 618 ILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-790 |
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: 676.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQ------GTLEDQIIQANPLLEAFGNAKTVRNDNSSRFG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQ 340
Cdd:cd14923 149 KFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASID 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14923 228 DSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14923 308 KVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTH 579
Cdd:cd14923 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 580 GKFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdriVGLDQVAGMNETA 657
Cdd:cd14923 464 NNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 658 FGaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 737
Cdd:cd14923 541 GG---KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 738 IVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14923 618 ILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-790 |
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: 671.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKAVKLQngilfyGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEAASGKMQ------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYRF--LSNGNIPIPGQQ 340
Cdd:cd14915 150 KFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRI 420
Cdd:cd14915 229 DQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 421 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14915 309 KVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 501 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTH 579
Cdd:cd14915 388 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 580 GKFQKPRQLKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivglDQVAGMNETA 657
Cdd:cd14915 465 NNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 658 FGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 737
Cdd:cd14915 538 GKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 738 IVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14915 618 ILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
103-790 |
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: 643.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--HLRSDLLLEGFNSYRFLS-NGNIPIPGQ 339
Cdd:cd14883 137 KFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK-LCHLLGMNVMEFTRAILSP 418
Cdd:cd14883 217 NDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKiVAKLLGVDPDKLKKALTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 419 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYT 498
Cdd:cd14883 297 QINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 499 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGT 578
Cdd:cd14883 376 NEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 579 HGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrIVGLDQVAGMNETAf 658
Cdd:cd14883 453 HPYYEKPDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 659 GAAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 738
Cdd:cd14883 531 TTSRGTSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHL 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 688558694 739 VFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14883 610 TFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
103-790 |
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: 638.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqngilfygeLERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-------------------------IENEILQTNPILEAFGNAKTLRNDNSSRFG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQD 341
Cdd:cd01383 135 KLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd01383 215 AKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd01383 295 AGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANER 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 502 LQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK 581
Cdd:cd01383 375 LQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSC 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 582 FQKPRqlkDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdrivgldqVAGMNETAFGAA 661
Cdd:cd01383 452 FKGER---GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF------------ASKMLDASRKAL 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 662 YKTKKGMF----RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 737
Cdd:cd01383 516 PLTKASGSdsqkQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTR 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 688558694 738 IVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd01383 596 MTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
103-790 |
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: 634.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkaVKlqngilfygeleRQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VK------------DMLLASNPLLEAFGNAKTLRNDNSSRFG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQD 341
Cdd:cd01378 141 KYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 421
Cdd:cd01378 221 AADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 422 VG---RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYT 498
Cdd:cd01378 300 TGgggRSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 499 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVDKLVQEQG 577
Cdd:cd01378 380 NEKLQQIFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 578 THGKFQKPRQLKD--KADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgldqvagmne 655
Cdd:cd01378 457 NHPHFECPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 656 tafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 735
Cdd:cd01378 525 -------LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFA 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 736 NRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd01378 598 YRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
102-790 |
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: 610.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAHVAsshkGRKDHNIPPespkavklqngilfygeLERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEGRS-----------------VEQQVLESNPLLEAFGNAKTVRNNNSSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQ 339
Cdd:cd01384 140 FGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAIL 416
Cdd:cd01384 220 DDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALC 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 417 SpRIKVGRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCI 495
Cdd:cd01384 300 K-RVIVTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 496 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQE 575
Cdd:cd01384 378 NLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQT 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 576 QGTHGKFQKPRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgldqvagmne 655
Cdd:cd01384 455 LKDHKRFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 656 tafgaaYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 734
Cdd:cd01384 521 ------EGTSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGY 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 735 PNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 790
Cdd:cd01384 595 PTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
102-790 |
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: 605.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------------------WIEQQILEANPILEAFGNAKTIRNDNSSRF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQ 340
Cdd:cd01381 136 GKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKK--ERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSP 418
Cdd:cd01381 216 DAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 419 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFQLNSFEQLCIN 496
Cdd:cd01381 296 TIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCIN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 497 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVDKLVQE 575
Cdd:cd01381 376 FANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHST 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 576 QGTHGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkDVDRIVGLDqvagmne 655
Cdd:cd01381 452 HGNNKNYLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 656 tafgAAYKTKkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFP 735
Cdd:cd01381 523 ----TRKKSP-----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYP 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 736 NRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd01381 594 IRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
102-790 |
0e+00 |
|
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: 566.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG------------------------PIEQRILEANPLLEAFGNAKTVRNNNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLegfnsyrflsngnipIPGQQ 340
Cdd:cd01382 137 FGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNT-------DQASMPENTAAQKlchLLGMNVMEF-- 411
Cdd:cd01382 202 DVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrv 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 412 ---TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFQLN 488
Cdd:cd01382 279 sltTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 489 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTF 568
Cdd:cd01382 357 SFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHF 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 569 VDKLVQEQGTHGKFQKPRQ--------LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKD 640
Cdd:cd01382 434 TSAVHQKHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFES 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 641 VDRIVGldqvagmnetafGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 720
Cdd:cd01382 514 STNNNK------------DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQC 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 721 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd01382 582 SGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
102-790 |
0e+00 |
|
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: 565.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkavklqngilfygeLERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------------VEQRVLLANPILEAFGNAKTLRNNNSSRF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGfnSYRFLSNGN-IPIPGQQ 340
Cdd:cd14872 136 GKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA--AYGYLSLSGcIEVEGVD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCH---LLGMNVMEFTRAILS 417
Cdd:cd14872 214 DVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 418 PRIKV-GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCIN 496
Cdd:cd14872 294 RLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCIN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 497 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQ 576
Cdd:cd14872 374 FTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 577 GTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrivgLDQvagmnet 656
Cdd:cd14872 451 AAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQ------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 657 afgaayKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 736
Cdd:cd14872 520 ------KTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPF 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 737 RIVFQEFRQRYEILtPNAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14872 591 RYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
102-790 |
4.26e-175 |
|
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: 548.22 E-value: 4.26e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 176
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 177 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhniPPESPKAvkLQNGILFYGELERQLLQANPILESFGNAKTVKND 256
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGA----SGEGEAA--SEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 257 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPI 336
Cdd:cd14890 155 NSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 337 PGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKErntDQASMPEN-TAAQKLCH---LLGMNVMEFT 412
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE---NDTTVLEDaTTLQSLKLaaeLLGVNEDALE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 413 RAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQ 492
Cdd:cd14890 312 KALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 493 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFV 569
Cdd:cd14890 391 LCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 570 DKLVQEQGT-------------HGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvae 636
Cdd:cd14890 469 SQLHASFGRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 637 lwkdvdrivgldqvagmnetafgaayKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLD 716
Cdd:cd14890 542 --------------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLR 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558694 717 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14890 594 QLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
102-790 |
2.38e-172 |
|
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: 540.88 E-value: 2.38e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnippESPKAVKLQngilfygelerQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-------------QRRNNLVTE-----------QILEATPLLEAFGNAKTVRNDNSSRF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG-NIPIPGQQ 340
Cdd:cd01387 137 GKYLEVFFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ---ASMPENTAAQKLCHLLGMNVMEFTRAILS 417
Cdd:cd01387 216 DADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 418 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINY 497
Cdd:cd01387 296 KVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 498 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQG 577
Cdd:cd01387 375 ANENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 578 THGKFQKPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNeta 657
Cdd:cd01387 452 LNELYSKPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGK--- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 658 fgAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 737
Cdd:cd01387 527 --GRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVR 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 738 IVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 790
Cdd:cd01387 605 LPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
102-790 |
1.14e-167 |
|
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: 528.19 E-value: 1.14e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIppespkavklqngilfygeleRQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI---------------------KKIIEVNPLLESFGNAKTVRNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsdLLLEGFNSYRFL-SNGNIPIPGQ 339
Cdd:cd14903 137 FGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGM 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASM--PENTAAQKLCHLLGMNVMEFTRAILS 417
Cdd:cd14903 215 SDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 418 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINY 497
Cdd:cd14903 295 RTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 498 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVqeqG 577
Cdd:cd14903 374 ANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---S 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 578 THGKFQK----PRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrIVGLDQVAGM 653
Cdd:cd14903 447 IHKDEQDviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAAST 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 654 NETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQG 733
Cdd:cd14903 522 SLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAA 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 734 FPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 790
Cdd:cd14903 602 YPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-790 |
2.34e-165 |
|
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: 523.09 E-value: 2.34e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLahVASSHKGrkdhnippespkavklqngilfYGE-LERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG----------------------YGSgVEQTILGAGPVLEAFGNAKTAHNNNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQ 339
Cdd:cd01385 137 FGKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKER-NTDQASMPENTAAQKL-CHLLGMNVMEFTRAILS 417
Cdd:cd01385 217 DEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 418 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFQLNSFEQL 493
Cdd:cd01385 297 KKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 494 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLV 573
Cdd:cd01385 376 CINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 574 QEQGTHGKFQKPrQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdriVGLDQVA-- 651
Cdd:cd01385 453 QQHKDNKYYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAvf 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 652 --GMNETAFGAAY--------------------------------KTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRC 697
Cdd:cd01385 524 rwAVLRAFFRAMAafreagrrraqrtaghsltlhdrttksllhlhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRC 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 698 IIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDP 777
Cdd:cd01385 602 IKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDR 677
|
730
....*....|...
gi 688558694 778 NLYRIGQSKIFFR 790
Cdd:cd01385 678 DNYQIGKTKVFLK 690
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
103-790 |
1.66e-161 |
|
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: 510.28 E-value: 1.66e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVAsshkgrkdhnippespKAVklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG----------------KAN--------NRTLEEKILQVNPLMEAFGNARTVINDNSSRFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGagehLRSDLLLEGFNS-------YRFLSNGNIP 335
Cdd:cd01379 138 KYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKLpenkpprYLQNDGLTVQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 336 IPGQQD--KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENTAA-QKLCHLLGMNVM 409
Cdd:cd01379 214 DIVNNSgnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEAD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 410 EFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFQL 487
Cdd:cd01379 294 ELQEALTSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 488 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDK 566
Cdd:cd01379 374 NSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 567 TFVDKLvqEQGTHGKFQKpRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdvdrivg 646
Cdd:cd01379 450 TLVEKF--HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ---------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 647 ldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEG 726
Cdd:cd01379 517 ------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLET 572
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558694 727 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 790
Cdd:cd01379 573 TRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
102-788 |
3.14e-161 |
|
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: 510.49 E-value: 3.14e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 173
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 174 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKGRKDHNIPPESpkavklqngilfygeLERQLLQANPILESFGNAK 251
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNATEREN---------------VRDRVLESNPILEAFGNAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 252 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL-- 329
Cdd:cd14901 145 TNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLns 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 330 SNGNIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-KKERNTDQASMPENTAAQKLCHLLGMNV 408
Cdd:cd14901 225 SQCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDM 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 409 MEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFQL 487
Cdd:cd14901 305 DVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFAT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 488 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKA 563
Cdd:cd14901 385 NSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 564 TDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdvdr 643
Cdd:cd14901 458 NDEKLANKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 644 ivgldqvagmnetafgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGV 723
Cdd:cd14901 531 ---------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGV 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558694 724 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrIGQSKIF 788
Cdd:cd14901 584 LEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
102-752 |
1.66e-160 |
|
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: 508.85 E-value: 1.66e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------------------LVEAQVLESNPLLEAFGNARTLRNDNSSR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVT---------GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN 331
Cdd:cd14888 139 FGKFIELQFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 332 GNIP------------------------IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD 387
Cdd:cd14888 219 DAKPisidmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 388 QASMPENTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD 464
Cdd:cd14888 299 EGAVVSASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 465 RTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErp 544
Cdd:cd14888 379 YSKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ-- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 545 ANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVAT 624
Cdd:cd14888 456 EKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 625 LLHQSTDKFVAELWKD-VDRIVGLdqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHE 703
Cdd:cd14888 534 VIKNSKNPFISNLFSAyLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQ 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558694 704 KRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 752
Cdd:cd14888 599 NVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
102-790 |
2.52e-160 |
|
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: 507.80 E-value: 2.52e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAHVAsshkgrkdhNIPPESPKAVKLQNgilfygeLERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVIS---------QQSLELSLKEKTSC-------VEQAILESSPIMEAFGNAKTVYNNNSSR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQ 339
Cdd:cd14873 145 FGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKkerNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14873 225 SDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 420 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYT 498
Cdd:cd14873 302 MFLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 499 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGT 578
Cdd:cd14873 379 NEKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHAN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 579 HGKFQKPRQLKDkaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrivgldqvAGMNETAF 658
Cdd:cd14873 455 NHFYVKPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTL 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 659 GAAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRI 738
Cdd:cd14873 525 KCGSKHRR---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRR 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 688558694 739 VFQEFRQRYEILTPNAIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14873 602 PFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
102-790 |
3.20e-159 |
|
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: 505.06 E-value: 3.20e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 174
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 175 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKAVKLQNGIlfygelERQLLQANPILESFGNAKTVK 254
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKGAANAHESI------EECVLLSNLILEAFGNAKTIR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 255 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN- 333
Cdd:cd14892 149 NDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNc 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 334 IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQ----ASMPENTAAQKLCHLLGMNVM 409
Cdd:cd14892 229 VEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 410 EFTRAILSPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDI 479
Cdd:cd14892 307 ELMFKLVTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 480 AGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECW 559
Cdd:cd14892 387 FGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQML 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 560 FP-KATDKTFVDKLVQEQ-GTHGKFQKPRQLKDkaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvael 637
Cdd:cd14892 464 LKrKTTDKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 638 wkdvdrivgldqvagmnetafgaayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQ 717
Cdd:cd14892 536 -------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQ 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 718 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELDPNLYRIGQSKIFFR 790
Cdd:cd14892 578 LIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-790 |
8.92e-157 |
|
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: 497.29 E-value: 8.92e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAHVASShkgrkDHnippespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS-----DD-------------------SDLLDKIVQINPLLEAFGNASTVMNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQ 340
Cdd:cd14897 137 FGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 D-------KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTR 413
Cdd:cd14897 217 DseeleyyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFQLNS 489
Cdd:cd14897 297 ALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 490 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFV 569
Cdd:cd14897 377 FDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 570 DKLVQEQGTHGKFQKPrqLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdvdrivgldq 649
Cdd:cd14897 454 QKLNKYCGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 650 vagmnetafgaayktkkgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRI 729
Cdd:cd14897 522 ------------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKI 577
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558694 730 CRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 790
Cdd:cd14897 578 RRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
103-750 |
4.98e-144 |
|
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: 461.70 E-value: 4.98e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 168
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 169 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASshkgrkdhnipPESPKAVKLQNGILfygELERQLLQANPILES 246
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGD-----------NNLAASVSMGKSTS---GIAAKVLQTNILLES 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 247 FGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhlrsdlllegfnsy 326
Cdd:cd14900 148 FGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 327 rflsngnipipGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPENTAAQKL----- 400
Cdd:cd14900 214 -----------AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrda 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 401 -CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIG 475
Cdd:cd14900 283 aATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 476 ILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLD 555
Cdd:cd14900 363 ILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLID 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 556 EECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDplndnvatLLHQSTdkfva 635
Cdd:cd14900 440 EECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 636 elwkdVDrivgldqvagmnetafgaayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 715
Cdd:cd14900 507 -----VD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVL 555
|
650 660 670
....*....|....*....|....*....|....*
gi 688558694 716 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 750
Cdd:cd14900 556 NQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-753 |
1.66e-141 |
|
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: 456.41 E-value: 1.66e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 172
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 173 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKAV-KLQNGIlfygelERQLLQANPILESFGNAK 251
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATsKSTKSI------EQKILSCNPILEAFGNAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 252 TVKNDNSSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLE----GFNSY 326
Cdd:cd14907 155 TVRNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 327 RFLSNGNIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK-KERNTDQASMPENTAA-QKLCHLL 404
Cdd:cd14907 235 YLKKSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 405 GMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGIL 477
Cdd:cd14907 315 GIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 478 DIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WSFIDFgLDLQPCIDLIERPanPPGVLALLD 555
Cdd:cd14907 395 DIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLD 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 556 EECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVA 635
Cdd:cd14907 472 DSCKLATGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIIS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 636 ELWkdvdriVGLDQVAGMNETAFGAAYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVL 715
Cdd:cd14907 551 SIF------SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVL 620
|
650 660 670
....*....|....*....|....*....|....*...
gi 688558694 716 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 753
Cdd:cd14907 621 NQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
104-790 |
7.81e-141 |
|
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: 453.98 E-value: 7.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 179
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 180 TGESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSS 259
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS-------------------------QLEQQILQVNPLLEAFGNAQTVMNDNSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 260 RFGKFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN--GNIPIP 337
Cdd:cd14889 138 RFGKYIQLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNgaGCKREV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 338 gQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQASMPENTAAQKL---CHLLGMNVMEFTRA 414
Cdd:cd14889 217 -QYWKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 415 ILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFQLNSFEQ 492
Cdd:cd14889 294 LTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 493 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPKATDKTFVDKL 572
Cdd:cd14889 374 ACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 573 VQEQGTHGKFQKPRQLKDKadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWK-DVDRIVGLDQVA 651
Cdd:cd14889 451 NIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 652 GM---NETAFGAAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 728
Cdd:cd14889 529 KLpqaGSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIR 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558694 729 ICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 790
Cdd:cd14889 603 IRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
102-790 |
6.59e-139 |
|
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: 448.34 E-value: 6.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 174
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 175 QSILCTGESGAGKTENTKKVIQYLAHvaSSHKGRKDHNIPPESPKAVKLQNGIlfygELERQLLQANPILESFGNAKTVK 254
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTT--RAVGGKKASGQDIEQSSKKRKLSVT----SLDERLMDTNPILESFGNAKTLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 255 NDNSSRFGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN 333
Cdd:cd14891 150 NHNSSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 334 -IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK----LCHLLGMNV 408
Cdd:cd14891 230 cVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEalatAAELLGVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 409 MEFTRAILSPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFQL 487
Cdd:cd14891 310 EALEKVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFET 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 488 -NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE-----WSfidfglDLQPCIDLIErpANPPGVLALLDEECWFP 561
Cdd:cd14891 388 kNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLIA--SKPNGILPLLDNEARNP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 562 KATDKTFVDKLVQEQGTHGKFQKPRQlKDKAD-FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQStDKFvaelwkd 640
Cdd:cd14891 460 NPSDAKLNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-AKF------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 641 vdrivgLDQVAGMNEtafgaayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 720
Cdd:cd14891 531 ------SDQMQELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRC 574
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558694 721 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14891 575 SGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
102-790 |
7.29e-135 |
|
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: 436.90 E-value: 7.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIppespkavklqngilfygeleRQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL---------------------RQPEDVLPILESFGHAKTILNANASRF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI-PIPGQQ 340
Cdd:cd14896 137 GQVLRLHLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ--ASMPENTAAQKLCHLLGMNVMEFTRAILSP 418
Cdd:cd14896 216 DAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 419 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINY 497
Cdd:cd14896 296 VTETPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 498 TNEKLQQLFNHTMFILEQEEYQREGIEWSFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQG 577
Cdd:cd14896 376 ASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 578 THGKFQKPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGmneta 657
Cdd:cd14896 453 DHPSYAKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 658 fgaayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNR 737
Cdd:cd14896 526 -------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVR 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 688558694 738 IVFQEFRQRYEILTpNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14896 593 VPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
102-790 |
3.68e-134 |
|
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: 435.14 E-value: 3.68e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPpespkavklqngilfygelerQLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA---------------------KVIDVNPLLESFGNAKTTRNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL--SNGNIPIPG 338
Cdd:cd14904 137 FGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 339 QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASmpenTAAQKLCHLLGMNVMEFTR--AIL 416
Cdd:cd14904 217 LDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRI----SNGSQLSQVAKMLGLPTTRieEAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 417 SPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCI 495
Cdd:cd14904 293 CNRSVVTRnESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 496 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKL--- 572
Cdd:cd14904 373 NYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtn 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 573 VQEQGTHGKFQKPRQlkDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrivgldqvaG 652
Cdd:cd14904 449 HQTKKDNESIDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------A 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 653 MNETAFGAAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 732
Cdd:cd14904 518 PSETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRS 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 733 GFPNRIVFQEFRQRYEILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 790
Cdd:cd14904 597 GYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
102-790 |
4.49e-132 |
|
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: 430.48 E-value: 4.49e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 171
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 172 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkaVKLQNGILFYGELERQLLQANPILESFGNAK 251
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEG-------------APNEGEELGKLSIMDRVLQSNPILEAFGNAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 252 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--------HLRSDLLLEGF 323
Cdd:cd14908 148 TLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 324 NSYRFLSNGNIPIPGQ-QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPE---NTAAQK 399
Cdd:cd14908 228 NEFHYTGQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLAR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 400 LCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGIL 477
Cdd:cd14908 308 VAKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 478 DIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEE 557
Cdd:cd14908 387 DIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 558 CWFP-KATDKTFVDKLV--------QEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLM-KNMDPLNdnvatllh 627
Cdd:cd14908 464 CRLGiRGSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 628 qstdkfvaelwkdvdrivgldqvagmnetafgaayKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAG 707
Cdd:cd14908 536 -----------------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPD 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 708 KLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQACERMI 770
Cdd:cd14908 580 LVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDLVKGVLS 658
|
730 740
....*....|....*....|....
gi 688558694 771 RALELDPNL----YRIGQSKIFFR 790
Cdd:cd14908 659 PAMVSMKNIpedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
102-752 |
7.70e-132 |
|
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: 430.85 E-value: 7.70e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 171
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 172 REDQSILCTGESGAGKTENTKKVIQYLAHVasshkGRKDHNIPPESPKAVKLQngilfygeleRQLLQANPILESFGNAK 251
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSV-----GRDQSSTEQEGSDAVEIG----------KRILQTNPILESFGNAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 252 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN 331
Cdd:cd14902 146 TIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 332 ---GNIPIPGQQDKDN--FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKE-RNTDQASMPENTAAQ--KLCHL 403
Cdd:cd14902 226 ygpSFARKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 404 LGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIG 475
Cdd:cd14902 306 MGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 476 ILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLD 555
Cdd:cd14902 386 ILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 556 EECWFPKATDKTFVDKLVQEQGTHGKfqkprqlkdkadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfva 635
Cdd:cd14902 463 QECLMPKGSNQALSTKFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN---- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 636 elwkDVDRIVGLDQVAGMNETAFGAAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHL 713
Cdd:cd14902 527 ----EVVVAIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRER 602
|
650 660 670
....*....|....*....|....*....|....*....
gi 688558694 714 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 752
Cdd:cd14902 603 MVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
100-843 |
4.87e-127 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 420.98 E-value: 4.87e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 100 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 179 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkavklQNGILfygelerqllQANPILESFGNAKTVKNDNS 258
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----------QNAIM----------AANPVLEAFGNAKTIRNNNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 259 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPG 338
Cdd:PTZ00014 245 SRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 339 QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASM--PENTAA-QKLCHLLGMNVMEFTR 413
Cdd:PTZ00014 325 IDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFQLNSFEQL 493
Cdd:PTZ00014 405 ELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 494 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLV 573
Cdd:PTZ00014 484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCN 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 574 QEQGTHGKFQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagm 653
Cdd:PTZ00014 561 TNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG------- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 654 netafgaayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQG 733
Cdd:PTZ00014 633 ---------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLG 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 734 FPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFF-RTGV--LAHLEEERDLKITDIII 810
Cdd:PTZ00014 702 FSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkKDAAkeLTQIQREKLAAWEPLVS 781
|
730 740 750
....*....|....*....|....*....|...
gi 688558694 811 YFQSVCRGYLARKAFAKKqqqlsaLKVLQRNCA 843
Cdd:PTZ00014 782 VLEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-790 |
9.75e-126 |
|
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: 412.86 E-value: 9.75e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnIPPEspkavKLQngilfygelerqllQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVE-----KLN--------------AALTVLEAFGNVRTALNGNATRF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSyrflSNGNIPIPGQQD 341
Cdd:cd01386 138 SQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KD------NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAI 415
Cdd:cd01386 214 EDkqkaaaAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 416 ------------LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGfe 483
Cdd:cd01386 294 fkhhlsggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG-- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 484 iFQLN---------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERP---ANPP--- 548
Cdd:cd01386 371 -FQNPahsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdl 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 549 ------GVLALLDEECWFPKATDKTFVDKLVQEQG--THGKFQKPRQLKDKA-DFCIIHYAGR--VDYKADEWLMK-NMD 616
Cdd:cd01386 450 rdedrrGLLWLLDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKEN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 617 PLNDNVATLLHQSTDKFvaelwkdvdrivgldqvagmnetafgAAYKtKKGMFRTVgqlyKESLTKLMATLRNTNPNFVR 696
Cdd:cd01386 530 PSAQNATQLLQESQKET--------------------------AAVK-RKSPCLQI----KFQVDALIDTLRRTGLHFVH 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 697 CIIPNHEkrAGKLEPH--------------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF--- 759
Cdd:cd01386 579 CLLPQHN--AGKDERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlns 656
|
730 740 750
....*....|....*....|....*....|...
gi 688558694 760 --MDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd01386 657 evADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
103-751 |
4.01e-125 |
|
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: 411.65 E-value: 4.01e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 170
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 171 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPPEspkavklqngilfygelerQLLQANPIL 244
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS-------------------ELLSANPIL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 245 ESFGNAKTVKNDNSSRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLL 319
Cdd:cd14895 136 ESFGNARTLRNDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 320 LEGFNS--YRFLSNGNIPI--PGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-------- 387
Cdd:cd14895 216 LELLSAqeFQYISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaa 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 388 -------QASMPENTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVH 457
Cdd:cd14895 296 sapcrlaSASPSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 458 RINKALDRTK----------RQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSF 527
Cdd:cd14895 376 KVNSASPQRQfalnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 528 IDFGLDlQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlKDKAD--FCIIHYAGRVDY 605
Cdd:cd14895 456 VDYEDN-SVCLEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRY 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 606 KADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKGmfrtVGQLYKESLTKLMA 685
Cdd:cd14895 531 QAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLD 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 686 TLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 751
Cdd:cd14895 607 VVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
102-788 |
2.08e-124 |
|
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: 407.45 E-value: 2.08e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkavklQNGILfygelerqllQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----------QTAIM----------AANPVLEAFGNAKTIRNNNSSR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQ 340
Cdd:cd14876 138 FGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGID 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 341 DKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAI 415
Cdd:cd14876 218 DVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKREL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 416 LSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFQLNSFEQLC 494
Cdd:cd14876 298 TVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 495 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQ 574
Cdd:cd14876 376 INITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 575 EQGTHGKFqKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagmn 654
Cdd:cd14876 453 KLKSNGKF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG-------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 655 etafgaayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGF 734
Cdd:cd14876 524 --------KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGY 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 735 PNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 788
Cdd:cd14876 594 SYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-752 |
2.04e-117 |
|
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: 388.05 E-value: 2.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 177
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 178 LCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnipPESPKAVKLQNGIlfygelERQLLQANPILESFGNAKTVKNDN 257
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAS----------PTSWESHKIAERI------EQRILNSNPVMEAFGNACTLRNNN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 258 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIp 337
Cdd:cd14880 145 SSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 338 gqqDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTA---AQKLCHLLGMNVMEFTRA 414
Cdd:cd14880 224 ---EEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 415 ILSPRIKVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQ 492
Cdd:cd14880 301 LQIRTIRAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 493 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKL 572
Cdd:cd14880 381 LCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 573 VQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAG 652
Cdd:cd14880 458 IESALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 653 MNETAfgaayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 732
Cdd:cd14880 538 QSRAP-----------VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAA 606
|
650 660
....*....|....*....|
gi 688558694 733 GFPNRIVFQEFRQRYEILTP 752
Cdd:cd14880 607 GFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-753 |
1.37e-116 |
|
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: 387.41 E-value: 1.37e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 179
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 180 TGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklQNGilfYGELERQLLQANPILESFGNAKTVKNDNSS 259
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNN-----------NNN---NNSIEKDILTSNPILEAFGNSRTTKNHNSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 260 RFGKFIRINFDVTGYIV-GANIETYLLEKSR-AIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEG-FNSYRFL------- 329
Cdd:cd14906 147 RFGKFLKIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvi 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 330 -------SNGNIPIPGQQDKD-NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQAS--MPENTAA-Q 398
Cdd:cd14906 227 ssfksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 399 KLCHLLGMNVMEFTRAILSPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------T 466
Cdd:cd14906 307 SVSKLLGYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 467 KRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAN 546
Cdd:cd14906 387 NKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 547 ppGVLALLDEECWFPKATDKTFVDKLVQE-QGTHGKFQkpRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATL 625
Cdd:cd14906 466 --GILSLLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 626 LHQSTDKFVAELWKdvdrivgldqvagMNETAFGAAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKR 705
Cdd:cd14906 541 LLASSNFLKKSLFQ-------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMD 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 688558694 706 AGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 753
Cdd:cd14906 607 CNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
102-790 |
2.02e-112 |
|
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: 373.07 E-value: 2.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 176 SILCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnippespKAVKLQNGILfygelerqllQANPILESFGNAKTVKN 255
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST--------------SSTDVQSLIL----------GSNPLLESFGNAKTLRN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 256 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI- 334
Cdd:cd14886 137 NNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCy 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 335 PIPGQQDKDNFQETMEAMHIMsFNHEEILSMLKVVSAVLQFGNIVFKKERN--TDQASMPENTAA-QKLCHLLGMNVMEF 411
Cdd:cd14886 217 DAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 412 TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFQLN 488
Cdd:cd14886 296 AQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 489 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTF 568
Cdd:cd14886 372 TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKF 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 569 VdklvqeQGTHGKFQKPRQLKDKA---DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIV 645
Cdd:cd14886 449 T------SSCKSKIKNNSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 646 GLdqvagmnetafgaayktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 725
Cdd:cd14886 523 GN-----------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFE 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 726 GIRICRQGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14886 584 SIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-790 |
4.11e-110 |
|
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: 367.21 E-value: 4.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 178
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 179 CTGESGAGKTENTKKVIQYLAHVASSHKGRkdhniPPESPKAVKLQNgilfygelerQLLQANPILESFGNAKTVKNDNS 258
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSN-----TSQRSIADKIDE----------NLKWSNPVMESFGNARTVRNDNS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 259 SRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDL-LLEGFNSYRFLSNGNI-- 334
Cdd:cd14875 146 SRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfv 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 335 --PIPGQ--QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVME 410
Cdd:cd14875 226 rrGVDGKtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 411 FTRAILsprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFQLNS 489
Cdd:cd14875 305 LRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 490 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFV 569
Cdd:cd14875 382 FEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFT 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 570 DKLVQEQGTHGK-FQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdrivgLD 648
Cdd:cd14875 459 TNLWDQWANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LS 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 649 QVAGMNETAfgaayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 728
Cdd:cd14875 529 TEKGLARRK------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIA 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 729 ICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSKIFFR 790
Cdd:cd14875 597 LKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
102-747 |
2.30e-105 |
|
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: 355.17 E-value: 2.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 170
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 171 DREDQSILCTGESGAGKTENTKKVIQYLA---HVASSHKGRKDHNIPPESPKAVKLqngilfygelERQLLQANPILESF 247
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcGTGNNNLTNSESISPPASPSRTTI----------EEQVLQSNPILEAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 248 GNAKTVKNDNSSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-----AGEHLRSDLLLE 321
Cdd:cd14899 151 GNARTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 322 GFNSYRFLSNG--NIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-----KKERNT--DQASMP 392
Cdd:cd14899 231 GPQSFRLLNQSlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 393 ENTAA-----QKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT- 466
Cdd:cd14899 311 SSTTGafdhfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQa 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 467 -------------KRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlD 533
Cdd:cd14899 391 sapwgadesdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-N 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 534 LQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKL---VQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEW 610
Cdd:cd14899 470 NRACLELFEH--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 611 LMKNMDPLNDNVATLLHQSTDKFVAELWK-DVDRIVGLDQVAGMNETAFGAAYKTKKGMFrTVGQLYKESLTKLMATLRN 689
Cdd:cd14899 548 LAKNKDSFCESAAQLLAGSSNPLIQALAAgSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRA 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 690 TNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 747
Cdd:cd14899 627 TTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
102-790 |
3.83e-95 |
|
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: 325.45 E-value: 3.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 173
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 174 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkavklqngilfygeLERQLLQANPILESFGNAKTV 253
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG--------------------LEARLLQSGPVLEAFGNAHTV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 254 KNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFnsyrflsng 332
Cdd:cd14887 141 LNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGD--------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 333 nipiPGQQDKDNFQETMEAMHIMSFNHEEIlsmLKVVSAVLQFGNIVFKKERNTDQASMPENTA--------AQKLCHLL 404
Cdd:cd14887 212 ----PESTDLRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 405 -------GMNVMEFTRAILS--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVH 457
Cdd:cd14887 285 evkclssGLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 458 RINKALDRTKR-------------QGASFIGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQRE 521
Cdd:cd14887 365 RINAGLQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 522 G--IEWSFIDFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVDKL 572
Cdd:cd14887 445 GvfQNQDCSAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKL 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 573 VQ--EQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLhQSTDKFVaelwkdvdRIVGLDQV 650
Cdd:cd14887 525 NKniINSAKYKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKN 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 651 AGMNetafgaAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIC 730
Cdd:cd14887 596 SGVR------AISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVM 666
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 731 RQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 790
Cdd:cd14887 667 ADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
103-754 |
1.56e-94 |
|
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: 318.77 E-value: 1.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 182
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT-------------------------SIEKLITAANLILEAFGNAKTQLNDNSSRFG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDvtGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLlegfNSYRFLSNGNIPIPGQQDK 342
Cdd:cd14898 133 KRIKLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 343 DNFQETMEAMHIMSFNHEEILSMlkvvsAVLQFGNIVFKKERNTDQASmpeNTAAQKLCHLLGMNVMEFTRAILSPRIKV 422
Cdd:cd14898 207 KMTCSAMKSLGIANFKSIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 423 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFQLNSFEQLCINYTNEKL 502
Cdd:cd14898 279 KGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 503 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLvqeqgthGKF 582
Cdd:cd14898 356 QNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKY 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 583 QKPRqLKDKADFCII--HYAGRVDYKADEWLMKNMDplndnvatllhqstdkfvaelwkdvdrivgldqvaGMNETAFGA 660
Cdd:cd14898 425 LNGF-INTKARDKIKvsHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKN 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 661 AYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 740
Cdd:cd14898 469 LLINDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPK 548
|
650
....*....|....
gi 688558694 741 QEFRQRYEILTPNA 754
Cdd:cd14898 549 DRFEERYRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
99-789 |
2.59e-94 |
|
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: 320.65 E-value: 2.59e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 99 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 168
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 169 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnippeSPKAVKLQNgilfygelerQLLQANPILESFG 248
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTKLSS----------QISAAEFVLDSFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 249 NAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRF 328
Cdd:cd14879 137 NAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 329 LSNGN----IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMpENTAA-QKLC 401
Cdd:cd14879 217 LASYGchplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 402 HLLGMNVMEFtRAILSPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGI 476
Cdd:cd14879 296 AFLGVSPEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 477 LDIAGfeiFQL------NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGV 550
Cdd:cd14879 371 LDFPG---FQNrsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 551 LALLDEEC-WFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD---FCIIHYAGRVDYKADEWLMKNMDPLndnvatll 626
Cdd:cd14879 445 LGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL-------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 627 hqSTDkFVAelwkdvdrivgldqvagmnetafgaayktkkgMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPNHEKRA 706
Cdd:cd14879 517 --SPD-FVN--------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLP 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 707 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMIRALELDPNLYRIGQSK 786
Cdd:cd14879 561 NSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTK 634
|
...
gi 688558694 787 IFF 789
Cdd:cd14879 635 VFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
102-790 |
1.00e-89 |
|
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: 307.51 E-value: 1.00e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 179 CTGESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkavklqngilfyGELERQLLQANPILESFGNAKTVKNDNS 258
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSR------------------------TTFDSRFKHVNCILEAFGHAKTTLNDLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 259 SRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG----N 333
Cdd:cd14878 137 SCFIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 334 IPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTR 413
Cdd:cd14878 217 STAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFQLNSF 490
Cdd:cd14878 297 ALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 491 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIewsfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECW 559
Cdd:cd14878 377 EQLCVNMTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 560 FPKATDKTFVDKL---VQEQGTHGKFQKPRQ------LKDK-ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQS 629
Cdd:cd14878 444 MIWSVEPNLPKKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 630 TDKFVAELwkdvdrivgldqvagmnetafgaaYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKL 709
Cdd:cd14878 524 ENVVINHL------------------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTF 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 710 EPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALELDPNL--YRIGQSKI 787
Cdd:cd14878 577 DNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVLQQCKLqgWQMGVRKV 653
|
...
gi 688558694 788 FFR 790
Cdd:cd14878 654 FLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-790 |
6.86e-87 |
|
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: 298.47 E-value: 6.86e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAhvasshKGRKDHNippespkavklqngilfygELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN-------------------EISNTLWDSNFILEAFGNAKTLKNNNSSRY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14937 132 GKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFnHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENT--AAQKLCHLLGMNVMEFTRAIL 416
Cdd:cd14937 212 AKDFGNLMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 417 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFQLNSFEQLCIN 496
Cdd:cd14937 291 FTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLIN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 497 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVDKLVQEQ 576
Cdd:cd14937 370 IANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 577 GTHGKFQKPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIvglDQVAGMNET 656
Cdd:cd14937 446 SKHEKYASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVS---ESLGRKNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 657 AFGaayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIcRQGFPN 736
Cdd:cd14937 522 TFK----------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQY 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 737 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 790
Cdd:cd14937 585 KYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
102-742 |
5.22e-79 |
|
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: 276.79 E-value: 5.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 173
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 174 DQSILCTGESGAGKTENTKKVIQYLAHVasshkgrkdhnippespkavklqNGILFYGELERQLLQANPILESFGNAKTV 253
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI-----------------------QTDSQMTERIDKLIYINNILESMSNATTI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 254 KNDNSSRFGKFIRINFD---------VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-AGEHLRSDLLLEGF 323
Cdd:cd14884 138 KNNNSSRCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNC 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 324 NSYRFLSN----------GNIPIPG----------QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKe 383
Cdd:cd14884 218 GVYGLLNPdeshqkrsvkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 384 rntdqasmpentaaqkLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL 463
Cdd:cd14884 297 ----------------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 464 DRTKRQGA-----------SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGl 532
Cdd:cd14884 361 LKCKEKDEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 533 DLQPCIDLIERpanppgVLALLDE-----ECWFPKATDKTFVD-------KLVQEQGTHGK-------FQKPRQLKDKAD 593
Cdd:cd14884 440 SYSDTLIFIAK------IFRRLDDitklkNQGQKKTDDHFFRYllnnerqQQLEGKVSYGFvlnhdadGTAKKQNIKKNI 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 594 FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdvdrivgldqvagmnetafgAAYKTKKGMFRTVG 673
Cdd:cd14884 514 FFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVS 570
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 674 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 742
Cdd:cd14884 571 KKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
103-777 |
4.51e-75 |
|
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: 263.90 E-value: 4.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 176 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipPESpkavklqngilfygELERQLLQANPILESFGNAKTVKN 255
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGGG---------PET--------------DAFKHLAAAFTVLRSLGSAKTATN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 256 DNSSRFGKFIRINFdVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFN--SYRFLSNGN 333
Cdd:cd14881 127 SESSRIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 334 IPIPGQQDKDNFQETMEAMHIMSFnheEILSMLKVVSAVLQFGNIVFkKERNTDQASMPENTAAQKLCHLLGMNVMEFTR 413
Cdd:cd14881 206 TRQNEAEDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 414 AILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIF 485
Cdd:cd14881 282 GLTTRTHNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 486 QLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKAT 564
Cdd:cd14881 358 KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGT 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 565 DKTFVDKLVQEQGTHGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvaelwkdvdri 644
Cdd:cd14881 434 AESYVAKIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 645 vgldqvagmneTAFGaayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVL 724
Cdd:cd14881 499 -----------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVL 558
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 725 EGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 777
Cdd:cd14881 559 ETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
105-789 |
3.94e-71 |
|
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: 255.28 E-value: 3.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 105 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 174
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 175 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDhnipPESpkavklQNGILFygELERQLLQANPILESFGNAKTVK 254
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD----SEG------ASGVLH--PIGQQILHAFTILEAFGNAATRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 255 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgEH---LRSDLLL-EGFNSYRFLS 330
Cdd:cd14893 152 NRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 331 N-----GNIPIpgqqDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF------KKERN-------TDQASMP 392
Cdd:cd14893 231 QadplaTNFAL----DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGgansttvSDAQSCA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 393 ENTAAQKL--CHLLGMNVMEF-----TRAILSpriKVGRDYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL 463
Cdd:cd14893 307 LKDPAQILlaAKLLEVEPVVLdnyfrTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGIL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 464 ----DRTKRQG----ASFIGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWS 526
Cdd:cd14893 384 ggifDRYEKSNivinSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 527 FIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD------------F 594
Cdd:cd14893 464 NVDITSEQEKCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllF 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 595 CIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKfvaelwkdVDRIVGLDQVAGmNETAFGAAYKTKKG----MFR 670
Cdd:cd14893 542 IVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAA-ASSEKAAKQTEERGstssKFR 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 671 TVGQLYKESLT--------------KLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 736
Cdd:cd14893 613 KSASSARESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTV 692
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 737 RIVFQEFRQRYeiltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 789
Cdd:cd14893 693 HLTYGHFFRRY---------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
103-790 |
3.10e-69 |
|
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: 247.70 E-value: 3.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnippespkavklqngilfygelerqLLQANPILESFGNAKTVKNDNSSR 260
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY-------------------------ILESGIILESFGHASTDSNHNSSR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN-GNIPIPGQ 339
Cdd:cd14905 135 WGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtdQASMPENTAAQKLCHLLGMNVMEFTRAILSPR 419
Cdd:cd14905 215 DDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 420 IKVGRDYVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14905 293 SMPVNEAVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 500 EKLQQLFNHTMFILEQEEYQREGIEW-SFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVDKLVQEQGT 578
Cdd:cd14905 361 ERLQQIYLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSR 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 579 HGKF-QKPRQlkdkadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKF-------------VAELWKDVD-- 642
Cdd:cd14905 434 HHLFgKKPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDak 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 643 --------RIVGL---------DQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHE 703
Cdd:cd14905 508 ntakksplSIVKVllscgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSK 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 704 KRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRI 782
Cdd:cd14905 588 KTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQV 665
|
....*...
gi 688558694 783 GQSKIFFR 790
Cdd:cd14905 666 GNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
102-755 |
1.21e-68 |
|
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: 244.78 E-value: 1.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 180
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 181 GESGAGKTENTKKVIQYLAHvasshkgrkdhniPPESPKAVKLQNGILFygelerqllqanpILESFGNAKTVKNDNSSR 260
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS-------------QPKSKVTTKHSSAIES-------------VFKSFGCAKTLKNDEATR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 261 FGKFIRINFDvTGYIVGANIE-TYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQ 339
Cdd:cd14874 125 FGCSIDLLYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 340 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPE--NTAAQKLCHLLGMNVMEFTRAIL 416
Cdd:cd14874 204 SDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 417 SPRIKVGrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFQLNSFEQLCIN 496
Cdd:cd14874 284 LPKSEDG-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLIN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 497 YTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDF----GLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKL 572
Cdd:cd14874 357 SVNERIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHC 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 573 VQEQGTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdvdrivgldqvag 652
Cdd:cd14874 432 NLNHTDRSSYGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------------- 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 653 mNETAfgaaykTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQ 732
Cdd:cd14874 498 -SYSS------NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIK 570
|
650 660
....*....|....*....|...
gi 688558694 733 GFPNRIVFQEFRQRYEILTPNAI 755
Cdd:cd14874 571 GYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
103-750 |
2.04e-62 |
|
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: 226.93 E-value: 2.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 183 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespKAVKLQNGIlfygelerqllqanPILESFGNAKTVKNDNSSRFG 262
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRG-----------ATGRVESSI--------------KAILALVNAGTPLNADSTRCI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 263 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHLRSDLLLEGFNsYRFL--SNGNIPIPG 338
Cdd:cd14882 137 LQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEVPPSKL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 339 QQDKDN-------FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKerNTDQASMPENTAAQKLCHLLGMNVMEF 411
Cdd:cd14882 216 KYRRDDpegnverYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 412 TRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFQ 486
Cdd:cd14882 294 MWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFH 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 487 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECwfPKATDK 566
Cdd:cd14882 371 RNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 567 TFVDKLVQEQgtHGKFQKPrqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivg 646
Cdd:cd14882 446 NYIMDRIKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN------ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 647 lDQVAGMnetafgaayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLEPHLVLDQLRCNGV 723
Cdd:cd14882 515 -SQVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAV 578
|
650 660
....*....|....*....|....*..
gi 688558694 724 LEGIRICRQGFPNRIVFQEFRQRYEIL 750
Cdd:cd14882 579 LDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
103-788 |
3.01e-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: 218.94 E-value: 3.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 182 ESGAGKTENTKKVIQYLAHVASSHKgRKDHNIPPESPKAVKLQNGILFYGELERQLLQANPILESFGNAKTVKNDNSSRF 261
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSR-RLPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 262 GKFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD 341
Cdd:cd14938 161 SKFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 342 KDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNI-----VFKKE---------------------RNTDQASMPENT 395
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 396 AAQKL-CHLLGMNVMEFTRAILSPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGAS 472
Cdd:cd14938 320 KNLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 473 FIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANppGVLA 552
Cdd:cd14938 399 YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 553 LLDEECWFPKATDKT-FVDKLVQEQGTHGKF-QKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQST 630
Cdd:cd14938 477 SLLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 631 DKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFVRCIIPNHEKRA 706
Cdd:cd14938 557 NEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKRE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 707 -GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIRALELDPNLYRIGQS 785
Cdd:cd14938 637 lCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNN 708
|
...
gi 688558694 786 KIF 788
Cdd:cd14938 709 MIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
124-274 |
3.43e-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: 3.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 124 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 202
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 203 SSHKGRKDHNIPPESPKAvklqngilfYGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 274
Cdd:cd01363 81 FNGINKGETEGWVYLTEI---------TVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1094-1953 |
4.05e-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: 147.13 E-value: 4.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1094 QAQIDELkiqLAKKEEELQAVLargdEEVA-------QKNNALKQLRELQAQLA-------ELQEDLESEKAARNKAEKL 1159
Cdd:TIGR02168 143 QGKISEI---IEAKPEERRAIF----EEAAgiskykeRRKETERKLERTRENLDrledilnELERQLKSLERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1160 KrDLSEELEALKTELEdTLDTTAAQQELRSKREQEvaelkkaiddetrnheSQIQEMRQRHGTALEEISEQLEQAKRVKG 1239
Cdd:TIGR02168 216 K-ELKAELRELELALL-VLRLEELREELEELQEEL----------------KEAEEELEELTAELQELEEKLEELRLEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1240 NLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1319
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1320 KKGIKLTKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEeknnlleqqeeeeesrknlekQLATLQAQLVETKKKL 1399
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLET-------LRSKVAQLEL---------------------QIASLNNEIERLEARL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1400 EDDVGALEGLEEVKRKLQKDMEvtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQivsNLEKKQKKFDQMLAEE 1479
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAEREL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1480 KTISAR-YAEERDRAEAEAREKDTKALSMARA--------LDEALEAKEEFER-LNKQLRAEMEDLI-SSKDDVGKNVHE 1548
Cdd:TIGR02168 485 AQLQARlDSLERLQENLEGFSEGVKALLKNQSglsgilgvLSELISVDEGYEAaIEAALGGRLQAVVvENLNAAKKAIAF 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1549 LEKSK--------------RTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF---DRDLQARDEQNEEKKR 1611
Cdd:TIGR02168 565 LKQNElgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPG 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1612 ALV-----KQVREMEAELEDERKQRALAVAAK---KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1683
Cdd:TIGR02168 645 YRIvtldgDLVRPGGVITGGSAKTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1684 RTsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQleee 1763
Cdd:TIGR02168 725 SR-------QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---- 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1764 leeEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSkFKASIAALEAKIL 1843
Cdd:TIGR02168 794 ---LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIE 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1844 QLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAS-RRKL 1922
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEY 949
|
890 900 910
....*....|....*....|....*....|....*...
gi 688558694 1923 QRELDDA-------TEASEGLSREVNTLKNRLRRGGPV 1953
Cdd:TIGR02168 950 SLTLEEAealenkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
880-1711 |
1.06e-34 |
|
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: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 880 LIKVKERQVKVENELVEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARL-VAKKQELEEILHDLESRVEEEEERNQ 958
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 959 SLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEE 1038
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1039 EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG 1118
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1119 DEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEvael 1198
Cdd:TIGR02168 417 ERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQALDAAEREL---- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1199 kkaidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNK-ELTNEV---KSLQQAKSESEHKRK 1274
Cdd:TIGR02168 485 -----AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEAalgGRLQAVVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1275 K-LEAQLQEVMAR--FSEGEKVKG-ELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQE-ETRQ 1349
Cdd:TIGR02168 560 KaIAFLKQNELGRvtFLPLDSIKGtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAlELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1350 KLNLSSRIRQLEEEK-----------NNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1418
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1419 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERDRAEAEAR 1498
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE-----------------AEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1499 EKDTKALSMARALDEALEAKEEFERLNKQ---LRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ 1575
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1576 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEkKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEaa 1655
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSE-LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-- 939
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1656 nkardeaikqlRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQL 1711
Cdd:TIGR02168 940 -----------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1057-1823 |
2.05e-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: 141.73 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1057 DLEERLKKEEKTRQELEKAKRKLDAettdLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQ 1136
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1137 AQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttaaqqELRSKREQEVAELKKAiDDETRNHESQIQEM 1216
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE----------ELKEELESLEAELEEL-EAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1217 RQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLqqakseSEHKRKKLEAQLQEVMARFSEGEKVKGE 1296
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI------EELLKKLEEAELKELQAELEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1297 LADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEetrqKLNLSSRIRQLEEEKNNLLEQQEEEEE 1376
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1377 S---RKNLEKQLAT-----LQAQLVETKKKLEDDVGALEGLEEVK-----------RKLQKDMEVTSQKLEEKAIAFDKL 1437
Cdd:TIGR02168 528 LisvDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRvtflpldsikgTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1438 EKTKNRLQQELDDLmvdLDHQRqIVSNLE-----KKQKKFDQML--AEEKTISARYAEERdraeaEAREKDTKALSMARA 1510
Cdd:TIGR02168 608 VKFDPKLRKALSYL---LGGVL-VVDDLDnalelAKKLRPGYRIvtLDGDLVRPGGVITG-----GSAKTNSSILERRRE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1511 LDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQA 1590
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1591 MKAQFDRDLQARDEQNEEKKRAlvkqvremEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ 1670
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEA--------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1671 AQMKDYQRELEEARTsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK 1750
Cdd:TIGR02168 831 RRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1751 RRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSA--------AQKSENARQQLERQNKDLKSKLQE 1822
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealENKIEDDEEEARRRLKRLENKIKE 983
|
.
gi 688558694 1823 L 1823
Cdd:TIGR02168 984 L 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
996-1877 |
2.28e-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: 134.81 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 996 EAKIKKMEEDIllleDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKtrQELEKA 1075
Cdd:TIGR02169 169 DRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR----EYEGYELLKEK--EALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1076 KRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLRELQAQLAELQEDLESEKAARN 1154
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1155 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaidDETRNHESQIQEMRQRHGTALEEIS---EQL 1231
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK----EELEDLRAELEEVDKEFAETRDELKdyrEKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1232 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1311
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1312 SCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRI-------RQLEEEKNNLLEQQEEEEESRknlekq 1384
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNR------ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1385 latLQAQLVEtkkkleDDVGALEGLEEVKRK-----------LQKDMEVTSQKLEEKA--------IAFDklEKTKNRLQ 1445
Cdd:TIGR02169 549 ---LNNVVVE------DDAVAKEAIELLKRRkagratflplnKMRDERRDLSILSEDGvigfavdlVEFD--PKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1446 QELDDLMV--DLDHQRQIVSN----------LEKKQKKFDQMLAEEKTISaRYAEERDRAEAEAREKDtkalSMARALDE 1513
Cdd:TIGR02169 618 YVFGDTLVveDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1514 ALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1593
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1594 QFDrdlQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQM 1673
Cdd:TIGR02169 773 DLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1674 KDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRL 1753
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1754 EARIAQLEEELEEEQSNMELLNDrFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfka 1833
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLE--------- 999
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 688558694 1834 siaaleakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQV 1877
Cdd:TIGR02169 1000 --------------------EERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1020-1759 |
2.56e-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: 134.81 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1020 KKLLEDRVGemTSQLAEEEEKAKN-LGKVKNKQEMMMVDLEERLKKEEKTRQELEKA-------KRKLDAETTDLQDQIA 1091
Cdd:TIGR02169 156 RKIIDEIAG--VAEFDRKKEKALEeLEEVEENIERLDLIIDEKRQQLERLRREREKAeryqallKEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1092 ELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnkaekLKRDLsEELEALK 1171
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKL----TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-----VKEKI-GELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1172 TELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESD 1251
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1252 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMarfSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvss 1331
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQ---EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1332 lESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE 1411
Cdd:TIGR02169 454 -EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1412 VKRKLQKDME-----------VTSQKLEEKAIAFDKLEKTK-------NRLQQELDDL--------------MVDLDHQR 1459
Cdd:TIGR02169 533 VGERYATAIEvaagnrlnnvvVEDDAVAKEAIELLKRRKAGratflplNKMRDERRDLsilsedgvigfavdLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1460 Q-----------IVSNLEKKQKKFDQM--------LAE-----------EKTISARYAEERDRAEAEAREKDtkalSMAR 1509
Cdd:TIGR02169 613 EpafkyvfgdtlVVEDIEAARRLMGKYrmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1510 ALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ 1589
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1590 AMKAQFDrdlQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKL 1669
Cdd:TIGR02169 769 ELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1670 QAQMKDYQRELEEARTSRDEIFTQSKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1742
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810
....*....|....*..
gi 688558694 1743 KAALLDEKRRLEARIAQ 1759
Cdd:TIGR02169 926 LEALEEELSEIEDPKGE 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
848-1642 |
1.55e-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: 129.02 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 848 LRHWQWWRLftkvkpLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEE 927
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 928 MRARLVAKKQELEEILHDLESrveEEEERNQSLQNEKKKmqshiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDIL 1007
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLER---QLEELEAQLEELESK------------------LDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1008 LLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLq 1087
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1088 dQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEEL 1167
Cdd:TIGR02168 434 -ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1168 EAlKTELEDTLDTTAAQQELRSKREQEV-AELKKAIDD-ETRNHESQIQ----------------EMRQRHGTALEeiSE 1229
Cdd:TIGR02168 513 KN-QSGLSGILGVLSELISVDEGYEAAIeAALGGRLQAvVVENLNAAKKaiaflkqnelgrvtflPLDSIKGTEIQ--GN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1230 QLEQAKRVKGNLEKNKQTLESDNK---------ELTNEVKSLQQAksesEHKRKKLEAQLQEVMA---RFSEGEKVKGEL 1297
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKlrkalsyllGGVLVVDDLDNA----LELAKKLRPGYRIVTLdgdLVRPGGVITGGS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1298 ADRTHKI---QTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1374
Cdd:TIGR02168 666 AKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1375 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSqkleekaIAFDKLEKTKNRLQQELDDLMVD 1454
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK-------EELKALREALDELRAELTLLNEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1455 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1534
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1535 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ-----ATEDAKLRLEVnMQAMKAQFDRDLQARDEQNEEK 1609
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEE-AEALENKIEDDEEEARRRLKRL 977
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 688558694 1610 KRAL----------VKQVREMEAELEDERKQRALAVAAKKKLE 1642
Cdd:TIGR02168 978 ENKIkelgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
985-1759 |
3.72e-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: 124.41 E-value: 3.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 985 RQKLQLEKVTAEA----KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEE 1060
Cdd:TIGR02169 200 LERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1061 RLKKEEKTRQ-ELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG---DEEVAQKNNALKQL---- 1132
Cdd:TIGR02169 280 KIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelEREIEEERKRRDKLteey 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1133 RELQAQLAELQEDLES-EKAARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhES 1211
Cdd:TIGR02169 360 AELKEELEDLRAELEEvDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1212 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF---- 1287
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRavee 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1288 ---SEGEKVKGELAD-----RTHKIQTE------LDNVSCLLEDAEKKGIKLTKDVsslesQLQDTQELLQEETRQKLNL 1353
Cdd:TIGR02169 515 vlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNVVVEDDAVAKEAIELLKRR-----KAGRATFLPLNKMRDERRD 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1354 SSRIR------------QLEEEKNNLLEQQEEEEESRKNLEKQLATL-QAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1420
Cdd:TIGR02169 590 LSILSedgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1421 EVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAE 1496
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1497 AREKDTKALSMARaLDEALEAKEefERLNKqLRAEMEDLisSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1576
Cdd:TIGR02169 750 EQEIENVKSELKE-LEARIEELE--EDLHK-LEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1577 TEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAAN 1656
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1657 KARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKE------NEKKLKSLEAEILQLQEDLASSERARRHAEQERD 1730
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
810 820
....*....|....*....|....*....
gi 688558694 1731 ELADEISNSASGKAALLDEKRRLEARIAQ 1759
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
108-731 |
4.56e-28 |
|
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: 123.70 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 108 LKDRYYSGLIYTYSGLFCV-VINPYKNL------PIYSENIIEMYRGKKRHE--MPPHIYAISE---------------- 162
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 163 ----SAYRCMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVAS----------------------------------- 203
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQpalskgseetckvsgstrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 204 -----------SHKGRKDHNI-----PPE----------SPKAVKLQNGILFYG--------ELERQL------------ 237
Cdd:cd14894 166 rteeartiallEAKGVEKYEIvlldlHPErwdemtsvsrSKRLPQVHVDGLFFGfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 238 ----LQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------KDERTFHV 302
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 303 FYQLLAGAGEH-----LRSDLLLEGFN--SYRFLSNGNIPIPG--------QQDKDNFQETMEAMHIMSFNHEEILSMLK 367
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 368 VVSAVLQFGNIVFKKERNTDQASMPEN---TAAQKLCHLLGMNVMEFTRAIL---SPRIKVGRDYVQKAQTKEQADFAVE 441
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLmtkSVSLQSTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 442 ALAKATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQl 505
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA- 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 506 fnhtmfileqEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATD----------KTFVDKLVQE 575
Cdd:cd14894 565 ----------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 576 QGTHGKfQKPRQLKDKA----------DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRiv 645
Cdd:cd14894 635 NSSRLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ-- 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 646 gLDQVAGMNETAFGAAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 725
Cdd:cd14894 712 -LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIR 789
|
....*.
gi 688558694 726 GIRICR 731
Cdd:cd14894 790 QMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1381-1953 |
4.81e-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: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1381 LEKQLATLQAQ---------LVETKKKLEDDVGAL--EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELD 1449
Cdd:COG1196 198 LERQLEPLERQaekaeryreLKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1450 DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1529
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1530 AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfDRDLQARDEQNEEK 1609
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1610 KRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE 1689
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1690 IftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE-----LADEISNSASGKAALLDEKRRLEARIAQLEEEL 1764
Cdd:COG1196 517 A--GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1765 EEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKilq 1844
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL--- 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1845 leEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQR 1924
Cdd:COG1196 672 --AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
570 580 590
....*....|....*....|....*....|...
gi 688558694 1925 ELDDATEAS----EGLSREVNTLKNRLRRGGPV 1953
Cdd:COG1196 750 EEALEELPEppdlEELERELERLEREIEALGPV 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
865-1563 |
2.01e-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: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 865 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 944
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 945 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1024
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1025 DRVGEMTSQLAEEEEKAKNLGKVKNKQEM--------MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI---AEL 1093
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELaqlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEGY 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1094 QAQIDelkiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE----DLESEKAARNKAEKLKRDLSEELEA 1169
Cdd:TIGR02168 536 EAAIE------AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLVK 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1170 LKTELEDTL-----------DTTAAQQELRSKREQEVAELKK--------AIDDETRNHESQIQEMRQRhgtaLEEISEQ 1230
Cdd:TIGR02168 610 FDPKLRKALsyllggvlvvdDLDNALELAKKLRPGYRIVTLDgdlvrpggVITGGSAKTNSSILERRRE----IEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1231 LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDN 1310
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1311 VSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQA 1390
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1391 QLVETKKKLEDDVGALEGLEEVKRKLQKD-------MEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1463
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1464 NLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1542
Cdd:TIGR02168 926 QLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFL 1005
|
730 740
....*....|....*....|.
gi 688558694 1543 GKNVHELEKSKRTLEQQVEEM 1563
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEI 1026
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1131-1878 |
5.10e-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: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1131 QLRELQAQLAELQEDLESEKAARNKAEKlkrDLSEELEALKTELEDTLDT----TAAQQELRSKREQEVAELKKA---ID 1203
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVI---DLQTKLQEMQMERDAMADIrrreSQSQEDLRNQLQNTVHELEAAkclKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1204 DETRNHESQIQEMRQ---RHGTALEEISEQLEQAKRVKGnleknKQTLESDNKElTNEVKSLQQAKSESehkRKKLEAQL 1280
Cdd:pfam15921 163 DMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFEEASG-----KKIYEHDSMS-TMHFRSLGSAISKI---LRELDTEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1281 QEVMAR-FSEGEKVKGELADRTHKI----QTELDNVSCLLEDAEKKGIKLTKDVSSLESQ---LQDTQELLQEETRQKLn 1352
Cdd:pfam15921 234 SYLKGRiFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1353 lSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLVETKKKLEDDVgalegleevkRKLQKDMEVTSQKLEEKAI 1432
Cdd:pfam15921 313 -SMYMRQLSD------------------LESTVSQLRSELREAKRMYEDKI----------EELEKQLVLANSELTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1433 AFDKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKTISARYAEERDR-AEAEAREKDTKAL---- 1505
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEALLKAMksec 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1506 --SMARALdEALEAKEEFERLNKQLRAEMEdliSSKDDVGKNVHELEKSKRTLE---QQVEEMRTQLEELEDELQAT--E 1578
Cdd:pfam15921 443 qgQMERQM-AAIQGKNESLEKVSSLTAQLE---STKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1579 DAKLRLEVNMQAMKAQfdrdlqarDEQNEEKkralvkQVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIE-AANK 1657
Cdd:pfam15921 519 ITKLRSRVDLKLQELQ--------HLKNEGD------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQlVGQH 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1658 ARDEAIKQLRK--LQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADE 1735
Cdd:pfam15921 582 GRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNE 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1736 ISNSASGKAALLDEKRRLEARIaqleeelEEEQSNMELLNDRFRkttMQVDTLNTELAGERSAAQKSENA---------- 1805
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNF-------RNKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSMEGSdghamkvamg 731
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1806 -RQQLER---QNKDLKSKLQELEGSVK--SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1878
Cdd:pfam15921 732 mQKQITAkrgQIDALQSKIQFLEEAMTnaNKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
938-1700 |
1.59e-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: 112.47 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 938 ELEEILHDLEsRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQ--------LEKVTAEAKIKKMEEDILLL 1009
Cdd:TIGR02169 171 KKEKALEELE-EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyellKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1010 EDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1089
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1090 IAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELqedlesEKAARNKAEKLKrDLSEELEA 1169
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------DKEFAETRDELK-DYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1170 LKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLE 1249
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1250 SDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF-------SEGEKVKGELAD-----RTHKIQTE------LDNV 1311
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveevlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1312 SCLLEDAEKKGIKLTKDVS------------------------------------------------------------- 1330
Cdd:TIGR02169 553 VVEDDAVAKEAIELLKRRKagratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaa 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1331 ----------SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1400
Cdd:TIGR02169 633 rrlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1401 DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1480
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1481 TISARyaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQV 1560
Cdd:TIGR02169 793 IPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1561 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDR------DLQARDEQNEEKKRALVKQVREMEAELEdERKQRALA 1634
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqieKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEE 949
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1635 VAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEI--FTQSKENEKK 1700
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIleRIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
926-1556 |
1.59e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.87 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 926 EEMRARL--------VAKK-QELEEILHDLESRVeeeeernqsLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE 996
Cdd:COG1196 196 GELERQLeplerqaeKAERyRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 997 AKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKAK 1076
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1077 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKA 1156
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1157 EKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR 1236
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1237 VKGNLEKNKQTLESDNKELTNEVkslQQAKSESEHKRKKLEAQL---------QEVMARFSEGEKVKGELADRTHKIQTE 1307
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGL---AGAVAVLIGVEAAYEAALeaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1308 L------------DNVSCLLEDAEKKGIK-LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1374
Cdd:COG1196 577 LpldkiraraalaAALARGAIGAAVDLVAsDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1375 EESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1454
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEE-------LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1455 LDHQRQIVSNLEkkqkkFDQMLAEEKTISARYAEERDRAEAEAREKDTKAlSMAR-------ALDEALEAKEEFERLNKQ 1527
Cdd:COG1196 730 LEAEREELLEEL-----LEEEELLEEEALEELPEPPDLEELERELERLER-EIEAlgpvnllAIEEYEELEERYDFLSEQ 803
|
650 660
....*....|....*....|....*....
gi 688558694 1528 LraemEDLISSKDDVGKNVHELEKSKRTL 1556
Cdd:COG1196 804 R----EDLEEARETLEEAIEEIDRETRER 828
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
985-1574 |
2.51e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 108.23 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 985 RQKLQLEKV-TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1063
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1064 KEEKTRQELEKAKRkldaETTDLQDQIAELQAQIDELKIQLAKKEEELqavlargdEEVAQKNNALKQLRELQAQLAELQ 1143
Cdd:PRK03918 232 ELEELKEEIEELEK----ELESLEGSKRKLEEKIRELEERIEELKKEI--------EELEEKVKELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1144 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ---EVAELKKAID--DETRNHESQIQEMRQ 1218
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1219 RH-GTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE---------------SEHKRKKLeaqLQE 1282
Cdd:PRK03918 380 RLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKEL---LEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1283 VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK--KGIKLTKDVSSLESQLQ--DTQELLQ-----EETRQKLN- 1352
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKkyNLEELEKkaeeyEKLKEKLIk 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1353 LSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAI 1432
Cdd:PRK03918 537 LKGEIKSLKKE-----------LEKLEELKKKLAELEKKLDELEEELAE---LLKELEELGFESVEELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1433 AFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErdraeaEAREKDTKALSMARALD 1512
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELA 676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1513 EALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1574
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1340-1905 |
2.72e-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: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1340 QELLQEETRQKLNLSS-RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1418
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1419 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1498
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1499 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1578
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1579 DAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRAlvKQVREMEAELEDERKQRALAVAAKKKLEM---------DLKDVE 1649
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavaVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1650 AQIEAANKARDEAIKQ--LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQ 1727
Cdd:COG1196 534 AAYEAALEAALAAALQniVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1728 ERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEeqsnMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQ 1807
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE----GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1808 QLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQY 1887
Cdd:COG1196 690 EEELELEEALLAEEEEE-----------RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 688558694 1888 KEQMEKANSRMKQLKRQL 1905
Cdd:COG1196 759 PPDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1064-1936 |
5.16e-23 |
|
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: 107.46 E-value: 5.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1064 KEEKTRQELEKAKRKLDaettDLQDQIAELQAQIDELKIQLAKKEE--ELQAVL--ARGDEEVAQKNNALKQLRELQAQL 1139
Cdd:TIGR02169 171 KKEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREKAERyqALLKEKreYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1140 AELQEDLEsekaarnKAEKLKRDLSEELEALKTELEDtldttaAQQELRSKREQEVAELKKAIDD---ETRNHESQIQEM 1216
Cdd:TIGR02169 247 ASLEEELE-------KLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGEleaEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1217 RQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFsegekvkGE 1296
Cdd:TIGR02169 314 ERE----LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-------AE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1297 LADRTHKIQTELDnvsclledaekkgiKLTKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEEknnlleqqeeeee 1376
Cdd:TIGR02169 383 TRDELKDYREKLE--------------KLKREINELKRELDRLQEELQR-------LSEELADLNAA------------- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1377 srknlekqLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDdlmvDLD 1456
Cdd:TIGR02169 429 --------IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA----EAE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1457 HQRQIVSNLEKKQKKFDQMLaeEKTISARYAEERDRAEAEARekdtkalsMARALDEALEAkeefeRLNkqlraemeDLI 1536
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVGER--------YATAIEVAAGN-----RLN--------NVV 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1537 SSKDDVGKNVHELEKSK---RTLEQQVEEMRTQLEELEdelQATEDAKLRLEVNMqamkAQFDRDLQA------RDE--- 1604
Cdd:TIGR02169 554 VEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDL----VEFDPKYEPafkyvfGDTlvv 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1605 QNEEKKRALVKQVR--EMEAELEDE--------RKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMK 1674
Cdd:TIGR02169 627 EDIEAARRLMGKYRmvTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1675 DYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLE 1754
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1755 ARIAQLEEELEEEQsnMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSV------K 1828
Cdd:TIGR02169 786 ARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkK 863
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1829 SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRqLEEA 1908
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-PKGE 942
|
890 900
....*....|....*....|....*...
gi 688558694 1909 EEEATRANASRRKLQRELDDATEASEGL 1936
Cdd:TIGR02169 943 DEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
870-1630 |
1.95e-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: 105.54 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 870 EEEMQAKDEELIKVKERQVKVE-------NELVEMERKHQQLLEEKNILAEQLQAE-TELFAEAEEMRARLVAKKQELEE 941
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 942 ILHDLESRVEEEEERNQSLqNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEakIKKMEEDILLLEDQNSKFLKEKK 1021
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRL-EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1022 LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK 1101
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1102 IQLAKKEEELQavlaRGDEEVAQKNNALKQLRELQAQLAELQED-----------LESEKAARNKAEKLKRDLSEELEAL 1170
Cdd:TIGR02169 406 RELDRLQEELQ----RLSEELADLNAAIAGIEAKINELEEEKEDkaleikkqewkLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1171 KTELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE----------------EIS 1228
Cdd:TIGR02169 482 EKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1229 EQLEQAKRVKG-------------------------------------------------------NLEKNKQ------- 1246
Cdd:TIGR02169 562 EAIELLKRRKAgratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvveDIEAARRlmgkyrm 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1247 -TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1325
Cdd:TIGR02169 642 vTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1326 TKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDD--- 1402
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSrip 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1403 --VGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1480
Cdd:TIGR02169 795 eiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1481 TISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTlEQQV 1560
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSL 953
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558694 1561 EEMRTQLEELEDELQATEDaklrleVNMQAMKaQFDRDLQARDEQnEEKKRALV---KQVREMEAELEDERKQ 1630
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEP------VNMLAIQ-EYEEVLKRLDEL-KEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
826-1468 |
1.02e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 826 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRLftkvkpllQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL 904
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 905 LEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshIQDLEEQLDEEEAA 984
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 985 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1064
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1065 EEKTRQELEKAKRKLDAEttdlqdqIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE 1144
Cdd:COG1196 433 LEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1145 DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAL 1224
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1225 EEISEQLEQAKRVKGNLEKNKQTLESDNK----ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADR 1300
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARyyvlGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1301 THKIQTEldnvscLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1380
Cdd:COG1196 666 SRRELLA------ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1381 LEKQLATLQAQLVETKKKLEDDVGALEG-LEEVKRKLQK----DMEVtsqkLEEkaiaFDKLEKTKNRLQQELDDLMVDL 1455
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELEReLERLEREIEAlgpvNLLA----IEE----YEELEERYDFLSEQREDLEEAR 811
|
650
....*....|...
gi 688558694 1456 DHQRQIVSNLEKK 1468
Cdd:COG1196 812 ETLEEAIEEIDRE 824
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1213-1824 |
3.36e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1213 IQEMRQRHGTaLEEISEQLEQAKRVKGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGE 1291
Cdd:COG1196 195 LGELERQLEP-LERQAEKAERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1292 KVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQD-TQELLQEEtrqklnlsSRIRQLEEEKNNLLEQ 1370
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEElEEELAELE--------EELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1371 QEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1450
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1451 LMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalsmARALDEALEAKEEFERLNKQLRA 1530
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1531 EMEDLISSKDDVGKNVHELEKSKRtLEQQVEEMRTQLEELEDELQATEDAKLRLEVNmqamkaqfDRDLQARDEQNEEKK 1610
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1611 RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDyqRELEEARTSRDEI 1690
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE--AALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1691 FTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSN 1770
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 1771 MELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1824
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1149-1707 |
4.74e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 100.91 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1149 EKAARNKAEKLKrdlseELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID---DETRNHESQIQEMRQRHGTaLE 1225
Cdd:PRK03918 161 ENAYKNLGEVIK-----EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINeisSELPELREELEKLEKEVKE-LE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1226 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQ 1305
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1306 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEEKNNLLEQQ------------ 1371
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekel 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1372 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdmEVTSQKLEEkaiafDKLEKTKNRLQQELDDL 1451
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE-----EHRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1452 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRA- 1530
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSl 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1531 -----EMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR-TQLEELEDELQATE----------DAKLRLEVNMQAMKAQ 1594
Cdd:PRK03918 545 kkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkDAEKELEREEKELKKL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1595 FDRDLQARDEQNEEKKRA--LVKQVREMEAELEDERKQRAlaVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQ 1672
Cdd:PRK03918 625 EEELDKAFEELAETEKRLeeLRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
570 580 590
....*....|....*....|....*....|....*...
gi 688558694 1673 ---MKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAE 1707
Cdd:PRK03918 703 leeREKAKKELEKLEKALERV-EELREKVKKYKALLKE 739
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1018-1892 |
6.28e-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: 100.82 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1018 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQE--------------LEKAKRKLDAET 1083
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAkkaleyyqlkekleLEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1084 TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDL 1163
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1164 SEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHgtaLEEISEQLEQAKRVKGNLEK 1243
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKLQ---EKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1244 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQlqevMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI 1323
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL----KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1324 KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDV 1403
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1404 GALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD--------------HQRQIVSNLEKKQ 1469
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIavleidpilnlaqlDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1470 KKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHEL 1549
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1550 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERK 1629
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1630 QRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQaqmKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1709
Cdd:pfam02463 782 KTEKLKVEEEKEE-KLKAQEEELRALEEELKEEAELLEEEQ---LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1710 QLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1789
Cdd:pfam02463 858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1790 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1869
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
890 900
....*....|....*....|...
gi 688558694 1870 LKEVFMQVEDERRHADQYKEQME 1892
Cdd:pfam02463 1018 RLKEFLELFVSINKGWNKVFFYL 1040
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1018-1740 |
2.78e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.06 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1018 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQElEKAKRKLDAETTDLQDQIAELQAQI 1097
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA-EDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1098 DELKIQLAKKEEEL-QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnKAEKLKRDLSE---------EL 1167
Cdd:PTZ00121 1174 DAKKAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEakkaeeernNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1168 EALKTELEDTLDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQT 1247
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1248 LESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA--RFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1325
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1326 TKdvSSLESQLQDTQELLQEETRQKLNLSSRI---RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDd 1402
Cdd:PTZ00121 1411 KK--AAAAKKKADEAKKKAEEKKKADEAKKKAeeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE- 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1403 vgALEGLEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQI--VSNLEKKQKKFDQMLAEEk 1480
Cdd:PTZ00121 1488 --AKKKAEEAKKK--------ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEE- 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1481 tisARYAEERDRAEAEAREKDTKALSMARAlDEALEAKEEfeRLNKQLRAEMEDLISSKDDVGKnvHELEKSKRTLEQQV 1560
Cdd:PTZ00121 1557 ---LKKAEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEA--RIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1561 EEMRTQLEELEDELQatEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAlaVAAKKK 1640
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEA--EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKA 1704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1641 LEMDLKDVEA--QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE---IFTQSKENEKKLKSLEAEILQLQEDL 1715
Cdd:PTZ00121 1705 EELKKKEAEEkkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
730 740
....*....|....*....|....*
gi 688558694 1716 ASSERARRHAEQERdELADEISNSA 1740
Cdd:PTZ00121 1785 LDEEDEKRRMEVDK-KIKDIFDNFA 1808
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
891-1262 |
4.65e-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: 97.82 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 891 ENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSH 970
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 971 IQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1050
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1051 QEMMMVDLEERLKKEEKTRQELEkakrkldAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK 1130
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1131 QLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR----SKREQEVAELKKAIDDET 1206
Cdd:TIGR02168 909 KRSELRRELEELREKLA---QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKELG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1207 RNHESQIQEmrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSL 1262
Cdd:TIGR02168 986 PVNLAAIEE--------YEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1018-1602 |
7.66e-20 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 97.03 E-value: 7.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1018 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKakrkLDAETTDLQDQIAE----- 1092
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAEterer 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1093 --LQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLE----SEKAARNKAEKLKRD---- 1162
Cdd:PRK02224 275 eeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDaddl 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1163 ------LSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIddetrnhesqiqemrqrhgtalEEISEQLEQAKR 1236
Cdd:PRK02224 355 eeraeeLREEAAELESELEEA-------REAVEDRREEIEELEEEI----------------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1237 VKGNLEKNKQTLESDNKELTNEVKSlqqaksesehkrkkLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLE 1316
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAE--------------LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1317 DAEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEknnlleqqeeeeesRKNLEKQLATLQAQLVETK 1396
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEER--------------REDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1397 KKLE---DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFD-KLEKTKNRLQQ--ELDDLMVDLDHQRQIVSNLEKKQK 1470
Cdd:PRK02224 537 ERAEelrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNsKLAELKERIESleRIRTLLAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1471 KFDQMLAEEKTisaRYAEERDRAEAEAREKDtkalsmARALDEALEAKEEFERLNKQLRAEMEDLISSKDDvgknvheLE 1550
Cdd:PRK02224 617 ALAELNDERRE---RLAEKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQ 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1551 KSKRTLEQQVEEmrtqLEELEDELQATEDAKLRLEV------NMQAMKAQFDRDLQAR 1602
Cdd:PRK02224 681 AEIGAVENELEE----LEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQR 734
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
888-1476 |
2.23e-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: 95.09 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 888 VKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKM 967
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 968 QSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1043
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1044 LGKVKNKQEMMMVDLEERLKKEEKTRqELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVA 1123
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1124 QKNNALKQLRELQAQLAELQEDL-----ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL 1198
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLnqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1199 KKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA 1278
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1279 QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIR 1358
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1359 QLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE--DDVGALEGLEEVKRKLQKDMEVTSQ-------KLEE 1429
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQtqkslkkKQEE 586
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 688558694 1430 KAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1476
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1138-1757 |
2.52e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.11 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1138 QLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttaaqqelrskrEQEVAELKKAIDDetrnHESQIQEMR 1217
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIE----------------EKEEKDLHERLNG----LESELAELD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1218 qrhgTALEEISEQLEQAKRVKGN----LEKNKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKV 1293
Cdd:PRK02224 220 ----EEIERYEEQREQARETRDEadevLEEHEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1294 KGELADRTHKIQTELDNVSCLLEDaekkgikLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqee 1373
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREE-------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA--------- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1374 eeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMV 1453
Cdd:PRK02224 359 -----EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1454 DLdhqrqivSNLEKKQKKFDQMLAEEKTISAryaeerdraeaearEKDTKALSMARALDEALEAKEEferlnkqLRAEME 1533
Cdd:PRK02224 434 TL-------RTARERVEEAEALLEAGKCPEC--------------GQPVEGSPHVETIEEDRERVEE-------LEAELE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1534 DLISSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqfdrDLQARDEQNEEKKRAL 1613
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIA----------------------ERRETIEEKRERAEEL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1614 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1693
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1694 SKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKR-RLEARI 1757
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 ... |
866-1753 |
9.56e-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: 93.50 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 866 VTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlVAKKQELEEILHD 945
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 946 LESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLED 1025
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1026 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLdaettdLQDQIAELQAQiDELKIQLA 1105
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL------EKLQEKLEQLE-EELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1106 KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTtaaqQ 1185
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----Q 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1186 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR---VKGNLEKNKQTLESDNKELTNEVKSL 1262
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglkVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1263 QQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ--TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1340
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKlrLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1341 ELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1420
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1421 EVTSQKLEEKAIAfdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREK 1500
Cdd:pfam02463 697 RQLEIKKKEQREK--EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1501 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDA 1580
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1581 KLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARD 1660
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1661 EAIKQLRKLQAQMKDYQRELEEartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSA 1740
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKE---------EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 688558694 1741 SGKAALLDEKRRL 1753
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
872-1563 |
1.19e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 872 EMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVE 951
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 952 EEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEdillledqNSKFLKEKKLLEDRVGEM 1030
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEE--------KKKADEAKKAEEKKKADE 1306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1031 TSQLAEEEEKAKNLGK----VKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAettdlqdqiAELQAQIDELKIQLAK 1106
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA---------AEEKAEAAEKKKEEAK 1377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1107 KEEElqaVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRdlseeLEALKTELEDTLDTTAA 1183
Cdd:PTZ00121 1378 KKAD---AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeaKKKAEEKKK-----ADEAKKKAEEAKKADEA 1449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1184 QQELRSKREQEvaELKKAIDDETRNHESQIQEMRQRHGTAL----EEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1259
Cdd:PTZ00121 1450 KKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1260 KSLQQAKS-----ESEHKRKKLEAQLQEVMARFSEGEKVkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1334
Cdd:PTZ00121 1528 KKAEEAKKadeakKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1335 QLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLVETKKKLEDDVGALEGLEE 1411
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEelkKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1412 VKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELD--DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisARYAEE 1489
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEAEEDKKKAEE----AKKDEE 1754
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558694 1490 RDRAEAEAREKDTKALSMARALDEALeAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1563
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM 1827
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
913-1291 |
3.54e-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: 91.67 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 913 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEK 992
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 993 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEmtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQEL 1072
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1073 EKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA 1152
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1153 RNKAEKLKRDLSEELEALKTELedtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtALEEIS---- 1228
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEEL--------SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-----ALEPVNmlai 978
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558694 1229 EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKR-KKLEAQLQEVMARFSEGE 1291
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 ... |
861-1710 |
7.22e-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: 90.80 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 861 KPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL-LEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL 939
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLeLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 940 EEILHDLESRVEEEEERNQSLQN-EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1018
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEkEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1019 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1098
Cdd:pfam02463 336 EIEELE--------KELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1099 ELKIQLAKKEEELQAVLArgDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK---AEKLKRDLSEELEALKTELE 1175
Cdd:pfam02463 408 QLLLELARQLEDLLKEEK--KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdelELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1176 DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE- 1254
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQk 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1255 LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1334
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1335 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKR 1414
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1415 KLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1494
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1495 AEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1574
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1575 QATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElEDERKQRALAVAAKKKLEMDLKDVEAQIEA 1654
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE-EEPEELLLEEADEKEKEENNKEEEEERNKR 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1655 ANKARDEAIKQLRKLQAQMKdyqrELEEARTSRDEIFTQSKENEKKLKSLEAEILQ 1710
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 ... |
1303-1949 |
7.55e-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: 90.62 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1303 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1382
Cdd:pfam01576 16 KVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1383 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1462
Cdd:pfam01576 96 NEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1463 SNLEKKQKKFDQMLAEektisaryAEERDRAEAEAREkdtkalsmaraldealeakeEFERLNKQLRAEMEDLISSKDDv 1542
Cdd:pfam01576 176 KSLSKLKNKHEAMISD--------LEERLKKEEKGRQ--------------------ELEKAKRKLEGESTDLQEQIAE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1543 gknvhelekskrtLEQQVEEMRTQLEELEDELQAtedAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEA 1622
Cdd:pfam01576 227 -------------LQAQIAELRAQLAKKEEELQA---ALARLE------------EETAQKNNALKKIRELEAQISELQE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1623 ELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE-EARTSRDEIFTQSKENEKKL 1701
Cdd:pfam01576 279 DLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1702 KSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1781
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1782 TMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQElEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANK 1861
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1862 IVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVN 1941
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
....*...
gi 688558694 1942 TLKNRLRR 1949
Cdd:pfam01576 598 NLEKKQKK 605
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1450 |
4.71e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.81 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 854 WRLFTKVKPLLQVTRQEEEMQAKDEEliKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLV 933
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTE--NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 934 AKKQELEEilhdLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlEKVTAEAKIKKMEEDILLLEDQN 1013
Cdd:PRK03918 242 ELEKELES----LEGSKRKLEEKIRELEERIEELKKEIEELE---------------EKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1014 SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDaETTDLQDQIAEL 1093
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1094 QAQIDELKIQlaKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE-----LE 1168
Cdd:PRK03918 378 KKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1169 ALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDE---TRNHE--SQIQEMRQR-HGTALEEISEQLEQAKRVKGNLE 1242
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselIKLKElaEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1243 KNKQTLESDNKELtNEVKSLQQAKSESEHKRKKLEAQLQEVMAR-----FSEGEKVKG-------------ELADRTHKI 1304
Cdd:PRK03918 536 KLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEErlkelepfyneylELKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1305 QTELDNVSCL---LEDAEKKGIKLTKDVSSLESQLQDTQELLQEET-----RQKLNLSSRIRQLEEEKNNLLEQQEEEEE 1376
Cdd:PRK03918 615 EREEKELKKLeeeLDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558694 1377 SRKNLEKQLATLQaqlvETKKKLEDDVGALEGLEEVKRKLQKdmevtsQKLEEKAIAFDKLEKTKNRLQQELDD 1450
Cdd:PRK03918 695 TLEKLKEELEERE----KAKKELEKLEKALERVEELREKVKK------YKALLKERALSKVGEIASEIFEELTE 758
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
918-1756 |
2.08e-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: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 918 ETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKkmqshiQDLEEQLDEEEAARQKLQLEKVTAEA 997
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 998 KIKKMEEDILLLEDQNSKFLKEkklledrvgemtsqlaeeeekakNLGKVKNKQEMmmvdleerlkkEEKTRQELEKAKR 1077
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDA-----------------------DIETAAADQEQ-----------LPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1078 KLDAETTDLQDQIAELQAQIdelkiqlAKKEEELQAVLARGDEEVAqknnalKQLRELQAQLAELQEDLES-EKAARNKA 1156
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRR-------SKIKEQNNRDIAGIKDKLA------KIREARDRQLAVAEDDLQAlESELREQL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1157 EKLKRDLSEELEALKTELEDT---LDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQ-LE 1232
Cdd:pfam12128 429 EAGKLEFNEEEYRLKSRLGELklrLNQATATPELLLQLENFDERIERA--REEQEAANAEVERLQSELRQARKRRDQaSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1233 QAKRVKGNLEKNKQTLEsdnkeltnEVKSLQQAKSESEHKRKKLEAQLQevmarfsegEKVKGELADRTHKIQTELDNVS 1312
Cdd:pfam12128 507 ALRQASRRLEERQSALD--------ELELQLFPQAGTLLHFLRKEAPDW---------EQSIGKVISPELLHRTDLDPEV 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1313 clleDAEKKGIKLTKDVSSLESQLQDTQELLQEEtrqklnlssriRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQL 1392
Cdd:pfam12128 570 ----WDGSVGGELNLYGVKLDLKRIDVPEWAASE-----------EELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1393 VETKKKLEDDVGALEGLEEVKRKLqkdmevTSQKLEEKaiafDKLEKTKNRLQQELDDLMVDLDHQRQIvsnLEKKQKKF 1472
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRL------FDEKQSEK----DKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAW 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1473 DQMLAEEKTiSARYAEERDRAEAEAREKDTKAlsmarALDEALEAKEE-FERLNKQLRAEMEDLISSKDDVGKNVHELEK 1551
Cdd:pfam12128 702 LEEQKEQKR-EARTEKQAYWQVVEGALDAQLA-----LLKAAIAARRSgAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1552 SKRTLEQQVEemrtqleeledelqatedaklRLEVNMQAMkAQFDRDLQardEQNEEKKRALVKQVREMEAELEDERKQR 1631
Cdd:pfam12128 776 EIRTLERKIE---------------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQL 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1632 ALAVAAKKkleMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQR-----ELEEARTSRDEIFTQSKENEKKLKSLEA 1706
Cdd:pfam12128 831 ARLIADTK---LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSE 907
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1707 EILQLQEDLASSERARRHAEQER--DELADEISNSASGKAALLDEKRRLEAR 1756
Cdd:pfam12128 908 SVKKYVEHFKNVIADHSGSGLAEtwESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1059-1634 |
2.94e-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: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1059 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLA----KKEEELQAVLARGDEEVAQKNNALKQLR- 1133
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEa 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1134 --------------ELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1199
Cdd:COG4913 367 llaalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1200 KAIDDETRNHESQIQ------EMRQR------------HGTALEEISEQlEQAKRVKGNLEKNKQTLESDNKELTNEVKS 1261
Cdd:COG4913 447 DALAEALGLDEAELPfvgeliEVRPEeerwrgaiervlGGFALTLLVPP-EHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1262 LQQAKSESEHKRKKLEAQ-------LQEVMARF-------SEGE------------KVKGELADRTHKIQTELDNVSCLL 1315
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKphpfrawLEAELGRRfdyvcvdSPEElrrhpraitragQVKGNGTRHEKDDRRRIRSRYVLG 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1316 EDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeknnLLEQQEEEEESRKNLEKQLATLQAQLvet 1395
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAEL--- 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1396 kKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkFDQM 1475
Cdd:COG4913 678 -ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEER 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1476 LAE------EKTISARYAEERDRAEAEAREKDTKALSMARA-----------LDEALEAKEEFERLNKQLRAemEDLISS 1538
Cdd:COG4913 755 FAAalgdavERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadLDADLESLPEYLALLDRLEE--DGLPEY 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1539 KDDVGKNVHELEKSKRT-----LEQQVEEMRTQLEELEDELQATE---DAKLRLEVNMQ--AMKAQFDRDLQA------- 1601
Cdd:COG4913 833 EERFKELLNENSIEFVAdllskLRRAIREIKERIDPLNDSLKRIPfgpGRYLRLEARPRpdPEVREFRQELRAvtsgasl 912
|
650 660 670
....*....|....*....|....*....|...
gi 688558694 1602 RDEQNEEKKRALVKQVREMEAELEDERKQRALA 1634
Cdd:COG4913 913 FDEELSEARFAALKRLIERLRSEEEESDRRWRA 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
868-1468 |
5.12e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 868 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLE 947
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 948 SRVEEEEERNQSLQN--EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEdillledqnSKFLKEKKLLED 1025
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA---------KKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1026 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKldaETTDLQDQIAELQAQIDELKIQ-- 1103
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEev 1597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1104 --LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRdlSEELEALKTELEdtldtt 1181
Cdd:PTZ00121 1598 mkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE------ 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1182 aAQQELRSKREQEvaELKKAIDDETRNHESQIQEmrqrhgtalEEISEQLEQAKrvKGNLEKNKQTLESDNKELTNEVKS 1261
Cdd:PTZ00121 1667 -AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE---------AEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKA 1732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1262 LQQAKSESEHKRKKLEAQLQE------VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQ 1335
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1336 --------LQDTQELLQEETRQKLNLSSriRQLEEEKNNLLEQQEEEEESRKNLEKqlatlQAQLVETKKKLEDDVGALE 1407
Cdd:PTZ00121 1813 ggkegnlvINDSKEMEDSAIKEVADSKN--MQLEEADAFEKHKFNKNNENGEDGNK-----EADFNKEKDLKEDDEEEIE 1885
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1408 GLEEVKRKLQKDMEV----TSQKLEEKAIAFDKLEKTKNRLQqelddlmvDLDHQRQIVSNLEKK 1468
Cdd:PTZ00121 1886 EADEIEKIDKDDIEReipnNNMAGKNNDIIDDKLDKDEYIKR--------DAEETREEIIKISKK 1942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
871-1586 |
5.79e-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: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 871 EEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRARLVAKK---QELEEILHDLE 947
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEgvlQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 948 srveeeeernqslQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQNSKFLKEKK-----L 1022
Cdd:pfam15921 198 -------------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkielL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1023 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK-EEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELK 1101
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQL----SDLESTVSQLRSELREAK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1102 IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTT 1181
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1182 AAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISE---QLEQAK----RVKGNLEKNKQTLESDNKE 1254
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltaQLESTKemlrKVVEELTAKKMTLESSERT 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1255 LTNEVKSLQQAK-------SESEHKRKKLEAQLQEVMARFSEG----------EKVKGELADRTHKIQ---TELDNVSCL 1314
Cdd:pfam15921 498 VSDLTASLQEKEraieatnAEITKLRSRVDLKLQELQHLKNEGdhlrnvqtecEALKLQMAEKDKVIEilrQQIENMTQL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1315 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeeESRKNLEK-QLATLQAQLV 1393
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR------------VSDLELEKvKLVNAGSERL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1394 ETKKKLEDDVGALegLEEVK------RKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1467
Cdd:pfam15921 646 RAVKDIKQERDQL--LNEVKtsrnelNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1468 KQ-KKFDQMLAEEKTISARyaeerdRAEAEAREKDTKAL--SMARALDEALEAKEEFERLNKqlraEMEDLISSKDDVGK 1544
Cdd:pfam15921 721 SDgHAMKVAMGMQKQITAK------RGQIDALQSKIQFLeeAMTNANKEKHFLKEEKNKLSQ----ELSTVATEKNKMAG 790
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 688558694 1545 NVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLEV 1586
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
847-1545 |
7.05e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 847 KLRHWQWWRLFTKVKPLLQVTRQ---EEEMQAKDEELIKVKERQVKVENELVEMERKhqqlLEEKNILAEQLQAETELFA 923
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 924 EAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQ-NEKKKMQSHIQDLEEQLDEEEAARQ-----KLQLEKVTAEA 997
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKKKEEAKKKADAAKKKaeekkKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 998 KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvKNKQEMMMVDLEERLKKEEKTRQELEKAKR 1077
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1078 KLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAE 1157
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1158 KLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAlEEISEQLEQAKRV 1237
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKV 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1238 ----KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRthkiqteldnvsc 1313
Cdd:PTZ00121 1636 eqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKK------------- 1696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1314 llEDAEKKGIKLTKdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnLLEQQEEEEESRKNLEKQLATLQAQLV 1393
Cdd:PTZ00121 1697 --EAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK--KKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1394 ETKKKLEDDVgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ-KKF 1472
Cdd:PTZ00121 1771 EEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEaDAF 1849
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558694 1473 DQMLAEEKTISaryAEERDRAEAEAREKDTKalsmaRALDEALEAKEEFERLNKQlraEMEDLISSKDDVGKN 1545
Cdd:PTZ00121 1850 EKHKFNKNNEN---GEDGNKEADFNKEKDLK-----EDDEEEIEEADEIEKIDKD---DIEREIPNNNMAGKN 1911
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
869-1708 |
8.56e-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: 83.94 E-value: 8.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 869 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNIlAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLES 948
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 949 RVEEEEERNQSLQ----------NEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1018
Cdd:TIGR00606 277 RKKQMEKDNSELElkmekvfqgtDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1019 E-------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIA 1091
Cdd:TIGR00606 357 DrhqehirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1092 ELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAEL--------------------QEDLESEKA 1151
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskaeknsltetlkkevkslqNEKADLDRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1152 ARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL---------KKAIDDETRNHESQIQEMRQRHGT 1222
Cdd:TIGR00606 517 LRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1223 ALEEIsEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE---------AQLQEVMARFSEGEKV 1293
Cdd:TIGR00606 596 LNKEL-ASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEksskqramlAGATAVYSQFITQLTD 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1294 KGE----LADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLL 1368
Cdd:TIGR00606 675 ENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEkRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1369 EQQEEEEESRKNL---EKQLATLQAQLvETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLE--EKAIAFDKLEKTKNR 1443
Cdd:TIGR00606 755 KVNRDIQRLKNDIeeqETLLGTIMPEE-ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQE 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1444 LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEA---EAREKDTKALSMARALDEALEAKEE 1520
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQDSP 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1521 FERLNKQLRAEMEDLISSKDDVGKNVH-ELEKSKRTLEQQVEEMRTQLEELEDelqATEDAKLRLEVNMQAMKAQFdrdl 1599
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL---- 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1600 qardEQNEEKKRALVKQVREMEAELEDERKQRALAV--AAKKKLEMDLKDVEAQIeaanKARDEAIKQLRKLQaQMKDYQ 1677
Cdd:TIGR00606 987 ----EECEKHQEKINEDMRLMRQDIDTQKIQERWLQdnLTLRKRENELKEVEEEL----KQHLKEMGQMQVLQ-MKQEHQ 1057
|
890 900 910
....*....|....*....|....*....|....
gi 688558694 1678 RELEEARTSRDE---IFTQSKENEKKLKSLEAEI 1708
Cdd:TIGR00606 1058 KLEENIDLIKRNhvlALGRQKGYEKEIKHFKKEL 1091
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1225-1944 |
8.63e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1225 EEISEQLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmARFSEGEKVKGELADRT 1301
Cdd:PTZ00121 1053 DGNHEGKAEAKAHVGQDEGLKPSYkdfDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1302 HKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNL 1381
Cdd:PTZ00121 1131 EEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1382 EKQLATLQAQLVETKKKLEddvgALEGLEEVKRKlqkdmevtsqklEEKAiafDKLEKTKNRLQ-QELDDLMVDLDHQRQ 1460
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAE----AVKKAEEAKKD------------AEEA---KKAEEERNNEEiRKFEEARMAHFARRQ 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1461 IVSNLEKKQKKFDQMLAEE--KTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISS 1538
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEkkKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1539 KDDVGKNVHELEKSKR---TLEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKaQFDRDLQARDEQNEEKKRA 1612
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEkaeAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKA 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1613 L-VKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIF 1691
Cdd:PTZ00121 1428 EeKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1692 TQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE---LADEISNSASGKAAllDEKRRLEARIAQLEEELEEEQ 1768
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekkKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1769 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLE--RQNKDLKSKLQEL----EGSVKSKFKASIAALEAKI 1842
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLkkkeAEEKKKAEELKKAEEENKI 1661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1843 LQLEEQLEQEAKERAAAN-KIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeAEEEATRANASRRK 1921
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKE 1738
|
730 740
....*....|....*....|....*
gi 688558694 1922 LQRELDDATEA--SEGLSREVNTLK 1944
Cdd:PTZ00121 1739 AEEDKKKAEEAkkDEEEKKKIAHLK 1763
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1310-1829 |
1.48e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1310 NVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQeetrqklNLSSRIRQLEEEKNNLLEQQEEEEEsrknLEKQLATLQ 1389
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELE-------KLEKEVKELEELKEEIEELEKELES----LEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1390 AQLVETKKKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ 1469
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1470 KKFDQMLAEEKTISARYAEERDRAEAeaREKDTKALSMARALdealeaKEEFERLNKQLRAEmedlisSKDDVGKNVHEL 1549
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAK------KEELERLKKRLTGL------TPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1550 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFDRDLQARDEQNEEKKRALvkqvREMEAELEDERK 1629
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL----EEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1630 QRALAVAAKKKLEMDLKDVEAQIEAANKAR--DEAIKQLRKLQAQMKDYQRE-LEEARTSRDEIFTQSKENEKKLKSLEA 1706
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1707 EILQLQE---DLASSERARRHAEQERDELADEISNSASGKAALLDEK---------------------RRLEARIAQLEE 1762
Cdd:PRK03918 547 ELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaekelEREEKELKKLEE 626
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1763 ELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSaaQKSENARQQLERQNKDLKSKLQELEGSVKS 1829
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
884-1712 |
2.08e-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: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 884 KERQVKVENELVEMERKHQQLLEEKNILAEQlqaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNE 963
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEK---------QKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 964 KKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDilLLEDQNSKFLKEKKLL---EDRVGEMTSQLAEEEEK 1040
Cdd:pfam15921 144 RNQLQNTVH----------------ELEAA------KCLKED--MLEDSNTQIEQLRKMMlshEGVLQEIRSILVDFEEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1041 AKNlgKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI-DELKIQLAKKEEELQAVLARGD 1119
Cdd:pfam15921 200 SGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1120 EEVA----QKNNALKQLRELQAQLAELQEDlesekaARNKAEKLKRDLSE----------ELEALKTELEDTLDTTAAQQ 1185
Cdd:pfam15921 278 VEITglteKASSARSQANSIQSQLEIIQEQ------ARNQNSMYMRQLSDlestvsqlrsELREAKRMYEDKIEELEKQL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1186 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQA 1265
Cdd:pfam15921 352 VLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1266 KSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL---TKDVSSLESQLQDTQEL 1342
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLessERTVSDLTASLQEKERA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1343 LQEETRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEV 1422
Cdd:pfam15921 512 IEATNAEITKLRSRV----DLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI---LRQQIENMTQLVGQHGRT 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1423 TSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfDQMLAEEKTISAryAEERDRAEAEAREKDT 1502
Cdd:pfam15921 585 AGAMQVEKA----QLEKEINDRRLELQEFKILKDKKDAKIRELEARVS--DLELEKVKLVNA--GSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1503 KALSMARALDEALEA-KEEFERLNKQLRAEMEdlisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1581
Cdd:pfam15921 657 QLLNEVKTSRNELNSlSEDYEVLKRNFRNKSE--------------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1582 ---LRLEVNMQ----AMKAQFDrdlqardeqneekkrALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQiea 1654
Cdd:pfam15921 723 ghaMKVAMGMQkqitAKRGQID---------------ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE--- 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1655 ankaRDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQ 1712
Cdd:pfam15921 785 ----KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1382-1949 |
4.14e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1382 EKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafdklEKtknrlQQELDDLMVDLDHQRQI 1461
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------ER-----REELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1462 VSNLEKKQKKFDQMLAEEKTISARYAEERD--RAEAEAREKDTKALSMARaldEALEAKEEferlnkQLRAEMEDLISSK 1539
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARR---EELEDRDE------ELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1540 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdRDLQARDEQNEEKKRALVKQVRE 1619
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV---------------EDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1620 MEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAikqlRKLQAQMK--DYQRELEEArtsrdEIFTQSKEN 1697
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA----EALLEAGKcpECGQPVEGS-----PHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1698 EKKLKSLEAEILQLQEDLASSErarrhaeqERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDR 1777
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1778 frkttmqVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfkASIAALEAKILqleeqleqeakerA 1857
Cdd:PRK02224 546 -------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIA-------------D 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1858 AANKIVRRTEKKlkEVFMQVEDERRhadqykEQMEKANSRMKQLKRQ-----LEEAEEEATRANASRRKLQRELDDATEA 1932
Cdd:PRK02224 604 AEDEIERLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
570
....*....|....*..
gi 688558694 1933 SEGLSREVNTLKNRLRR 1949
Cdd:PRK02224 676 RDDLQAEIGAVENELEE 692
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1267-1948 |
4.84e-15 |
|
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: 81.65 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1267 SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV----SCLLEDAEKKGIKLTKDVSSLESQLQDTQEL 1342
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1343 LQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNL-EKQLATLQAQLVETKKKLEddvgALEGLEEVKRKLQKDME 1421
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIA----SLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1422 VTSQKLEEKaiaFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKD 1501
Cdd:TIGR02169 322 ERLAKLEAE---IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1502 TKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1581
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1582 LRLEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMEAELE------------DERKQRALAVAAKKKLEMDLKDVE 1649
Cdd:TIGR02169 479 DRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNNVVVEDD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1650 AQIEaankardEAIKQLRKLQA---------QMKDYQRELEEARTS------------------------RDEIFTQSKE 1696
Cdd:TIGR02169 558 AVAK-------EAIELLKRRKAgratflplnKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfGDTLVVEDIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1697 NEKKLK------SLEAEILQLQEDLASSERARRHAE-------QERDELADEISNSASGKAALLDEKRRLEARIAQLEEE 1763
Cdd:TIGR02169 631 AARRLMgkyrmvTLEGELFEKSGAMTGGSRAPRGGIlfsrsepAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1764 LEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEA--- 1840
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEArls 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1841 --KILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAS 1918
Cdd:TIGR02169 790 hsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750
....*....|....*....|....*....|
gi 688558694 1919 RRKLQRELDDATEASEGLSREVNTLKNRLR 1948
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1144-1874 |
6.84e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.34 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1144 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQrhgta 1223
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----- 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1224 lEEISEQLEQAKRVkgnlEKNKQTLESDNKEltnEVKSLQQAKSESEHKRKKLEAQLQEVmaRFSEGEKvKGELADRTHK 1303
Cdd:PTZ00121 1166 -AEEARKAEDAKKA----EAARKAEEVRKAE---ELRKAEDARKAEAARKAEEERKAEEA--RKAEDAK-KAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1304 IQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEK 1383
Cdd:PTZ00121 1235 AKKDAEEAK--KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1384 QlATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQElddlmvdldhqrQIVS 1463
Cdd:PTZ00121 1310 K-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA---DEAEAAEEKAEAA------------EKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1464 NLEKKQKKFDQMLAEEKtisaRYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVG 1543
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEK----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1544 KNVHELEKSKRTLEQQVEEMRT--QLEELEDELQATEDAKLRLEVNMQamKAQFDRDLQARDEQNEEKKRALVKQVREME 1621
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1622 AELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1701
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1702 KSLEA----EILQLQEDLASSERARRHAEQERDELADEISNS---------ASGKAALLDEKRRLEARIAQLEEELEEEQ 1768
Cdd:PTZ00121 1608 KAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1769 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQ---KSENAR----QQLERQNKDLKSKLQEL--EGSVKSKFKASIAALE 1839
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENkikaEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEE 1767
|
730 740 750
....*....|....*....|....*....|....*..
gi 688558694 1840 AKILQLEEQLEQEAKERAAANKIVRR--TEKKLKEVF 1874
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRmeVDKKIKDIF 1804
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1133-1842 |
1.38e-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: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1133 RELQAQLAELQEDLESEKAARNKAEKLKR--DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaiDDETRNHE 1210
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR---LELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1211 SQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE-LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1289
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1290 GEKvkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlle 1369
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL--------- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1370 qqeeeeesRKNLEKQLATLQAQ------LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNR 1443
Cdd:COG4913 446 --------RDALAEALGLDEAElpfvgeLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1444 LQqelddlmVDLDHqrqivsnLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFE 1522
Cdd:COG4913 512 GR-------LVYER-------VRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1523 RLNKQLRAEmeDLISSkddvGKNVHELEKSKRTLEQQV--EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQ 1600
Cdd:COG4913 572 RHPRAITRA--GQVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEA--------LE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1601 ARDEQNEEKKRALVKQVREMEAELEDERKQRALAvaakkklemdlkDVEAQIEAANKARDEaikqLRKLQAQMKDYQREL 1680
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEIDVASAEREIA------------ELEAELERLDASSDD----LAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1681 EEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQL 1760
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1761 EEELEEEQSNMELLNDRFRKT-TMQVDTLNTELAGERSAAQKsenaRQQLERQnkDLKSKLQELEGSVKSKFKASIAALE 1839
Cdd:COG4913 779 RARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEED--GLPEYEERFKELLNENSIEFVADLL 852
|
...
gi 688558694 1840 AKI 1842
Cdd:COG4913 853 SKL 855
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
878-1553 |
1.71e-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: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 878 EELIKVKERQVKVENELVEMERKHQqllEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHD----------LE 947
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 948 SRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIK-KMEEDILLLEDQNSKFLKEKKLLEDR 1026
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1027 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTD----LQDQIAELQAQIDELKI 1102
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1103 ------QLAKKEE----ELQAVLARGDEEVAQKNNALKQLREL-----------QAQLAELQEDLESEKAARNKAEKLKR 1161
Cdd:pfam05483 322 atkticQLTEEKEaqmeELNKAKAAHSFVVTEFEATTCSLEELlrteqqrleknEDQLKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1162 DLSEELEALKT---ELEDTLDTTAAQQELRSK---REQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISEQLE 1232
Cdd:pfam05483 402 NKEVELEELKKilaEDEKLLDEKKQFEKIAEElkgKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1233 QAKRVKGNLEKNKQTLESDNKELTNE----VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1308
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1309 DNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1388
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKL 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1389 QAQLVETKKKLEDDVGALEGLEEVKRklqkdmeVTSQKLEEKAIAFDKLEKTKNRLQQELDdlmVDLDHQ-RQIVSNLEK 1467
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDKK-------ISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKiAEMVALMEK 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1468 KQKKFDQMLaeektisaryaEERDRAEAEAREKDTKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNV 1546
Cdd:pfam05483 712 HKHQYDKII-----------EERDSELGLYKNKEQEQSSAKAALEIELSnIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
....*..
gi 688558694 1547 HELEKSK 1553
Cdd:pfam05483 781 AILKDKK 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
863-1448 |
2.19e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 863 LLQVTRQEEEMQAKDeelikVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLvakkQELEEI 942
Cdd:PRK02224 189 LDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 943 LHDLESRVEEEEERNQSLQNEkkkmqshIQDLEeqldeeeAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1022
Cdd:PRK02224 260 IEDLRETIAETEREREELAEE-------VRDLR-------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1023 LEDRVGEMTSQLAEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1102
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDAD-------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1103 QLAKKEEELQAVLARGDEEVAQKNnalkqlrELQAQLAELQEDLESEKAARNKAEKLKR-----------------DLSE 1165
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERD-------ELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsphvETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1166 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID--DETRNHESQIQEMRQRHGTALEEISEQLEQakrvkgnLEK 1243
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEE-------LRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1244 NKQTLEsdnkeltnevkslqqakSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTeLDNVSCLLEDAEKKGi 1323
Cdd:PRK02224 545 RAAELE-----------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1324 kltKDVSSLESQLQDTQElLQEETRQKL-NLSSRIRQLEEEknNLLEQQEEEEESRKNLEKQLATLQ---AQLVETKKKL 1399
Cdd:PRK02224 606 ---DEIERLREKREALAE-LNDERRERLaEKRERKRELEAE--FDEARIEEAREDKERAEEYLEQVEeklDELREERDDL 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 688558694 1400 EDDVGALEG----LEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQQEL 1448
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 ... |
863-1611 |
4.87e-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: 78.09 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 863 LLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQqlleeknilaEQLQAETELFAEAEEMRARLVAKKQELEEI 942
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE----------KELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 943 LHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1022
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1023 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1102
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1103 QLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA 1182
Cdd:pfam02463 518 DGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1183 AQQELRSKREQEVAELKKAIDDETRNHES---QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1259
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEgilKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1260 KSLQQAKSESE----HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQ 1335
Cdd:pfam02463 678 IQELQEKAESElakeEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1336 LQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLvETKKKLEDDVGALEGLEEVKRK 1415
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA-ELLEEEQLLIEQEEKIKEEELE 836
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1416 LQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEA 1495
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEELLQELL-----LKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1496 EAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQ 1575
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-------EEEERNKRLLLAKEELGKVNLMAIEEFE 984
|
730 740 750
....*....|....*....|....*....|....*.
gi 688558694 1576 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKR 1611
Cdd:pfam02463 985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
826-1478 |
5.61e-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: 78.09 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 826 AKKQQQLSALKVLqRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELiKVKERQVKVENELVEMERKHQQLL 905
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-RAQEAVLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 906 EEKNILAEQLQaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAAR 985
Cdd:TIGR00618 297 AHIKAVTQIEQ-------QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 986 QKLQleKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKE 1065
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1066 EKTRQ-------ELEKAKRKLDAETTDLQDQ-----------------IAELQAQIDELKIQLAKKEEELQAV------- 1114
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKeqihlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1115 --LARGDEEVAQKNNALK----QLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR 1188
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1189 SK-----REQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQL------EQAKRVKGNLEKNKQTLESDNKELTN 1257
Cdd:TIGR00618 608 DMlaceqHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrEHALSIRVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1258 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvSSLESQLQ 1337
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA-RTEAHFNN 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1338 DTQELLQEETRQKL-----NLSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLvetKKKLEDDVGALEGLEEv 1412
Cdd:TIGR00618 767 NEEVTAALQTGAELshlaaEIQFFNRLREE------------------DTHLLKTLEAEI---GQEIPSDEDILNLQCE- 824
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1413 krKLQKDMEVTSQKLEEkaiafdklektKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1478
Cdd:TIGR00618 825 --TLVQEEEQFLSRLEE-----------KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1225-1893 |
6.42e-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: 77.37 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1225 EEISEQLEQAKRVKGNLEKNKQ---TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegEKVKGELADRT 1301
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDkinKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKEN-------KKNIDKFLTEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1302 HKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLS---SRIRQLEEEKNNLLEQQEEEEESR 1378
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1379 KNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL--MVDLD 1456
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1457 HQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEME 1533
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1534 DLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQatedaKLRLEVNmqamkaqfdrDLQARDEQNEEKKRAL 1613
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE-----RLKETII----------KNNSEIKDLTNQDSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1614 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1693
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1694 SKENEKKLKSLEAEILQLQEDLASSErarrhAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1773
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKEN-----LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1774 -------LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkSKFKASIAALE--AKILQ 1844
Cdd:TIGR04523 608 kekkissLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII----KKIKESKTKIDdiIELMK 683
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 688558694 1845 LEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEK 1893
Cdd:TIGR04523 684 DWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELEN 732
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
900-1649 |
9.55e-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: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 900 KHQQLLEEKNILAEQLQAETELfaeAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQshiqdleeqld 979
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLC---TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 980 eeeaARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFlkekklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLE 1059
Cdd:TIGR00618 254 ----EQLKKQQLLKQLRARIEELRAQEAVLEETQERI------------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1060 ERLKKEEKTRQELEKAKrKLDAETTDLQDQIAELQAQIDELKIQ-----LAKKEEELQAVLARGDEEVAQKNNALKQLRE 1134
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQEIHIRDAhevatSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1135 LQAQLAELQEDLESEKAARNKAEklkRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQ 1214
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1215 EMRQrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1294
Cdd:TIGR00618 474 QLQT-----KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1295 GELADRTHKIQTELDNVSCLLEDAEKKGIK---LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQ 1371
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCdnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1372 EEEEESRkNLEKQLATLQAQLVETKKKLEDdvgaleglEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1451
Cdd:TIGR00618 629 DVRLHLQ-QCSQELALKLTALHALQLTLTQ--------ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1452 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAE 1531
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1532 MEDLISskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLqardeqneEKKR 1611
Cdd:TIGR00618 780 LSHLAA----------EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKS 841
|
730 740 750
....*....|....*....|....*....|....*...
gi 688558694 1612 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVE 1649
Cdd:TIGR00618 842 ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1396-1759 |
3.07e-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: 75.49 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1396 KKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqivsnlekkqkkfdqm 1475
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----------------------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1476 laeektisaRYAEERDRAEaearekDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1555
Cdd:TIGR02169 212 ---------RYQALLKEKR------EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1556 LEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1627
Cdd:TIGR02169 277 LNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1628 RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN-------EKK 1700
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlNAA 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1701 LKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQ 1759
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1082-1741 |
5.75e-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: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1082 ETTDLQDQIAELQAQIDELkiqlakkeEELQAVLargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK-----A 1156
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1157 EKLKRDLSEELEALKTELEDTldttaaqqelrskrEQEVAELKKAIdDETRNHESQIQEMRQRHGTaleeisEQLEQAKR 1236
Cdd:COG4913 287 QRRLELLEAELEELRAELARL--------------EAELERLEARL-DALREELDELEAQIRGNGG------DRLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1237 vkgnleknkqtlesdnkeltnEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvkgELADRTHKIQTELDNVSCLLE 1316
Cdd:COG4913 346 ---------------------EIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1317 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlleqqeeeeesRKNLEKQLATLQAQ----- 1391
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-----------------RDALAEALGLDEAElpfvg 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1392 -LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNRLQqelddlmVDLDHqrqivsnLEKKQK 1470
Cdd:COG4913 465 eLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLRGR-------LVYER-------VRTGLP 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1471 KFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFERLNKQLRAemEDLISSKDDVG-KNVHE 1548
Cdd:COG4913 525 DPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELRRHPRAITR--AGQVKGNGTRHeKDDRR 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1549 LEKSKRTL----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdLQARDEQNEEKKRalVKQVREMEAEL 1624
Cdd:COG4913 597 RIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDEID--VASAEREIAEL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1625 EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftQSKENEKKLKSL 1704
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALL 751
|
650 660 670
....*....|....*....|....*....|....*..
gi 688558694 1705 EAEILQLQEDlASSERARRHAEQERDELADEISNSAS 1741
Cdd:COG4913 752 EERFAAALGD-AVERELRENLEERIDALRARLNRAEE 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1224-1878 |
1.24e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.13 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1224 LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA---RFSEGEKVKGELadr 1300
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSdlsKINSEIKNDKEQ--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1301 THKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1380
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1381 LEKQLATLQAqLVETKKKLEDDvgaLEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDlmvdldhQRQ 1460
Cdd:TIGR04523 199 LELLLSNLKK-KIQKNKSLESQ---ISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDE-------QNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1461 IVSNLEKKQKKFDQmlAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRaEMEDLISSKD 1540
Cdd:TIGR04523 265 IKKQLSEKQKELEQ--NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS-QNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1541 DVgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREM 1620
Cdd:TIGR04523 342 EQ---ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1621 EAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKK 1700
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1701 LKSLEAEILQLqedlasserarrhaEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEeleeeqsnmELLNDRFRK 1780
Cdd:TIGR04523 498 LKKLNEEKKEL--------------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED---------ELNKDDFEL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1781 TTmqvDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAAN 1860
Cdd:TIGR04523 555 KK---ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
650
....*....|....*...
gi 688558694 1861 KIVRRTEKKLKEVFMQVE 1878
Cdd:TIGR04523 631 SIIKNIKSKKNKLKQEVK 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1381-1928 |
2.01e-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: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1381 LEKQLATLQaQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIafDKLEKTKNRLQQELDDLMVDLDHQRQ 1460
Cdd:COG4913 247 AREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1461 IVSNLEKkqkkfdQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLI 1536
Cdd:COG4913 324 ELDELEA------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1537 SSKDDVGKNVHELEKSKRTLEQQveemrtqLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQneekkralVK- 1615
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE--------LPf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1616 -----QVREMEAE-----------------LEDERKQRALAVAAKKKLEMDL-------KDVEAQIEAA----------- 1655
Cdd:COG4913 463 vgeliEVRPEEERwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRLvyervrtGLPDPERPRLdpdslagkldf 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1656 --NKARDEAIKQLRKL--------QAQMKDYQREL---------EEARTSRDEIFTQSK-----ENEKKLKSLEAEILQL 1711
Cdd:COG4913 543 kpHPFRAWLEAELGRRfdyvcvdsPEELRRHPRAItragqvkgnGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1712 QEDLASSERARRHAEQERDELAD---------EISNSASGKAALLDEKRRLEARIAQleeeleeeqsnMELLNDRFRKTT 1782
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELER-----------LDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1783 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKI 1862
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-----------DRLEAAEDLARLELRALLEERFAAALG 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1863 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKAnsrMKQLKRQLEEAEEEATRANASRRKLQRELDD 1928
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDR 823
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1033-1759 |
2.02e-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: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1033 QLAEEEEK----AKNLGKVKNKQEMMMVDLE---ERL----------KKEEKTRQELEKAKRKLDAET---TDLQDQIAE 1092
Cdd:COG3096 300 QLAEEQYRlvemARELEELSARESDLEQDYQaasDHLnlvqtalrqqEKIERYQEDLEELTERLEEQEevvEEAAEQLAE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1093 LQAQ-------IDELKIQLAKKEEEL-----------QAVLARGDEEVAQKNNAL--KQLRELQAQL-AELQEDLESEKA 1151
Cdd:COG3096 380 AEARleaaeeeVDSLKSQLADYQQALdvqqtraiqyqQAVQALEKARALCGLPDLtpENAEDYLAAFrAKEQQATEEVLE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1152 ARNK---AEKLKRDLSEELEALK-----TELEDTLDTtaAQQELRSKREQE-----VAELKKAIDDETRNHESQIQEMRQ 1218
Cdd:COG3096 460 LEQKlsvADAARRQFEKAYELVCkiageVERSQAWQT--ARELLRRYRSQQalaqrLQQLRAQLAELEQRLRQQQNAERL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1219 rhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfsegEKVKGELA 1298
Cdd:COG3096 538 -----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR----APAWLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1299 DRTHKIQTEldnVSCLLEDAekkgikltkdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR 1378
Cdd:COG3096 609 DALERLREQ---SGEALADS-----------QEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRL 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1379 KNLEKQL-ATLQAQLVEtKKKLEDD--VGALEG----------LEEVKRKLQkDMEVTSQKL---EEKAIAFDKlektKN 1442
Cdd:COG3096 675 LALAERLgGVLLSEIYD-DVTLEDApyFSALYGparhaivvpdLSAVKEQLA-GLEDCPEDLyliEGDPDSFDD----SV 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1443 RLQQELDDLMVDLDHQRQI-VSNLEK--------KQKKFDQMLAEEKTISARYAEER------DRAEAEAREKDTKALSM 1507
Cdd:COG3096 749 FDAEELEDAVVVKLSDRQWrYSRFPEvplfgraaREKRLEELRAERDELAEQYAKASfdvqklQRLHQAFSQFVGGHLAV 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1508 ARALDEALEAKE------EFERLNKQLRAEMEDLISSKDDVGKNVHELEK--------SKRTLEQQVEEMRTQLEELED- 1572
Cdd:COG3096 829 AFAPDPEAELAAlrqrrsELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllADETLADRLEELREELDAAQEa 908
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1573 --ELQATEDAKLRLEVNMQAMK---AQFDRdLQARDEQNEEKKRALVKQVREMEaeledERKQRALAVAAKKKLEM---- 1643
Cdd:COG3096 909 qaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----EVVQRRPHFSYEDAVGLlgen 982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1644 -DLKD-VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEaeilqLQEDLASSERA 1721
Cdd:COG3096 983 sDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG-----VQADAEAEERA 1057
|
810 820 830
....*....|....*....|....*....|....*...
gi 688558694 1722 RrhaeQERDELADEISNSASGKAALLDEKRRLEARIAQ 1759
Cdd:COG3096 1058 R----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1088-1735 |
2.48e-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: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1088 DQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLS--- 1164
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlr 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1165 ---EELEALKTELEDT-------------LDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEIS 1228
Cdd:TIGR00618 267 ariEELRAQEAVLEETqerinrarkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1229 EQLEQAKRVKGNLEKNKQTLESDNKE----LTNEVKSLQQAKSESEHKRK-------KLEAQLQEVMARFSEGEKVKGEL 1297
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCqqhtLTQHIHTLQQQKTTLTQKLQslckeldILQREQATIDTRTSAFRDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1298 ADRTHKIQTELD----------NVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1367
Cdd:TIGR00618 427 AHAKKQQELQQRyaelcaaaitCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1368 LEQQEEEEESRKNLEKQLAT--LQAQLVETKKKLEDDVGALEGLEEVKRK----LQKDMEVTSQKLEEKAIAFDKLEKTK 1441
Cdd:TIGR00618 507 CGSCIHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVYHQLTSERKqrasLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1442 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKAlsmARALDEALEAKEEF 1521
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH---ALQLTLTQERVREH 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1522 ERLNKQLRAEMEDLISSKDDVGKNVHE-LEKSKRTLEQQVEEMRTQLEELEdelqatEDAKLRLEVNMQAMKAQfdRDLQ 1600
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIE------EYDREFNEIENASSSLG--SDLA 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1601 ARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL 1680
Cdd:TIGR00618 736 AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1681 EEARTSRDEIFTQSKENEK----KLKSLEAEILQLQEDLASSERARRHAEQERDELADE 1735
Cdd:TIGR00618 816 EDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1380-1948 |
1.19e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1380 NLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLmvdlDHQR 1459
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1460 QIVSNLEKKQKKFDQmlaEEKTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKqlraEMEDLISSK 1539
Cdd:PRK03918 238 EEIEELEKELESLEG---SKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSE----FYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1540 DDVGKNVHELEKSKRTLEQQV---EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqFDRDLQARDEQNEEKKRALVKQ 1616
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1617 VREMEAELEDERKqralavaAKKKLEMDLKDVEAQI---EAANKARDEAIKQLRKLQAQMKDYQRELEEARtsRDEIFtq 1693
Cdd:PRK03918 386 PEKLEKELEELEK-------AKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKCPVCGRELTEEH--RKELL-- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1694 sKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsgkaaLLDEKRRLEARIAQLEEELEEEQSN-ME 1772
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLEELEKKAEeYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1773 LLNDRFRKTTMQVDTLNTELagerSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLeqe 1852
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY--- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1853 aKERAAANKIVRRTEKKLKEVfmqvEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEAT-----RANASRRKLQRELD 1927
Cdd:PRK03918 602 -NEYLELKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeELREEYLELSRELA 676
|
570 580
....*....|....*....|.
gi 688558694 1928 DATEASEGLSREVNTLKNRLR 1948
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLE 697
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1029-1757 |
1.33e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 70.37 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1029 EMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL--QDQIAELQAQIDELKIQLak 1106
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqQEKIERYQADLEELEERL-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1107 keEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESE----------KAARNKAEKLKRD-------LSE 1165
Cdd:PRK04863 365 --EEQNEVVEEADEQQeeneARAEAAEEEVDELKSQLADYQQALDVQqtraiqyqqaVQALERAKQLCGLpdltadnAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1166 ELEALKTELED-TLDTTAAQQELRSK---REQ--EVAELKKAIDDET-------------------RNHESQIQEMRQRH 1220
Cdd:PRK04863 443 WLEEFQAKEQEaTEELLSLEQKLSVAqaaHSQfeQAYQLVRKIAGEVsrseawdvarellrrlreqRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1221 GTALEEISEQ------LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvk 1294
Cdd:PRK04863 523 SELEQRLRQQqraerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA-- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1295 geLADRTHKIQTELDNVSclledaEKKGIKLTkDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNnlleqqeee 1374
Cdd:PRK04863 601 --RAPAWLAAQDALARLR------EQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE--------- 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1375 eesrknlekQLATLQAQLVETKKKLEDDVGAL---EGLEEVkrKLQkDMEVTSQKLEE--KAIAFDKLEKTKNRLQQE-- 1447
Cdd:PRK04863 663 ---------RLSQPGGSEDPRLNALAERFGGVllsEIYDDV--SLE-DAPYFSALYGParHAIVVPDLSDAAEQLAGLed 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1448 -LDDLMV---DLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErDRAEAEAREKDTKALSMARALDEALEAKEEF-- 1521
Cdd:PRK04863 731 cPEDLYLiegDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEV-PLFGRAAREKRIEQLRAEREELAERYATLSFdv 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1522 ---ERLNKQLR----------------AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL--------------- 1567
Cdd:PRK04863 810 qklQRLHQAFSrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnllad 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1568 -------EELEDELQATEDAKL-------------RLEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMeaeleDE 1627
Cdd:PRK04863 890 etladrvEEIREQLDEAEEAKRfvqqhgnalaqlePIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TE 963
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1628 RKQRALAVAAKKKLEMDLKDVE------AQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1701
Cdd:PRK04863 964 VVQRRAHFSYEDAAEMLAKNSDlneklrQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1702 KSleaeiLQLQEDLASSERARRHaeqeRDELADEISNSASGKAALLDEKRRLEARI 1757
Cdd:PRK04863 1044 QD-----LGVPADSGAEERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
994-1787 |
1.48e-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: 70.08 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 994 TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM------MVDLEERLKKEEK 1067
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIehnlskIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1068 TRQELEKAKRKLDAETTDLQDQIAElqaQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLaELQEDLE 1147
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDE---QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL-LVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1148 SEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQevaeLKKAIDDETRNHESQIQEMRQRHGTALEEI 1227
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTL----VIERQEDEAKTAAQLCADLQSKERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1228 SEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEhKRKKLEAQLQEVMARFSegekvkgeLADRTHKIQTE 1307
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELRKAERELS--------KAEKNSLTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1308 LDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQL 1385
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmlTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1386 ATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDME-VTSQKLEEKAIAFDKLekTKNRLQQELDDLMVDLDHQRQIVSN 1464
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEsKEEQLSSYEDKLFDVC--GSQDEESDLERLKEEIEKSSKQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1465 LEKKQKKFDQMLAEEKTISARYAEERDR---AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSK-- 1539
Cdd:TIGR00606 658 LAGATAVYSQFITQLTDENQSCCPVCQRvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRqs 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1540 --DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQaTEDAKLRLEVNMQAMKAQFDRdLQARDEQNEekkralvKQV 1617
Cdd:TIGR00606 738 iiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKI 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1618 REMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIKQLRKLQA---QMKDYQRELEEARTSRDEIFT 1692
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQQVNQEKQEKQheLDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEE 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1693 QSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADeiSNSASGKAALL------------------------- 1747
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS--SKETSNKKAQDkvndikekvknihgymkdienkiqd 966
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 688558694 1748 ---DEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1787
Cdd:TIGR00606 967 gkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT 1009
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
825-1176 |
1.69e-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: 69.70 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 825 FAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPL-LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQ 903
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 904 LLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeea 983
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-------- 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 984 arqklqlekvtaeAKIKKMEEDILLLEDQnskflkekklledrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1063
Cdd:TIGR02168 845 -------------EQIEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1064 KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQK-NNALKQLRELQAQLAEL 1142
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRL 977
|
330 340 350
....*....|....*....|....*....|....
gi 688558694 1143 QEDLESEKAARNKAEKLKRDLSEELEALKTELED 1176
Cdd:TIGR02168 978 ENKIKELGPVNLAAIEEYEELKERYDFLTAQKED 1011
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1059-1952 |
2.05e-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: 69.60 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1059 EERLKKEEKT---RQELEKAKRKLDAEttdlQDQIAELQAQIDELKIQLAKKEEELQAvlarGDEEVAQKNNALKQLREL 1135
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQA----ASDHLNLVQTALRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1136 ---QAQLAELQEDLESEKAARnkaeklkrdlsEELEALKTELEDTLdtTAAQQELRSKREQeVAELKKAID-DETRNheS 1211
Cdd:COG3096 350 eryQEDLEELTERLEEQEEVV-----------EEAAEQLAEAEARL--EAAEEEVDSLKSQ-LADYQQALDvQQTRA--I 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1212 QIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegE 1291
Cdd:COG3096 414 QYQQAVQ----ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV-------C 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1292 KVKGELaDRthkiqteldnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEknnLLE 1369
Cdd:COG3096 483 KIAGEV-ER---------------SQAWQTARELLRRYRSQQALAQRLQQLRAQlaELEQRLRQQQNAERLLEE---FCQ 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1370 QQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVgalEGLEEVKRKLQkDMEVTSQKLEEKA----IAFDKLEKTKNRLQ 1445
Cdd:COG3096 544 RIGQQLDAAEELEELLAELEAQLEELEEQAAEAV---EQRSELRQQLE-QLRARIKELAARApawlAAQDALERLREQSG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1446 QELDDLmVDLDHQRQIVSNLEKKQKKFDQMLAEEKtisARYAEERDRAEAEAREKDTKALSMARAL----------DEAL 1515
Cdd:COG3096 620 EALADS-QEVTAAMQQLLEREREATVERDELAARK---QALESQIERLSQPGGAEDPRLLALAERLggvllseiydDVTL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1516 EAKEEFERLNKQLR---------------AEMED------LIS----SKDDVGKNVHELEK------SKRTL-------- 1556
Cdd:COG3096 696 EDAPYFSALYGPARhaivvpdlsavkeqlAGLEDcpedlyLIEgdpdSFDDSVFDAEELEDavvvklSDRQWrysrfpev 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1557 --------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDL-----QARDEQNEEKKRALVKQVREMEA 1622
Cdd:COG3096 776 plfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELER 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1623 ELED----ERKQRALAVAAKKKLEMdlkdVEAQIEAANKARDEAikqlrkLQAQMKDYQRELEEARTSRDEIFTQSK--- 1695
Cdd:COG3096 851 ELAQhraqEQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELDAAQEAQAFIQQHGKala 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1696 ENEKKLKSLEAEILQ---LQEDLASSERARRHAEQERDELADEISNSA----SGKAALLDEKRRLEARIAQLEEELEEEQ 1768
Cdd:COG3096 921 QLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEKLRARLEQAEEAR 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1769 SNmelLNDRFRKTTMQVDTLNTELAGERSAAQkseNARQQLerqnKDLKSKLQELEGSVKSkfkasiaaleakilqleeq 1848
Cdd:COG3096 1001 RE---AREQLRQAQAQYSQYNQVLASLKSSRD---AKQQTL----QELEQELEELGVQADA------------------- 1051
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1849 leqEAKERAAANKivrrtekklkevfmqvederrhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDD 1928
Cdd:COG3096 1052 ---EAEERARIRR-----------------------DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQ 1105
|
970 980 990
....*....|....*....|....*....|....
gi 688558694 1929 ATEASEG----------LSREvNTLKNRLRRGGP 1952
Cdd:COG3096 1106 EREQVVQakagwcavlrLARD-NDVERRLHRREL 1138
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1058-1840 |
2.34e-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: 69.48 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1058 LEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRE--- 1134
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSele 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1135 -LQAQL-AELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhesq 1212
Cdd:pfam12128 326 aLEDQHgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAK---- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1213 IQEMRQRHGTALEEISEQLEQAKRvkgnleknkQTLESDNKELTNEVKSLQQAKSEsehkrkkleAQLQEVMARFSEGEK 1292
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALESELR---------EQLEAGKLEFNEEEYRLKSRLGE---------LKLRLNQATATPELL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1293 VKGELAD-RTHKIQTELdnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqq 1371
Cdd:pfam12128 464 LQLENFDeRIERAREEQ-------EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ-------- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1372 eeeeesrknLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLektknRLQQelddl 1451
Cdd:pfam12128 529 ---------LFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKL-----DLKR----- 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1452 mvdLDHQRQIVSNlekkqkkfDQMLAEEKTISARYAEERDRAEAEarekdTKALSMARALDEALEAKEEFERlnkqlrae 1531
Cdd:pfam12128 590 ---IDVPEWAASE--------EELRERLDKAEEALQSAREKQAAA-----EEQLVQANGELEKASREETFAR-------- 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1532 mEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEledELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKR 1611
Cdd:pfam12128 646 -TALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE---RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1612 ALVKQVREMEAELEDERKQRALAVAAKkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIf 1691
Cdd:pfam12128 722 VVEGALDAQLALLKAAIAARRSGAKAE------LKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV- 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1692 TQSKENEKKLKSLEAEILQLQedlasSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNM 1771
Cdd:pfam12128 795 LRYFDWYQETWLQRRPRLATQ-----LSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEM 869
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1772 ELLNdrfrktTMQVDTLNTELAGERSaaqksenarqQLERQNKDLKSKLQELEGSVKSK---FKASIAALEA 1840
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 |
3.65e-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: 3.65e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 688558694 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, ... |
1018-1236 |
4.37e-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: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1018 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1097
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1098 DELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLeseKAARNKAEKLKRDLSEELEALKTELEDT 1177
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL---RADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1178 LDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKR 1236
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1060-1731 |
7.22e-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: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1060 ERLKK-EEKTRQELEKAKRKLDAETTDLQDQ---IAELQAQIDELKIQLakkEEELQAvlargDEEVAQKNNALKQ---- 1131
Cdd:pfam05483 88 EKIKKwKVSIEAELKQKENKLQENRKIIEAQrkaIQELQFENEKVSLKL---EEEIQE-----NKDLIKENNATRHlcnl 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1132 LRELQAQLAELQEDLESEkaaRNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKREQE---VAELKKAIDDETR 1207
Cdd:pfam05483 160 LKETCARSAEKTKKYEYE---REETRQVYMDLNNNIEKMILAFEElRVQAENARLEMHFKLKEDhekIQHLEEEYKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1208 NHESQI---------QEMRQRHGT-ALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE 1277
Cdd:pfam05483 237 DKEKQVsllliqiteKENKMKDLTfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1278 AQLQ---EVMARFSEGEKVKGELADRTHK----IQTELDNVSCLLED---AEKKGIKLTKD-VSSLESQLQDTQELLQEE 1346
Cdd:pfam05483 317 EDLQiatKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEEllrTEQQRLEKNEDqLKIITMELQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1347 TRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQ------LVETKKK----LEDDVGALEGLEEVKRKL 1416
Cdd:pfam05483 397 TKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKeqelifLLQAREKeihdLEIQLTAIKTSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1417 QKDMEVTSQKLEEKAIAF----DKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKfdqMLAEEKTISARYAEERDR 1492
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELtahcDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1493 AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELED 1572
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1573 ELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQI 1652
Cdd:pfam05483 630 QLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALM 709
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1653 EAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRdeiftqskenEKKLKSLEAEILQLQEDLASSERARRHAEQERDE 1731
Cdd:pfam05483 710 EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL----------EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
919-1650 |
7.28e-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: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 919 TELFAEAEEMR-------ARLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQshiqdleeqldeeeaarqkLQLE 991
Cdd:pfam05483 81 SKLYKEAEKIKkwkvsieAELKQKENKLQENRKIIEAQRKAI----QELQFENEKVS-------------------LKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 992 KVTAEAKikkmeeDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNL-GKVKNKQEMMMVDLEERLKKEEKTRQ 1070
Cdd:pfam05483 138 EEIQENK------DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVyMDLNNNIEKMILAFEELRVQAENARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1071 E----LEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQAQlaELQEDL 1146
Cdd:pfam05483 212 EmhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKD-LTFLLEESRDKANQLEEKTKLQDE--NLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1147 ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAiddetRNHESQIQEMRQRHGTALEE 1226
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1227 ISEQLEQakrvkgNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQT 1306
Cdd:pfam05483 364 LLRTEQQ------RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1307 ELDNVSCLLEDAEKK----GIKLTKDVSSLESQLQDTQELLQEETRQKLnlssRIRQLEEEKNNLLEQQEEEEESRKNLE 1382
Cdd:pfam05483 437 KEQELIFLLQAREKEihdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKL----KNIELTAHCDKLLLENKELTQEASDMT 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1383 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTS----QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQ 1458
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVReefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1459 RQIVSNLEK----KQKKFDQMLAEEKTIsaryaeeRDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1534
Cdd:pfam05483 593 ENKCNNLKKqienKNKNIEELHQENKAL-------KKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIED 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1535 LISSKDDVgknVHELEKSKRTLEQQVeemrtqleELEDELQATEDAKLRLEVN-MQAMKAQFDRDLQARDEQ-----NEE 1608
Cdd:pfam05483 666 KKISEEKL---LEEVEKAKAIADEAV--------KLQKEIDKRCQHKIAEMVAlMEKHKHQYDKIIEERDSElglykNKE 734
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 688558694 1609 KKRALVKQVREME-----AELEDERKQRALAVAAKKKLEMDLKDVEA 1650
Cdd:pfam05483 735 QEQSSAKAALEIElsnikAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1057-1298 |
8.14e-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: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1057 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvlargdeevaqknnALKQLRELQ 1136
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--------------LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1137 AQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhESQIQEM 1216
Cdd:COG4942 97 AELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1217 RQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG--EKVK 1294
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgfAALK 252
|
....
gi 688558694 1295 GELA 1298
Cdd:COG4942 253 GKLP 256
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
872-1289 |
8.49e-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: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 872 EMQAKDEELikvKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLESRVE 951
Cdd:pfam05483 385 ELQKKSSEL---EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE-KIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 952 EEEERNQSLQNEKKKMqshiqdleeqldeeeaarqKLQLEKvtaeAKIKKMEedillLEDQNSKFLKEKKLLEDRVGEMT 1031
Cdd:pfam05483 461 AIKTSEEHYLKEVEDL-------------------KTELEK----EKLKNIE-----LTAHCDKLLLENKELTQEASDMT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1032 SQLAEEEEKAKNlgkVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL 1111
Cdd:pfam05483 513 LELKKHQEDIIN---CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1112 QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1191
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1192 EQ--------------EVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKN----KQTLESDNK 1253
Cdd:pfam05483 670 EEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEqssaKAALEIELS 749
|
410 420 430
....*....|....*....|....*....|....*.
gi 688558694 1254 ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1289
Cdd:pfam05483 750 NIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1087-1308 |
8.51e-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: 65.94 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1087 QDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1166
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1167 LEALKTELEDTLDTTAAQ--QELRSKREQEVAELKKAID-DETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEK 1243
Cdd:COG4942 92 IAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1244 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1308
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
863-1451 |
1.08e-10 |
|
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: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 863 LLQVTRQEE--EMQAKDEELIKVKERQVK-----VENELVEMERKHQQLLEEKNILAEQ----LQAETELFAEAEEMRAR 931
Cdd:pfam12128 272 TLIASRQEErqETSAELNQLLRTLDDQWKekrdeLNGELSAADAAVAKDRSELEALEDQhgafLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 932 LVAKKQELEEILHDLESRVEEEEERNQSLqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDI-LLLE 1010
Cdd:pfam12128 352 WQSELENLEERLKALTGKHQDVTAKYNRR--RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELrEQLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1011 DQNSKFLKEKKLLEDRVGEMTSQLAE---EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1087
Cdd:pfam12128 430 AGKLEFNEEEYRLKSRLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1088 D---QIAELQAQIDELKIQLAKK---------------EEELQAVLARG------------DEEVAQKNNA------LKQ 1131
Cdd:pfam12128 510 QasrRLEERQSALDELELQLFPQagtllhflrkeapdwEQSIGKVISPEllhrtdldpevwDGSVGGELNLygvkldLKR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1132 L---------RELQAQLAELQEDLESEKA-----------ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1191
Cdd:pfam12128 590 IdvpewaaseEELRERLDKAEEALQSAREkqaaaeeqlvqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1192 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKgnlEKNKQTLESDnkeLTNEVKSLQQAKSESEH 1271
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK---QAYWQVVEGA---LDAQLALLKAAIAARRS 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1272 KRKKLEAQLQEVMARFSEGEKVKGelaDRTHKIQTELDNVSCLLEDAEKKGikltKDVSSLESQLQDTqeLLQEETRQKL 1351
Cdd:pfam12128 744 GAKAELKALETWYKRDLASLGVDP---DVIAKLKREIRTLERKIERIAVRR----QEVLRYFDWYQET--WLQRRPRLAT 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1352 NLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVK-----RKLQKDMEVTSQK 1426
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERLAQ 894
|
650 660
....*....|....*....|....*
gi 688558694 1427 LEEkaiAFDKLEKTKNRLQQELDDL 1451
Cdd:pfam12128 895 LED---LKLKRDYLSESVKKYVEHF 916
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
938-1292 |
1.12e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.97 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 938 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1017
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1018 KEKKLLEDRVgemtsqlaeeeekaKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1097
Cdd:TIGR04523 419 QEKELLEKEI--------------ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1098 DELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRDLSEELEALKTELedt 1177
Cdd:TIGR04523 485 EQKQKELKSKEKELKKL----NEEKKELEEKVKDLTKKISSLKEKIEKLESEK---KEKESKISDLEDELNKDDFEL--- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1178 ldTTAAQQELRSKREQEVAELKKAIDDETRNHEsQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTN 1257
Cdd:TIGR04523 555 --KKENLEKEIDEKNKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
330 340 350
....*....|....*....|....*....|....*
gi 688558694 1258 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEK 1292
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
788-1310 |
1.17e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 788 FFRTGVLahleEERDL--KITDIIIYFQSVCRgylARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWW 854
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 855 RLFTKVKpLLQ--VTRQEEEMQAKDEELIKVKERQVKVENELVEMerkHQQLLEEKNILAEQLQAETElfaEAEEMRARL 932
Cdd:COG4913 285 FAQRRLE-LLEaeLEELRAELARLEAELERLEARLDALREELDEL---EAQIRGNGGDRLEQLEREIE---RLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 933 VAKKQELEEILHDLESRVEEEEernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 1012
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1013 NS----KFLKEKKLLEDRVGEMTS---------QLAEEEEK-------------------AKNLGKV-----KNKQEMMM 1055
Cdd:COG4913 435 KSnipaRLLALRDALAEALGLDEAelpfvgeliEVRPEEERwrgaiervlggfaltllvpPEHYAAAlrwvnRLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1056 VDLEERLKKEEKTRQELEKAK--RKLDAETTDLQDQI-AELQAQIDELKIQlakKEEELQ--------AVLARGDEEVAQ 1124
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLeAELGRRFDYVCVD---SPEELRrhpraitrAGQVKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1125 KN-------------NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELE---DTLDTTAAQQELR 1188
Cdd:COG4913 592 KDdrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1189 SKrEQEVAELKKAIDDetrnhesqIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQA--- 1265
Cdd:COG4913 672 EL-EAELERLDASSDD--------LAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRlea 738
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 688558694 1266 --KSESEHKRKKLEAQLQEVMARFSEGEKVKgELADRTHKIQTELDN 1310
Cdd:COG4913 739 aeDLARLELRALLEERFAAALGDAVERELRE-NLEERIDALRARLNR 784
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1553-1759 |
2.10e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1553 KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnMQAMKAQFDR--DLQARDEQNEEKKRALVKQVREMEAELEDERKQ 1630
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1631 RALAvaAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ-AQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1709
Cdd:COG4913 299 ELRA--ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 1710 QLQEDLAS-SERARRHAE---QERDELADEISNSASGKAALLDEKRRLEARIAQ 1759
Cdd:COG4913 377 ASAEEFAAlRAEAAALLEaleEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1510-1744 |
2.20e-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: 64.79 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1510 ALDEALEAKEEFERLNKQL---RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1586
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIaelEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1587 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQL 1666
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1667 RKLQAQMKDYQRELEEARTSRDEIFTQSkenEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1744
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1038-1438 |
2.44e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1038 EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQA--VL 1115
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1116 ARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEV 1195
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1196 AELKKAIDDETRNHESQIQEMRQRHgtALEEISEQLEQAKR-------------------------------VKGNLEKN 1244
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLllliaaallallglggsllsliltiagvlflVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1245 KQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIK 1324
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1325 LTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEE--EKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1400
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 688558694 1401 DDVGALEGLEEVKRKLQKDMEVtSQKLEEKAIAFDKLE 1438
Cdd:COG4717 450 ELREELAELEAELEQLEEDGEL-AELLQELEELKAELR 486
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
985-1756 |
3.72e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.36 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 985 RQKLQLEKVTAEAKIKKMEEDILLLEDQnskfLKEKKLLedrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKk 1064
Cdd:PRK04863 336 HLNLVQTALRQQEKIERYQADLEELEER----LEEQNEV---VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALD- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1065 EEKTR--------QELEKAKRKLDA---ETTDLQDQIAELQAQIDEL---------KIQLAKK-----EEELQAVLARGD 1119
Cdd:PRK04863 408 VQQTRaiqyqqavQALERAKQLCGLpdlTADNAEDWLEEFQAKEQEAteellsleqKLSVAQAahsqfEQAYQLVRKIAG 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1120 E---EVAQKN--NALKQLRE----------LQAQLAELQEDLESEKAAR------NKAEKLKRDLSEELEALKTELEDTL 1178
Cdd:PRK04863 488 EvsrSEAWDVarELLRRLREqrhlaeqlqqLRMRLSELEQRLRQQQRAErllaefCKRLGKNLDDEDELEQLQEELEARL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1179 DTTAAQQElrskreqEVAELKKAIDDETRNHESQIQEMRQRhGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNE 1258
Cdd:PRK04863 568 ESLSESVS-------EARERRMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLER 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1259 VKSLQQAKSESEHKRKKLEAQLQEVMAR-FSEGEKVKGeLADRTHKIQ-TEL-DNVSclLEDA----------------- 1318
Cdd:PRK04863 640 ERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNA-LAERFGGVLlSEIyDDVS--LEDApyfsalygparhaivvp 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1319 EKKGIK---------------LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNlleqqeeeeeSRKNLEK 1383
Cdd:PRK04863 717 DLSDAAeqlagledcpedlylIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLF----------GRAAREK 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1384 QLATLQAQ---LVETKKKLEDDVgalegleevkRKLQKDMEVTSQKL-EEKAIAFD-----KLEKTKNRLQQ---ELDDL 1451
Cdd:PRK04863 787 RIEQLRAEreeLAERYATLSFDV----------QKLQRLHQAFSRFIgSHLAVAFEadpeaELRQLNRRRVElerALADH 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1452 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTIsaryAEER--DRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1529
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALNRLLPRLNLL----ADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ 931
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1530 AEMEDLisskDDVGKNVHELEKSKRTLEQQVEEMrTQLEELEDELqATEDAklrleVNMQAMKAQFDRDLQARDEQNEEK 1609
Cdd:PRK04863 932 SDPEQF----EQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHF-SYEDA-----AEMLAKNSDLNEKLRQRLEQAEQE 1000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1610 KRALVKQVREMEAELEDerkqralavaaKKKLEMDLKdveAQIEAANKARDEAIKQLRKLQAQmkdYQRELEE-ARTSRD 1688
Cdd:PRK04863 1001 RTRAREQLRQAQAQLAQ-----------YNQVLASLK---SSYDAKRQMLQELKQELQDLGVP---ADSGAEErARARRD 1063
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688558694 1689 EIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL------DEKRRLEAR 1756
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLrlvkdnGVERRLHRR 1137
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1259-1729 |
4.00e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1259 VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ- 1337
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1338 -DTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEddvgalEGLEEVKRKL 1416
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEER-----------LEELRELEEELEELEAELAELQEELE------ELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1417 QKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH--QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1494
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1495 AEAREKDTKALSMA----------RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR 1564
Cdd:COG4717 271 LILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1565 TQLEELEDELQ--ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVREMEAELEDERK--QRALAVAAKKK 1640
Cdd:COG4717 351 ELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGelEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1641 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY--QRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLASS 1718
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEEL-------KAELRELAEEWAALKLALELL 502
|
490
....*....|.
gi 688558694 1719 ERARRHAEQER 1729
Cdd:COG4717 503 EEAREEYREER 513
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1000-1508 |
4.47e-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: 64.84 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1000 KKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEE--EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELE 1073
Cdd:pfam10174 137 KTLEEMELRIETQkqtlGARDESIKKLLEMLQSKGLPKKSGEEdwERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELH 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1074 KAKRKLD--AETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQlaelqedlesEKA 1151
Cdd:pfam10174 217 RRNQLQPdpAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSH----------SKF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1152 ARNKAEKLKRDLSE---ELEALKTELE-------------DTLDTTAAQQELRSKREQ-EVAELKKAIDDETR---NHES 1211
Cdd:pfam10174 287 MKNKIDQLKQELSKkesELLALQTKLEtltnqnsdckqhiEVLKESLTAKEQRAAILQtEVDALRLRLEEKESflnKKTK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1212 QIQEMRQRHGTALEEIS------------------------EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKS 1267
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRdlkdmldvkerkinvlqkkienlqEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALS 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1268 ESE-------HKRKKLEAQLQEVMARFSEGEKV--------KGELADRTHKIQTELDNVSCLLEDAEKKGIKL------- 1325
Cdd:pfam10174 447 EKEriierlkEQREREDRERLEELESLKKENKDlkekvsalQPELTEKESSLIDLKEHASSLASSGLKKDSKLksleiav 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1326 ---TKDVSSLESQLQDTQElLQEETRQKLNLSSRIRQLEEEknnLLEQQEEEEESRKNLEKQLATLQAqlVETKKKLEDD 1402
Cdd:pfam10174 527 eqkKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE---VARYKEESGKAQAEVERLLGILRE--VENEKNDKDK 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1403 -VGALEGLEEVKRKLQ--KDMEVTSQKLEEKAIAFDKLEK--------TKNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1471
Cdd:pfam10174 601 kIAELESLTLRQMKEQnkKVANIKHGQQEMKKKGAQLLEEarrrednlADNSQQLQLEELMGALEKTRQELDATKARLSS 680
|
570 580 590
....*....|....*....|....*....|....*..
gi 688558694 1472 FDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1508
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1632-1866 |
5.77e-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: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1632 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQL 1711
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1712 QEDLasserarrhaEQERDELADEIS----NSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLnDRFRKTTMQVDT 1787
Cdd:COG4942 96 RAEL----------EAQKEELAELLRalyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1788 LNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1866
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1377-1640 |
8.58e-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: 62.86 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1377 SRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1456
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1457 HQRQivsNLEKKQKKFDQMLAEektisaryaeerdrAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLI 1536
Cdd:COG4942 94 ELRA---ELEAQKEELAELLRA--------------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1537 SSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQARDEQNEEKKRALVKQ 1616
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 688558694 1617 VREMEAELEDERKQRALAVAAKKK 1640
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1303-1947 |
1.09e-09 |
|
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: 63.50 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1303 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1382
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1383 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1462
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1463 SNLEKKQKKFDQMLAEektisaryaeerdraeAEAREKDTKALSmaralDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1542
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQ----------------ISELKKQNNQLK-----DNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1543 GKNVHELEKSkrtlEQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA 1622
Cdd:TIGR04523 263 NKIKKQLSEK----QKELEQNNKKIKELEKQLN---QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1623 ELEDERKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLK 1702
Cdd:TIGR04523 336 IISQLNEQIS-------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1703 SLEAEILQLQEDLASSERARRHAEQERDELADEISNsasgkaaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTT 1782
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-------LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1783 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKsKFKASIAALEAKILQleeqleqeaKERAAANKI 1862
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISD---------LEDELNKDD 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1863 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNT 1942
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
....*
gi 688558694 1943 LKNRL 1947
Cdd:TIGR04523 632 IIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1493-1718 |
1.65e-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: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1493 AEAEAREKDTKALSMARA-LDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE 1571
Cdd:COG4942 17 AQADAAAEAEAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1572 DELQATEDAKLRLEVNMQAMK--------------AQFDRDLQARDEQNeekkRALVKQVREMEAELEDERKQRALAVAA 1637
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLA----PARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1638 KKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLAS 1717
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPA 245
|
.
gi 688558694 1718 S 1718
Cdd:COG4942 246 A 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1504-1745 |
1.71e-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: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1504 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR 1583
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1584 LEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAI 1663
Cdd:COG4942 88 LEKEIAELRAE----LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1664 KQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGK 1743
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 688558694 1744 AA 1745
Cdd:COG4942 244 PA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1086-1830 |
1.71e-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: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1086 LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLREL-QAQLAELQE-DLESEKAARNKAEKLK--R 1161
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEEIQenK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1162 DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqemrqrhgTALEEISEQLEQAK-----R 1236
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlemhfK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1237 VKGNLEKNKQTLESDNKELTN---EVKSLQQAKSESEHKRKKLEAQLQEVMARFSE-GEKVK------GELADRTHKIQT 1306
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDkekQVSLLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKlqdenlKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1307 ELDNVSCLLEDAEKKGIKLTKDV---SSLESQLQDTQELLQEET-RQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1382
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLqiaTKTICQLTEEKEAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1383 KQLATLQAQLVETKKKLEDdVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqiv 1462
Cdd:pfam05483 377 DQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLL---------- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1463 SNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLISS 1538
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENKELTQEASDMTLELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1539 KddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDEL-QATEDAKLRLEVNMQAMKAQFDRDLQARDEQN--EEKKRALVK 1615
Cdd:pfam05483 526 K----KQEERMLKQIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKK 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1616 QVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFtqsk 1695
Cdd:pfam05483 602 QIENKNKNIEELHQENK---ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL---- 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1696 ENEKKLKSLEAEILQLQEdlasserarrhaeqerdELADEISNSASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLN 1775
Cdd:pfam05483 675 EEVEKAKAIADEAVKLQK-----------------EIDKRCQHKIAEMVALMEKHKHQYDKIIEER------DSELGLYK 731
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1776 DRFRKTTMQVDTLNTELAGERsAAQKSENARQQLERQNKD-LKSKLQELEGSVKSK 1830
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIK-AELLSLKKQLEIEKEEKEkLKMEAKENTAILKDK 786
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
864-1238 |
2.06e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 864 LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL---- 939
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 940 EEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKE 1019
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1020 KK------------LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1087
Cdd:COG4717 271 LIltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1088 DQIAELQAQIDELKIQLAKKEEE--LQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKlkrdlSE 1165
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----AL 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558694 1166 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHEsqIQEMRQRHGTALEEISEQLEQAKRVK 1238
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALK 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
913-1301 |
2.26e-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: 62.45 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 913 EQLQAETELFAEAEEMRA-------RLVAKKQELEEILHDLESRVEEEEERNQSLQNEK--KKMQSHIQDLEEQLDEEEA 983
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 984 ARQKLQLEKVTAEAKIKKmeEDILLLEDQNSKFLKEKKL----LEDRVGEMtsQLAEEEEKAKNLGKVKNKQEMMMvdle 1059
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKREL--ERIRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1060 ERLKKEEKTRQELEKAkRKLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLR-ELQAQ 1138
Cdd:pfam17380 386 ERQQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIR---AEQEEARQREVRRLEEERAREMERVRLEEqERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1139 LAELQEDLESEKAARNKAEKLKRDLSEelealkteledtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQ 1218
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKR-----------------AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1219 RHGTALEEiseqleqAKRVKGNLEKNKQtlesdnKELtNEVKSLQQAKSESEHKRKKLEA--QLQEVMARFSEGEKVKGE 1296
Cdd:pfam17380 525 RQKAIYEE-------ERRREAEEERRKQ------QEM-EERRRIQEQMRKATEERSRLEAmeREREMMRQIVESEKARAE 590
|
....*
gi 688558694 1297 LADRT 1301
Cdd:pfam17380 591 YEATT 595
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1092-1925 |
2.35e-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: 62.76 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1092 ELQAQIDEL--KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1169
Cdd:TIGR00606 170 ALKQKFDEIfsATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1170 LKT---ELEDTL-------DTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKG 1239
Cdd:TIGR00606 250 LKNrlkEIEHNLskimkldNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1240 NLEKNKQTLESDNKELTNEVKSLQ-QAKSESEHKRKKlEAQLQEVMARFSEGEKVKGELADRthkiqtELDNVSCL-LED 1317
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLATRLELDGFERGPFSER------QIKNFHTLvIER 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1318 AEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrknLEKQlatlQAQLVETKK 1397
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEI----------------LEKK----QEELKFVIK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1398 KLEDDVGALEGLEEVKRKLQKDMEVTSqKLEEKAIAFDKLEKTKNRLQQELDdlmvdldhqrqivsnLEKKQKKFDQMLA 1477
Cdd:TIGR00606 462 ELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQNEKAD---------------LDRKLRKLDQEME 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1478 EEKtisaRYAEERDRAEAEAREKDTKalsmaraldealeakeeFERLNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLE 1557
Cdd:TIGR00606 526 QLN----HHTTTRTQMEMLTKDKMDK-----------------DEQIRKIKSRHSDELTSLLGYF-PNKKQLEDWLHSKS 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1558 QQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFDRDLQARDEQneekkralvkqvremEAELEDerkqRALAVAA 1637
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ---------------LSSYED----KLFDVCG 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1638 KKKLEMDLKDVEAQIEAANKardeaikQLRKLQAQMKDYQRELEEARTSR-------DEIFTQSKENEKKLKSLEAEILQ 1710
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRL 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1711 LQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMElLNDRFRKTTMQVDTLNT 1790
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAK 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1791 ELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVK----SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1866
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1867 EKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRE 1925
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1058-1534 |
3.30e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1058 LEERLKKEektRQELEKAKRKLDaetTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQA 1137
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1138 QLAELQEDLEsekaARNKAEKLKRDLSEELEALKtELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR 1217
Cdd:COG4717 120 KLEKLLQLLP----LYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1218 QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAksesehKRKKLEAQLQEVMARFSEGEKVKGEL 1297
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE------ERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1298 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEES 1377
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1378 RKNLEKQLATLQAQLvetkkkleddvgALEGLEEVKRKLQKDMEVTS-QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1456
Cdd:COG4717 349 LQELLREAEELEEEL------------QLEELEQEIAALLAEAGVEDeEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1457 HQRQIVSNLEKKQKKfdQMLAEEKTISARYAEERDRAEAEAREKDTKaLSMARALDEALEAKEEFERLNKQLRAEMED 1534
Cdd:COG4717 417 ELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAE-LEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
958-1184 |
3.62e-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: 60.93 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 958 QSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEE 1037
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1038 EEKaknLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLAR 1117
Cdd:COG4942 103 KEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1118 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ 1184
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1418-1813 |
6.14e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1418 KDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQmLAEEKTISARYAEERDRAEA-E 1496
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1497 AREKDTKAL--SMARALDEALEAKEEFERLNKQL----RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEL 1570
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1571 EDELQATEDAK-----------------------------------LRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVK 1615
Cdd:COG4717 233 ENELEAAALEErlkearlllliaaallallglggsllsliltiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1616 QVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRkLQAQMKDYQRELEEARTSRDEIFTQSK 1695
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1696 ENEKKLKSLEAEILQLQEDLASSERARRH--AEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1773
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 688558694 1774 --LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQN 1813
Cdd:COG4717 472 aeLLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
903-1284 |
7.78e-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: 60.29 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 903 QLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEE 982
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 983 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERL 1062
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1063 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAvlargdeevaqknnALKQLRELQAQLAel 1142
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEA--------------LLEELRSLQERLN-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1143 qedlesekAARNKAEKLKRDLSE---------------ELEALKTELEdTLDTTAAQQELRSKREQEVAELKKAIDDETR 1207
Cdd:pfam07888 248 --------ASERKVEGLGEELSSmaaqrdrtqaelhqaRLQAAQLTLQ-LADASLALREGRARWAQERETLQQSAEADKD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1208 NHESQIQEMRQRHGTALEEISEQleQAKRVKGNLEK--NKQTLESDNKELTNEVKSLQQAKSESEHkrkkLEAQLQEVM 1284
Cdd:pfam07888 319 RIEKLSAELQRLEERLQEERMER--EKLEVELGREKdcNRVQLSESRRELQELKASLRVAQKEKEQ----LQAEKQELL 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1087-1312 |
1.06e-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: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1087 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEE 1166
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1167 LEALK---------------TELEDTLDTTAAQQELRSKREQEVAELKKAIdDETRNHESQIQEMRQRHGTALEEISEQL 1231
Cdd:COG3883 92 ARALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1232 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1311
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
.
gi 688558694 1312 S 1312
Cdd:COG3883 251 A 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
985-1291 |
1.23e-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: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 985 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR--VGEMTSQLAEEEEKAKNLgkvknKQEMMMVD-LEER 1061
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELERL-----DASSDDLAaLEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1062 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1141
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1142 LQEDLESEKA-ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQE-----VAELKKAIDDETRNHESQIQ- 1214
Cdd:COG4913 774 RIDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFVADLLs 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1215 EMRQrhgtALEEISEQLEQAKRVKGNLEKNKQT---LESDNKELTnEVKSLQQ--------AKSESEHKRKKLEAQLQEV 1283
Cdd:COG4913 854 KLRR----AIREIKERIDPLNDSLKRIPFGPGRylrLEARPRPDP-EVREFRQelravtsgASLFDEELSEARFAALKRL 928
|
....*...
gi 688558694 1284 MARFSEGE 1291
Cdd:COG4913 929 IERLRSEE 936
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1066-1288 |
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 688558694 1066 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQ--LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1143
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1144 EDLES--EKAARNKAEKLKRDLSEELEALKTELEDTLDT-TAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRH 1220
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQ-IAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1221 GTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFS 1288
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
900-1281 |
1.44e-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: 60.14 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 900 KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEIlhdlESRVEEEEERNQSLQNEKKKMqshiqdleeqld 979
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA----EKARQAEMDRQAAIYAEQERM------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 980 eeeAARQKLQLEKVTAEAKIKKMEEdillledqnskflkekklledrvgemtsqlAEEEEKAKNLGKVKNKQEMMMvdle 1059
Cdd:pfam17380 343 ---AMERERELERIRQEERKRELER------------------------------IRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1060 ERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDELK--------IQLAKKEEELQAVLARGDEEVAQKNNALKQ 1131
Cdd:pfam17380 386 ERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVER 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1132 LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEElealktELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHES 1211
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1212 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQtlesdNKELTNEVKslqqaksESEHKRKKLEAQLQ 1281
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----EREMMRQIV-------ESEKARAEYEATTP 596
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1557-1769 |
1.59e-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: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1557 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVA 1636
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1637 AKKKLEMDLKDVEAQIEAANKArdEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLA 1716
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 688558694 1717 SSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQS 1769
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1479-1949 |
1.70e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1479 EKTISARYAEERDRAEAEArekdtkALSMARALDEALEAKEEFERLNkqlraemeDLISSKDDVGKNVHELEKSKRTLEQ 1558
Cdd:PRK02224 169 ERASDARLGVERVLSDQRG------SLDQLKAQIEEKEEKDLHERLN--------GLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1559 QVEEMRTQLEELEDELQATEDAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1638
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIE------------DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1639 KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlqedLASS 1718
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE-------LEEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1719 ERARRHAEQERDELADEIsnsasgkaalldekRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELageRSA 1798
Cdd:PRK02224 376 REAVEDRREEIEELEEEI--------------EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL---RTA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1799 AQKSENARQQLERQNkdLKSKLQELEGS----VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVrRTEKKLKEVF 1874
Cdd:PRK02224 439 RERVEEAEALLEAGK--CPECGQPVEGSphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLE 515
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1875 MQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1949
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1240-1839 |
2.38e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.53 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1240 NLEKNKQTLESDNKELTNEVKSLQQAK---SESEHKRKKLEAQLQEVMarfsegekvkgelaDRTHKIQTELDNVSCLLE 1316
Cdd:PRK01156 184 NIDYLEEKLKSSNLELENIKKQIADDEkshSITLKEIERLSIEYNNAM--------------DDYNNLKSALNELSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1317 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIrqleeeknnlleqqeeeeESRKNLEKQLATLQAQLVETK 1396
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPV------------------YKNRNYINDYFKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1397 KKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1476
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV--------LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1477 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEAleaKEEFERLNKQLRAemedLISSKDDVGKNVHEL------- 1549
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI---SSKVSSLNQRIRA----LRENLDELSRNMEMLngqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1550 --------EKSKRTLEQQVEE---MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVR 1618
Cdd:PRK01156 457 vcgttlgeEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-RADLEDIK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1619 EMEAELEDERKQRALAVAAKKklEMDLKDVEAQ---------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1683
Cdd:PRK01156 536 IKINELKDKHDKYEEIKNRYK--SLKLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1684 RTSRDEIFtqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELAdeisnsasGKAALLDEKRRLEARIAQleee 1763
Cdd:PRK01156 614 KSYIDKSI---REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSIIPDLKEITSRIND---- 678
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1764 leeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvksKFKASIAALE 1839
Cdd:PRK01156 679 ----------IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK-----KIKKAIGDLK 739
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
865-1285 |
2.51e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 865 QVTRQEEEMQAKDEELIKVKERQVKVENELVEME---RKHQQLLEEKNILAEQLQAETELFAEAEEMRaRLVAKKQELEE 941
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELReelEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 942 ILHDLESRVEEEEERNQSLQNEKKK----MQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1017
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1018 KEKKLLEDR-----VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1092
Cdd:COG4717 241 LEERLKEARlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1093 LQAQIDELKIQLAKKEEELQAVLARgdeevaqknnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKT 1172
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDR-----------IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1173 ELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1252
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
410 420 430
....*....|....*....|....*....|...
gi 688558694 1253 keltnevkSLQQAKSESEHKRKKLEAQLQEVMA 1285
Cdd:COG4717 470 --------ELAELLQELEELKAELRELAEEWAA 494
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1590-1757 |
2.94e-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: 56.47 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1590 AMKAQFDR--DLQARD---EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIK 1664
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1665 QLRKLQA--QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsg 1742
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL-- 158
|
170
....*....|....*
gi 688558694 1743 kAALLDEKRRLEARI 1757
Cdd:COG1579 159 -EELEAEREELAAKI 172
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
828-1428 |
3.23e-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: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 828 KQQQLSALKVLQRNCAAYLKLRHWqwwRLFTKVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERK---HQQL 904
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 905 LEEKNILAEQLQAETELFAEAEEMRAR------------LVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQ 972
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 973 DLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFlkEKKL--------LEDRVGEMTSQLAEEEEKAKNL 1044
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY--EDKLfdvcgsqdEESDLERLKEEIEKSSKQRAML 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1045 GKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQ 1124
Cdd:TIGR00606 659 AGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1125 KNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRS---KREQEVAELKKA 1201
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDverKIAQQAAKLQGS 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1202 IDDETRnheSQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQ 1281
Cdd:TIGR00606 819 DLDRTV---QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST 895
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1282 EVMARFSE--------------GEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQE--LLQE 1345
Cdd:TIGR00606 896 EVQSLIREikdakeqdspletfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdyLKQK 975
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1346 ETrqklNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLveTKKKLEDDVGALEGLEEVKRKLQKDMEV 1422
Cdd:TIGR00606 976 ET----ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNL--TLRKRENELKEVEEELKQHLKEMGQMQV 1049
|
....*.
gi 688558694 1423 TSQKLE 1428
Cdd:TIGR00606 1050 LQMKQE 1055
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
878-1833 |
3.26e-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: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 878 EELIKVKERQVKVENELVEMERKHQQLLEEKniLAEQLQAETELFAEAEEMRARLVAK-KQELEEILHDLESRVEEEEER 956
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMETATVELH--LSNIENKKNELLDIIVEIKKHIHGEiNKDLNKILEDFKNKEKELSNK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 957 NQSLQNEK---KKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQ 1033
Cdd:TIGR01612 771 INDYAKEKdelNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1034 LAEEEEKAKNlgKVKNKQEMMmVDLEERLKKEEKTRQeLEKAKRKLDaettDLQDQIAELQAQIDE--LKIQLAKKEEEL 1111
Cdd:TIGR01612 851 FINFENNCKE--KIDSEHEQF-AELTNKIKAEISDDK-LNDYEKKFN----DSKSLINEINKSIEEeyQNINTLKKVDEY 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1112 QAVLARGDEEVAQKNNALKQLRE-LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTlDTTAAQQEL--- 1187
Cdd:TIGR01612 923 IKICENTKESIEKFHNKQNILKEiLNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLN-DYEAKNNELiky 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1188 ------------RSKREQEVAELKKAIDD---ETRNHESQIQEMRQRHGTALEEISEQLEqaKRVKGNLEK-NKQTLESD 1251
Cdd:TIGR01612 1002 fndlkanlgknkENMLYHQFDEKEKATNDieqKIEDANKNIPNIEIAIHTSIYNIIDEIE--KEIGKNIELlNKEILEEA 1079
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1252 NKELTNEVKSLQQAK----------------SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNvsclL 1315
Cdd:TIGR01612 1080 EINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQIND----L 1155
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1316 EDAEKKGIKlTKDVSSLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNNLLEQQEEEEESRKNLEKqlaTLQ 1389
Cdd:TIGR01612 1156 EDVADKAIS-NDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGK---LFL 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1390 AQLVETKKKLEDDVGALEG----LEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDD----LMVDLDHQRQI 1461
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEAyiedLDEIKEK--------SPEIENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI 1300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1462 vSNLEKKQKKFDQMLAEEKTISARYAE-ERDRAEAEAREKDT--------------KALSMARALDEALEAKEEFERLNK 1526
Cdd:TIGR01612 1301 -SDIREKSLKIIEDFSEESDINDIKKElQKNLLDAQKHNSDInlylneianiynilKLNKIKKIIDEVKEYTKEIEENNK 1379
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1527 QLRAEM---EDLISS-KDDVgknvhELEKSKRTLEQQVEEmrTQLEELEDELQATEDAKLRLEVNMqamkaqfDRDLQAR 1602
Cdd:TIGR01612 1380 NIKDELdksEKLIKKiKDDI-----NLEECKSKIESTLDD--KDIDECIKKIKELKNHILSEESNI-------DTYFKNA 1445
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1603 DEQNEEKKrALVKQVremeaELEDERKQRALAVA---AKKKLEMDLKDVEAQIEAANKARDEA---IKQLRKLQAQMKDY 1676
Cdd:TIGR01612 1446 DENNENVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQY 1519
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1677 QRELEE------ARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK 1750
Cdd:TIGR01612 1520 KKDVTEllnkysALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQ 1599
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1751 RRLEA------RIAQLEEELEEEQSNMELLNDRFrkTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1824
Cdd:TIGR01612 1600 LSLENfenkflKISDIKKKINDCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD 1677
|
....*....
gi 688558694 1825 gSVKSKFKA 1833
Cdd:TIGR01612 1678 -ELDSEIEK 1685
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1284 |
3.28e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 859 KVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRarlvaKKQE 938
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 939 leeilhdlesrveeeeernqslqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1018
Cdd:PTZ00121 1631 ------------------------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1019 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAElqaQID 1098
Cdd:PTZ00121 1687 EKKAAE--------ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEE 1755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1099 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRDLSEELEAlkTELE 1175
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiieGGKEGNLVINDSKEMED--SAIK 1833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1176 DTLDTTAAQQElRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1255
Cdd:PTZ00121 1834 EVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDL----KEDDEEEIEEADEIEKIDKDDIEREIPNNNMA 1908
|
410 420
....*....|....*....|....*....
gi 688558694 1256 TNEVKSLQQAKSESEHKRKKLEAQLQEVM 1284
Cdd:PTZ00121 1909 GKNNDIIDDKLDKDEYIKRDAEETREEII 1937
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1036-1212 |
3.36e-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: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1036 EEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVL 1115
Cdd:COG3883 17 QIQAKQKELSELQAELE----AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1116 A-----------------------------RGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1166
Cdd:COG3883 93 RalyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 688558694 1167 LEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQ 1212
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1565-1949 |
4.08e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1565 TQLEELEDELQATEDAKLRLevnmqamkaqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAL--AVAAKKKLE 1642
Cdd:COG4717 71 KELKELEEELKEAEEKEEEY------------AELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1643 MDLKDVEAQIEAAnkarDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ-SKENEKKLKSLEAEILQLQEDLASSERA 1721
Cdd:COG4717 139 AELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1722 RRHAEQERDELADEISNSASGKAALLDEKRRLEARI------------AQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1789
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1790 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1869
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1870 --LKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEASEGLSREVNTLKN 1945
Cdd:COG4717 374 alLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELRE 453
|
....
gi 688558694 1946 RLRR 1949
Cdd:COG4717 454 ELAE 457
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1078-1231 |
4.50e-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: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1078 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAV---LARGDEEVAQKNNALKQLRELQA-------------QLAE 1141
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteLEDLEKEIKRLELEIEEVEARIKkyeeqlgnvrnnkEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1142 LQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHG 1221
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
170
....*....|
gi 688558694 1222 TALEEISEQL 1231
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1085-1681 |
5.37e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1085 DLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLS 1164
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1165 EELEALK--TELEDTLDTTAAQQELRSKRE-QEVAELKKAIDDETR---NHESQIQEMRQRHGTA--LEEISEQLEQAKR 1236
Cdd:PRK01156 267 MELEKNNyyKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKKQilsNIDAEINKYHAIIKKLsvLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1237 VKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSclle 1316
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS---- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1317 daekkgikltKDVSSLESQLQDTQELLQEETRQKLNLSSRIR------QLEEEKNNLLEQQEEEEESRknlekqlatlqa 1390
Cdd:PRK01156 423 ----------SKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSNHIINHYNEKKSR------------ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1391 qLVETKKKLEDDVGAlegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKnrlQQELDDLMVDLdhqrqivSNLEKKQK 1470
Cdd:PRK01156 481 -LEEKIREIEIEVKD---IDEKIVDLKKRKEYLESEEINKSINEYNKIESA---RADLEDIKIKI-------NELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1471 KFDQMLAEEKTISARYAEER----------------DRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1534
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSKrtswlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1535 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQ---LEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEqneekKR 1611
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKIDNYKKQiaeIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR-----LE 701
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1612 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIkqLRK-----LQAQMKDYQRELE 1681
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAM--IRKsasqaMTSLTRKYLFEFN 774
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1477-1740 |
5.51e-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: 57.73 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1477 AEEKTISARYAEERDRaeaeaREKDTKALS-MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1555
Cdd:pfam05667 226 WNSQGLASRLTPEEYR-----KRKRTKLLKrIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1556 L----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQ---NEEKKRALVKQVREMEAELEDER 1628
Cdd:pfam05667 301 ThtekLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLE-DLESSIQElekEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1629 KQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-EEARTSRDEIFTQSKENEKKL---KSL 1704
Cdd:pfam05667 380 EELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLiEEYRALKEAKSNKEDESQRKLeeiKEL 459
|
250 260 270
....*....|....*....|....*....|....*.
gi 688558694 1705 EAEILQLQEDLASSERARRHAEQERDELADEISNSA 1740
Cdd:pfam05667 460 REKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSA 495
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1271-1944 |
6.94e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.93 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1271 HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSslesqlQDTQELLQEETRQK 1350
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1351 LNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE--------VKRKLQKDMEV 1422
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAkynrrrskIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1423 TSQKLE--------EKAIAFDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQMLAEEKTISARyaEERDRA 1493
Cdd:pfam12128 395 IKDKLAkireardrQLAVAEDDLQALESELREQLEAGKLEFnEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1494 EAEAREKDTKAL-SMARALDEALEAKEEFERLNKQLRAEmedlisskddvgknvhelekskrtlEQQVEEMRTQLEELED 1572
Cdd:pfam12128 473 IERAREEQEAANaEVERLQSELRQARKRRDQASEALRQA-------------------------SRRLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1573 ELQA---TEDAKLRLEVNM--QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA-ELEDERKQRALAVAAKKKLEMDLK 1646
Cdd:pfam12128 528 QLFPqagTLLHFLRKEAPDweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1647 DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSrdeiFTQSKENEKKLKS-LEAEILQLQEdlaSSERARRHA 1725
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1726 EQERDELADEISNSASGKAALLDEKRR--LEARIAQLeeeleeeQSNMELLNDRfrktTMQVDTLNTELAGERSAAQKSE 1803
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL----DAQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1804 NArqqLERQNK-DLKSKlqELEGSVKSKFKASIAALEAKIlqleeqleqeakERAAankiVRRTEKKLKEVFMQvEDERR 1882
Cdd:pfam12128 750 KA---LETWYKrDLASL--GVDPDVIAKLKREIRTLERKI------------ERIA----VRRQEVLRYFDWYQ-ETWLQ 807
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1883 HADQYKEQMEKANSRMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLS---REVNTLK 1944
Cdd:pfam12128 808 RRPRLATQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRcemSKLATLK 876
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1332-1884 |
6.98e-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: 57.83 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1332 LESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEE 1411
Cdd:pfam05557 32 LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLAD-------ARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1412 VKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERD 1491
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1492 RAEaearekdtkalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQvEEMRTQLEELE 1571
Cdd:pfam05557 185 DSE------------IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-EKYREEAATLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1572 DELQATEdAKLRLEVNMQAMKAQFDR---DLQARDEQNEEKKRALVKQVREMEAELEDERKQRalavaakKKLEMDLKDV 1648
Cdd:pfam05557 252 LEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR-------RELEQELAQY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1649 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEART---SRDEIFTQSKENEKKLKSLE--AEILQLQEDLASSERARR 1723
Cdd:pfam05557 324 LKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQAHNEEMEAQL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1724 HAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELL--NDRFR--KTTMQVDTLNTELAGERSAA 1799
Cdd:pfam05557 404 SVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLEleRQRLReqKNELEMELERRCLQGDYDPK 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1800 -----QKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK---LK 1871
Cdd:pfam05557 484 ktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKnqrLK 563
|
570
....*....|...
gi 688558694 1872 EVFMQVEDERRHA 1884
Cdd:pfam05557 564 EVFQAKIQEFRDV 576
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1155-1872 |
8.95e-08 |
|
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: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1155 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR-QRHGTAL--EEISEQL 1231
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNaTRHLCNLlkETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1232 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRTHKIQTELDNV 1311
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE------DHEKIQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1312 SCLLEDAEKKgikltkdvsslESQLQDTQELLqEETRQKLNlssrirQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQ 1391
Cdd:pfam05483 243 SLLLIQITEK-----------ENKMKDLTFLL-EESRDKAN------QLEEKTKLQDENLKELIEKKDHLTKELEDIKMS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1392 L---VETKKKLEDDVG-ALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQ----ELDDLMVDLDHQRQIVS 1463
Cdd:pfam05483 305 LqrsMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1464 NLEKKQKKFDQMlaeektisaryAEERDRAEAEAREKDTKALSMARALDEaleaKEEFERLNKQLRAEMEDLISSKDDVG 1543
Cdd:pfam05483 385 ELQKKSSELEEM-----------TKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1544 KNVHELE-------KSKRTLEQQVEEMRTQLE-ELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ--------NE 1607
Cdd:pfam05483 450 KEIHDLEiqltaikTSEEHYLKEVEDLKTELEkEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQediinckkQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1608 EKKRALVKQVREMEAELEDE--------RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE 1679
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDElesvreefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1680 LEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASserARRHAEQERDELADEISNSASGKAALLDEKRRLEARIaq 1759
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA-- 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1760 leeeleeeqsnmellnDRFRKTTMQVDTLNTELAGERSAAQKSENAR--QQLERQNKDL---KSKLQElEGSVKSKFKAS 1834
Cdd:pfam05483 685 ----------------DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydKIIEERDSELglyKNKEQE-QSSAKAALEIE 747
|
730 740 750
....*....|....*....|....*....|....*...
gi 688558694 1835 IAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1872
Cdd:pfam05483 748 LSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
985-1199 |
1.09e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 985 RQKLQlekvTAEAKIK--KMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEErL 1062
Cdd:COG3206 188 RKELE----EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-S 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1063 KKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAkkeEELQAVLARGDEEVAQknnALKQLRELQAQL 1139
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREASLQAQL 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1140 AELQEDLESEKAARNKAEKLKRDlseeLEALKTELEDTLdttAAQQELRSKREQEVAELK 1199
Cdd:COG3206 337 AQLEARLAELPELEAELRRLERE----VEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1340-1583 |
1.19e-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: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1340 QELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1418
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1419 DMEVTSQKLEEKAIAFDKLEktknrlQQELDDLMVDLDHQRQIVSNLEkkqkKFDQMLAEEKTISARYAEERDRAEAEAR 1498
Cdd:COG4942 98 ELEAQKEELAELLRALYRLG------RQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1499 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1578
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 688558694 1579 DAKLR 1583
Cdd:COG4942 248 FAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
906-1128 |
1.33e-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: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 906 EEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDE--EEA 983
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 984 ARQKLQLEKVTAEA-KIKKMEEDILLLEDQN-SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEER 1061
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1062 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAVLARGDEEVAQKNNA 1128
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
865-1430 |
1.36e-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: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 865 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELE 940
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 941 EILHDLESRVEEEEernQSLQNEKKKMQSHiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1020
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKN--------------EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1021 KLLedrvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERlkkeektrqelEKAKRKLDAETTDLQDQIAELQAQIDEL 1100
Cdd:pfam05483 412 KIL----AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR-----------EKEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1101 KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldt 1180
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE----- 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1181 tAAQQELRSKREqevaELKKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVK 1260
Cdd:pfam05483 552 -SVREEFIQKGD----EVKCKLDKSEENARSIEYEVLKKE-KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1261 SLQQAKSESEHKRKKLEAQLQEVMARFsegekvkGELADRTHK-IQTELDNVSCLLEDAEK------KGIKLTKDVsSLE 1333
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKF-------EEIIDNYQKeIEDKKISEEKLLEEVEKakaiadEAVKLQKEI-DKR 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1334 SQlQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDvgaleglEEVK 1413
Cdd:pfam05483 698 CQ-HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIE-------KEEK 769
|
570
....*....|....*..
gi 688558694 1414 RKLQKDMEVTSQKLEEK 1430
Cdd:pfam05483 770 EKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1597-1808 |
1.42e-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: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1597 RDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1676
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1677 QRELEEA-RTSRDEIFTQSKENEKKLKSLE----------AEILQLQEDLASSERARRHAEQERDELADEISNSASGKAA 1745
Cdd:COG4942 110 LRALYRLgRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558694 1746 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQ 1808
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
997-1419 |
1.50e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 997 AKIKKMEEDILLLEDQNSKF---LKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM---------MVDLEERLKK 1064
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1065 EEKTRQELEKAKRKLDAettdLQDQIAELQAQIDELKIQL-AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1143
Cdd:COG4717 151 LEERLEELRELEEELEE----LEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1144 EDLESEKAARNKAEKLKRDLSEE-----------LEALKTELEDTLDTTAA------------QQELRSKREQEVAELKK 1200
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1201 AIDDETRN--HESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELtnEVKSLQQAKSESEHKRK-KLE 1277
Cdd:COG4717 307 LQALPALEelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGvEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1278 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLNLSSRI 1357
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1358 RQLEEEKNNLleqqeeeeesrkNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1419
Cdd:COG4717 463 EQLEEDGELA------------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1059-1269 |
1.58e-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: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1059 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRE-LQA 1137
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREeLGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1138 QLAELQED----------LESE----------------KAARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQELRSKR 1191
Cdd:COG3883 91 RARALYRSggsvsyldvlLGSEsfsdfldrlsalskiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1192 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1269
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1523-1949 |
1.72e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1523 RLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnmqamkAQFDRDLQAR 1602
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1603 DEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV----EAQIEAANKARDEAIKQLRKLQAQMKDYQR 1678
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1679 ELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL-----DEKRRL 1753
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLflllaREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1754 EARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKskLQELEGSVKSKFKA 1833
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1834 SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVfmqvedERRHADQYKEQMEKansRMKQLKRQLEEAEEEAT 1913
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL------EELLEALDEEELEE---ELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 688558694 1914 RANASRRKLQRELDDATEASE--GLSREVNTLKNRLRR 1949
Cdd:COG4717 450 ELREELAELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1298-1534 |
1.77e-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: 55.54 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1298 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeees 1377
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1378 rKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH 1457
Cdd:COG4942 86 -AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA---LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1458 QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1534
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
961-1714 |
2.41e-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: 56.21 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 961 QNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQ-NSKFLKEKKLLEDRVGEMTSQLaEEEE 1039
Cdd:TIGR01612 532 QNIKAKLYKEIEAGLKESYELAKNWKKLIHE---IKKELEEENEDSIHLEKEiKDLFDKYLEIDDEIIYINKLKL-ELKE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1040 KAKNLGKvKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI-AELQAQIDEL-KIQLAKKEEELQAVLAR 1117
Cdd:TIGR01612 608 KIKNISD-KNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIySTIKSELSKIyEDDIDALYNELSSIVKE 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1118 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELEDTLDTTAaqQELRSKR 1191
Cdd:TIGR01612 687 NAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVElhlsniENKKNELLDIIVEIKKHIHGEINKDLNKIL--EDFKNKE 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1192 EQEVAELK--KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRvkgNLEKNKQTL------ESDNKELTNEVKSLQ 1263
Cdd:TIGR01612 765 KELSNKINdyAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQ---NYDKSKEYIktisikEDEIFKIINEMKFMK 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1264 QAKSESEHKRKKLEAQLQEVM----ARFSE-GEKVKGELADR-------------------THKIQTELDNVSCLLEDAE 1319
Cdd:TIGR01612 842 DDFLNKVDKFINFENNCKEKIdsehEQFAElTNKIKAEISDDklndyekkfndskslineiNKSIEEEYQNINTLKKVDE 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1320 KkgIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKl 1399
Cdd:TIGR01612 922 Y--IKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIE--KSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNN- 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1400 eddvGALEGLEEVKRKLQKDMEVTSQKleekaiAFDKLEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEE 1479
Cdd:TIGR01612 997 ----ELIKYFNDLKANLGKNKENMLYH------QFDEKEKATNDIEQKIEDA-------NKNIPNIEIAIHTSIYNIIDE 1059
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1480 ktISARYAEERDRAEAEAREKDTKALSMARALDEALE-------AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKS 1552
Cdd:TIGR01612 1060 --IEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKhynfddfGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1553 KRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFDRDLQARDEQNEekkraLVKQVREMEAELEDERK 1629
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEE 1211
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1630 QRALAVA---------------AKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMkDYQRELEEARTSRDEI---F 1691
Cdd:TIGR01612 1212 VKGINLSygknlgklflekideEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEMETFNISHDDDkdhH 1290
|
810 820
....*....|....*....|...
gi 688558694 1692 TQSKENEKKLKSLEAEILQLQED 1714
Cdd:TIGR01612 1291 IISKKHDENISDIREKSLKIIED 1313
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1539-1759 |
3.02e-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: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1539 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVR 1618
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAK-LLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1619 EMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIK-------QLRKLQAQMKDYQREL-EEARTSRD 1688
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688558694 1689 EIFTQSKENEKKLKSLEAEILQLQEDLAS-SERARRHAEQERD-ELADEISNSasgkaaLLdeKRRLEARIAQ 1759
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1110-1282 |
3.28e-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: 53.39 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1110 ELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtlDTTAAQQELRS 1189
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1190 KREQEvaelkkAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1269
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|...
gi 688558694 1270 EHKRKKLEAQLQE 1282
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1389-1607 |
3.69e-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: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1389 QAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1468
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1469 QKKFDQMLAEEKTI--SARYAEERDRAEAEAREKDtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknv 1546
Cdd:COG3883 95 LYRSGGSVSYLDVLlgSESFSDFLDRLSALSKIAD----ADADLLEELKADKAELEAKKAELEAKLAELEALKA------ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558694 1547 hELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNE 1607
Cdd:COG3883 165 -ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1055-1932 |
4.30e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1055 MVDLEERLKKEEKT---RQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlakkEEELQAVLARgdeeVAQKNNAL-- 1129
Cdd:PRK04863 275 MRHANERRVHLEEAlelRRELYTSRRQLAAEQYRLVEMARELAELNEAESDL----EQDYQAASDH----LNLVQTALrq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1130 -KQLRELQAQLAELQEDLESEKAARNKAeklkRDLSEELEALKTELEDTLDTTAAQqelrskreqeVAELKKAID-DETR 1207
Cdd:PRK04863 347 qEKIERYQADLEELEERLEEQNEVVEEA----DEQQEENEARAEAAEEEVDELKSQ----------LADYQQALDvQQTR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1208 NheSQIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarf 1287
Cdd:PRK04863 413 A--IQYQQAVQ----ALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV---- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1288 segekvkgeladrtHKIQTELDNvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEKN 1365
Cdd:PRK04863 483 --------------RKIAGEVSR-----SEAWDVARELLRRLREQRHLAEQLQQLRMRlsELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1366 NLLEQQEeeeesrkNLEKQLATLQAQLVEtkkkleddvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK---- 1441
Cdd:PRK04863 544 KRLGKNL-------DDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawl 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1442 ------NRLQ----------QELDDLMVD-LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKA 1504
Cdd:PRK04863 607 aaqdalARLReqsgeefedsQDVTEYMQQlLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1505 LSMARAlDEALEAKEEFERLNKQLR---------------AEMEDL----------ISSKDDVGKNVHELEK------SK 1553
Cdd:PRK04863 687 LSEIYD-DVSLEDAPYFSALYGPARhaivvpdlsdaaeqlAGLEDCpedlyliegdPDSFDDSVFSVEELEKavvvkiAD 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1554 RTL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDLQ-----ARDEQNEEKKR 1611
Cdd:PRK04863 766 RQWrysrfpevplfgraarEKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELR 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1612 ALVKQVREMEAELED----ERKQRALAVAAKKKL--------EMDLKDVEAQIEAANKARDEaIKQLRKLQAQMKDYQRE 1679
Cdd:PRK04863 841 QLNRRRVELERALADhesqEQQQRSQLEQAKEGLsalnrllpRLNLLADETLADRVEEIREQ-LDEAEEAKRFVQQHGNA 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1680 LEeartsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAllDEKRRLEARIAq 1759
Cdd:PRK04863 920 LA-----------QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAKNSD- 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1760 leeeleeeqsnmelLNDRFRkttmqvdtlntelagersaaQKSENARQQLERQNKDLKSKLQELegsvkSKFKASIAALE 1839
Cdd:PRK04863 986 --------------LNEKLR--------------------QRLEQAEQERTRAREQLRQAQAQL-----AQYNQVLASLK 1026
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1840 AkilqleeqleqeakERAAANKIVRRTEKKLKEVFMQVEDE-----RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR 1914
Cdd:PRK04863 1027 S--------------SYDAKRQMLQELKQELQDLGVPADSGaeeraRARRDELHARLSANRSRRNQLEKQLTFCEAEMDN 1092
|
970
....*....|....*...
gi 688558694 1915 ANASRRKLQRELDDATEA 1932
Cdd:PRK04863 1093 LTKKLRKLERDYHEMREQ 1110
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1201-1443 |
4.36e-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: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1201 AIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQL 1280
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1281 QEVMARFsegEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1360
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1361 EEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKT 1440
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 688558694 1441 KNR 1443
Cdd:COG4942 250 ALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1466-1949 |
4.48e-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: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1466 EKKQKKFDQMLAEEKTISARYAEERDRAEA----EAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDD 1541
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1542 VGKNVHELEKSKRTLEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRAL 1613
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1614 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1693
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1694 SKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1766
Cdd:TIGR02169 415 LQRLseeladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1767 EQSNMELLNDRFRKTTMQVDTLNTEL------------------------AGERSAAQKSEN------ARQQLERQN--- 1813
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgeryataievaAGNRLNNVVVEDdavakeAIELLKRRKagr 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1814 ------KDLKSKLQELE--------------------------------------------------------------- 1824
Cdd:TIGR02169 575 atflplNKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtlegelfeksga 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1825 ---GSVKSKFKASIAA-LEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQ 1900
Cdd:TIGR02169 655 mtgGSRAPRGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1901 LKRQLEEAEEE-------ATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1949
Cdd:TIGR02169 735 LKERLEELEEDlssleqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
870-1396 |
4.68e-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: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 870 EEEMQAKDEELIKVKERQVKVENELVEMER-KHQQLLEEKNILAEQLQAETELFAeaeemrarlVAKKQELEEILHDLES 948
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQnKNHINNELESKEEQLSSYEDKLFD---------VCGSQDEESDLERLKE 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 949 RVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVG 1028
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRD 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1029 EMTS----QLAEEEEKAKNLGKVKNKQEMMMVD-------LEERLKKEEKTRQELEKAK---------RKLDAETTDLQD 1088
Cdd:TIGR00606 727 EMLGlapgRQSIIDLKEKEIPELRNKLQKVNRDiqrlkndIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDVER 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1089 QIAELQAQID---------ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQedleSEKAARNKAEKL 1159
Cdd:TIGR00606 807 KIAQQAAKLQgsdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK----SEKLQIGTNLQR 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1160 KRDLSEELEALKTELEDTLdttaaqQELRSKREQEVAELKKAIDDETRNHE--SQIQEMRQRHGTALEEISEQLEQAKRV 1237
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLI------REIKDAKEQDSPLETFLEKDQQEKEEliSSKETSNKKAQDKVNDIKEKVKNIHGY 956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1238 KGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSegekvkgeladrTHKIQTELDNVSCLLE 1316
Cdd:TIGR00606 957 MKDIENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID------------TQKIQERWLQDNLTLR 1024
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1317 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETK 1396
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKL--EENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1358-1947 |
4.71e-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: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1358 RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKL 1437
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV---HEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1438 EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDR-AEAEAREKDTKALSMARALD---- 1512
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmSTMHFRSLGSAISKILRELDteis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1513 -------------EAL--EAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTleqQVEEMRTQLEELEDELQAT 1577
Cdd:pfam15921 235 ylkgrifpvedqlEALksESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARS---QANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1578 EDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELE----------------DERKQRALAVAAKKKL 1641
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTearterdqfsqesgnlDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1642 EMDLKDVEAQ------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAE-- 1707
Cdd:pfam15921 392 ELSLEKEQNKrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQle 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1708 -----ILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNmellNDRFRKTT 1782
Cdd:pfam15921 472 stkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQ 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1783 MQVDTLNTELAGERSAA----QKSENARQ-----------------QLERQNKDLKSKLQELEgSVKSKFKASIAALEAK 1841
Cdd:pfam15921 548 TECEALKLQMAEKDKVIeilrQQIENMTQlvgqhgrtagamqvekaQLEKEINDRRLELQEFK-ILKDKKDAKIRELEAR 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1842 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQME--KANSRMK---------QLKRQLEEAEE 1910
Cdd:pfam15921 627 VSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKseemetttnKLKMQLKSAQS 706
|
650 660 670
....*....|....*....|....*....|....*..
gi 688558694 1911 EATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1947
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI 743
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1330-1754 |
4.86e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1330 SSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEkQLATLQAQLVETKKKLEDDVGALEG 1408
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1409 LEEVKRKLQKDMEVTSQ---------KLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkfDQMLAEE 1479
Cdd:COG4717 124 LLQLLPLYQELEALEAElaelperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1480 KTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR-----AEMEDLISSKDDVGKNVHE------ 1548
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaAALLALLGLGGSLLSLILTiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1549 ------------LEKSKRTLEQQVEEMR--TQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDL-----QARDEQNEEK 1609
Cdd:COG4717 281 lvlgllallfllLAREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1610 KRALVKQVREMEAEL--------EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRK--LQAQMKDYQRE 1679
Cdd:COG4717 361 EELQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1680 LEEARTSRDEIftqskenEKKLKSLEAEILQLQED--LASSERARRHAEQERDELADEISNSASGKAALLDEKRRLE 1754
Cdd:COG4717 441 LEELEEELEEL-------REELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
947-1158 |
5.19e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 947 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIlllEDQNSKFLKEKKLLEDR 1026
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1027 VGEM-----TSQLAEEEEKAKNLGKVKNKQEMMMVDLE---ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1098
Cdd:COG3883 92 ARALyrsggSVSYLDVLLGSESFSDFLDRLSALSKIADadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1099 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1158
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1039-1171 |
6.74e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.45 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1039 EKAK-NLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLakkEEELQAVLAR 1117
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1118 GDEEVAQknnALKQLRELQAQLA------ELQEDLESEKAARNKAEKLKRDLSEELEALK 1171
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYasvkahELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1383-1949 |
7.36e-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: 54.46 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1383 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEekaiafDKLEKTKNRLQQELDDLMVDLDHQRQIV 1462
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1463 SNLEKKQKKFDQMLAEEKtisARYAEERD--RAEAEAREKDTKALsmaraLDEALEAKEEFERLnKQLRAEmedliSSKD 1540
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKAL-----TGKHQDVTAKYNRR-RSKIKE-----QNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1541 DVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlEVNMQamkaqfdrdlQARDEQNEEKKRALVKQVREM 1620
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL-EFNEE----------EYRLKSRLGELKLRLNQATAT 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1621 EAELEDERKQRALAVAAKKKLEMDLKDVE-AQIE--AANKARDEAIKQLRKLQAQMKDYQRELEEARTsrdEIFTQSKEN 1697
Cdd:pfam12128 460 PELLLQLENFDERIERAREEQEAANAEVErLQSElrQARKRRDQASEALRQASRRLEERQSALDELEL---QLFPQAGTL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1698 EKKLKSLEAEILQLQEDLASSE---RARRHAEQERDELADEISNSASGkaalLDEKR-----------RLEARIAQLEEE 1763
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPEllhRTDLDPEVWDGSVGGELNLYGVK----LDLKRidvpewaaseeELRERLDKAEEA 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1764 LEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKiL 1843
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ-L 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1844 QLEEQLEQEAKERAAANKIVRRTEK--KLKEVfmqVEDERRHADQYKEQMEKANSrmkQLKRQLEEAEEEATRANASRrk 1921
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKqaYWQVV---EGALDAQLALLKAAIAARRS---GAKAELKALETWYKRDLASL-- 763
|
570 580
....*....|....*....|....*...
gi 688558694 1922 lqrelDDATEASEGLSREVNTLKNRLRR 1949
Cdd:pfam12128 764 -----GVDPDVIAKLKREIRTLERKIER 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
985-1141 |
9.47e-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: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 985 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknLGKVKNKQEMmmvdleERLKK 1064
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEY------EALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1065 EEKTrqeLEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1141
Cdd:COG1579 97 EIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1262-1927 |
9.78e-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: 53.96 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1262 LQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADrthKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQE 1341
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE---EIQENKDLIK--ENNATRHLCNLLKETCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1342 LLQEETRQ-KLNLSSRIrqleeEKNNLLEQQEEEEESRKNLEKQLatlqaqlvetkkKLEDDVGALEGLEEVKRKLQKDm 1420
Cdd:pfam05483 176 YEREETRQvYMDLNNNI-----EKMILAFEELRVQAENARLEMHF------------KLKEDHEKIQHLEEEYKKEIND- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1421 evtsqklEEKAIAFDKLEKTKNrlQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEARek 1500
Cdd:pfam05483 238 -------KEKQVSLLLIQITEK--ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1501 dtKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAted 1579
Cdd:pfam05483 307 --RSMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI--- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1580 aklrlevnmqamkaqFDRDLQARDEQNEEkkraLVKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKAR 1659
Cdd:pfam05483 382 ---------------ITMELQKKSSELEE----MTKFKNNKEVELEELKK----ILAEDEKLLDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1660 DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNS 1739
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1740 ASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1819
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1820 LQELEGSVKSKFKasiaaleaKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMK 1899
Cdd:pfam05483 596 CNNLKKQIENKNK--------NIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
650 660
....*....|....*....|....*...
gi 688558694 1900 QLKRQLEEAEEEATRANASRRKLQRELD 1927
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1526-1742 |
9.91e-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: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1526 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdlQARDEQ 1605
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1606 NEEKKR-------------ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQ 1672
Cdd:COG3883 97 RSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1673 MKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1742
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1649-1872 |
1.07e-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: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1649 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLasserarrhaEQE 1728
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1729 RDELADEI------SNSASGKAALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAqks 1802
Cdd:COG3883 85 REELGERAralyrsGGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1803 ENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1872
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
813-1275 |
1.23e-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: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 813 QSVCRGYLARkafAKKQQQLSALKVLQRNCAAY-----LKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVKErq 887
Cdd:TIGR00618 419 FRDLQGQLAH---AKKQQELQQRYAELCAAAITctaqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL-- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 888 vKVENELVEMER---KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEK 964
Cdd:TIGR00618 494 -ARLLELQEEPCplcGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 965 KKMQSHIQDLEEQLDEEEAARQKLQLE-KVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1043
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLtEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1044 LGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAKKEEELQAVLARGDE 1120
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEmlaQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1121 EVAQKNNALKQ-LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1199
Cdd:TIGR00618 733 DLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1200 KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKK 1275
Cdd:TIGR00618 813 PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----QLTQEQAKIIQLSDKLNGINQI 884
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
870-1359 |
1.29e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 870 EEEMQAKDEELIKVKErqvkvenELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVA---KKQELEEILHDL 946
Cdd:PRK01156 189 EEKLKSSNLELENIKK-------QIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSledMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 947 ESRVEEEEERN---QSLQNEKKKMQS--------HIQDLEEQLDEEEAARQKLQ---LEKVTAEAKIKKMEEdillLEDQ 1012
Cdd:PRK01156 262 ESDLSMELEKNnyyKELEERHMKIINdpvyknrnYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1013 NSKFLKEKKLLEDRVGEMT----------SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAE 1082
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1083 TTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG----------------------------DEEVAQKNNALKQLRE 1134
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhiinhynekksrlEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1135 LQAQLAELQEDLESEKAARNKAEKLKrdlseeLEALKTELEDTLDTTAAQQELRSKREQEVAELKKA-IDDETRNHESQI 1213
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1214 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN-----------KELTNEVKSLQQAKSESEHKRKKLEA---- 1278
Cdd:PRK01156 572 NALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFpddksyidksiREIENEANNLNNKYNEIQENKILIEKlrgk 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1279 --QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDA-------EKKGIKLTKDVSSLESQLQDTQELLQ--EET 1347
Cdd:PRK01156 652 idNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTIEILRTRINELSDRINDINETLEsmKKI 731
|
570
....*....|..
gi 688558694 1348 RQKLNLSSRIRQ 1359
Cdd:PRK01156 732 KKAIGDLKRLRE 743
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1255-1637 |
1.35e-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: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1255 LTNEVKSLQQAKSESEhkrkKLEAQLQEVMArfsEGEKVKGELADRTHKIQT---ELDNVSCLLEDAEKKGIKLTKDVSS 1331
Cdd:pfam19220 36 IEAILRELPQAKSRLL----ELEALLAQERA---AYGKLRRELAGLTRRLSAaegELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1332 LESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeeesRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE 1411
Cdd:pfam19220 109 LRIELRDKTAQAEALERQLAAETEQNRALEEE--------------NKALREEAQAAEKALQRAEGELATARERLALLEQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1412 VKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERD 1491
Cdd:pfam19220 175 ENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQ-----------------AERERAEAQLEEAVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1492 RAEAEARekdtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE 1571
Cdd:pfam19220 238 AHRAERA-------SLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1572 DELQATEDAKLRLEVNMQAM-KAQFDRD------------LQARDEQ----NEEKKRALVKQVREMEAELEDERKQRALA 1634
Cdd:pfam19220 311 QQFQEMQRARAELEERAEMLtKALAAKDaaleraeeriasLSDRIAEltkrFEVERAALEQANRRLKEELQRERAERALA 390
|
...
gi 688558694 1635 VAA 1637
Cdd:pfam19220 391 QGA 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1435-1648 |
1.63e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1435 DKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1498
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1499 EKDTKALSMARALDEALEAKEEFERLNKQLR---------AEMEDLISSKDDVGKnvhelekskrtLEQQVEEMRTQLEE 1569
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITK-----------IKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1570 LEDELQatEDAKLRLEVNMQAMKAqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1648
Cdd:PHA02562 318 LDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1419-1638 |
1.70e-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: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1419 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEA 1497
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1498 REKDT----KALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1573
Cdd:COG3883 97 RSGGSvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1574 LQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1638
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
998-1206 |
1.80e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.01 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 998 KIKKMEEDILL-LEDQNSKFLKE-------------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK--------QEMMM 1055
Cdd:PRK05771 2 APVRMKKVLIVtLKSYKDEVLEAlhelgvvhiedlkEELSNERLRKLRSLLTKLSEALDKLRSYLPKlnplreekKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1056 VDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK------------------------IQLAKKEEEL 1111
Cdd:PRK05771 82 KSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfkyvsvfvgtVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1112 QAVLARGDEEVAQKNN---------------ALKQLRELQAQLAELQEDLESEKAARNKAEKLKR------DLSEELEAL 1170
Cdd:PRK05771 162 LESDVENVEYISTDKGyvyvvvvvlkelsdeVEEELKKLGFERLELEEEGTPSELIREIKEELEEiekereSLLEELKEL 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 688558694 1171 KTELEDTLdtTAAQQELRSKREQEVAELKKAIDDET 1206
Cdd:PRK05771 242 AKKYLEEL--LALYEYLEIELERAEALSKFLKTDKT 275
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
869-1092 |
2.17e-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: 52.07 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 869 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELEEILH 944
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 945 DLESRVEEEEERNQSLQneKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE--AKIKKMEEDILLLEDQNSKFLKEKKL 1022
Cdd:COG4942 98 ELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArrEQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1023 LEdrvgemtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1092
Cdd:COG4942 176 LE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1111-1340 |
2.58e-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: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1111 LQAVLARGDEEVAQKNNALKQLRE----LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQE 1186
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA------EAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1187 LRSKREQevaeLKKaiddetRNHESQIQEMRQRHGTAL---EEISEQLEQAKRVKGNLEKNKQTLE---SDNKELTNEVK 1260
Cdd:COG3883 81 IEERREE----LGE------RARALYRSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADADLLEelkADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1261 SLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1340
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1058-1626 |
3.16e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.50 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1058 LEERLKKEEKTRQELEKAKRKLDAETT-------DLQDQIAELQAQIDELKIQLAKKE--EELQAVLARGDEEVAQKNNA 1128
Cdd:PRK10246 299 IQEQSAALAHTRQQIEEVNTRLQSTMAlrarirhHAAKQSAELQAQQQSLNTWLAEHDrfRQWNNELAGWRAQFSQQTSD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1129 LKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE---LEDTLDTTAAQQELRSKREQEVAELKKAIDDE 1205
Cdd:PRK10246 379 REQLRQWQQQLTHAEQKLNALPAI---TLTLTADEVAAALAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1206 TRNHESQIQEMRQRHGTALEEISEQ---LEQAKRVKgNLEKNKQTLESDNK-----ELTNEVKSLQQAKSESEHKRKkLE 1277
Cdd:PRK10246 456 QTQRNAALNEMRQRYKEKTQQLADVktiCEQEARIK-DLEAQRAQLQAGQPcplcgSTSHPAVEAYQALEPGVNQSR-LD 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1278 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELL-----QEETRQKLN 1352
Cdd:PRK10246 534 ALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldaQEEHERQLR 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1353 LSSRIRQLEEEKNNLleqqeeeeesrknlEKQLATLQAQLVETKKKLEDDVGAL------EGLEEvkrKLQKDMEVTSQK 1426
Cdd:PRK10246 614 LLSQRHELQGQIAAH--------------NQQIIQYQQQIEQRQQQLLTALAGYaltlpqEDEEA---SWLATRQQEAQS 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1427 LEEKAIAFDKLEKTKNRLQQELDDL--MVDLDHQRQIVSnLEKKQKKFDQML---AEEKTISARYAEERDRAeAEAREKD 1501
Cdd:PRK10246 677 WQQRQNELTALQNRIQQLTPLLETLpqSDDLPHSEETVA-LDNWRQVHEQCLslhSQLQTLQQQDVLEAQRL-QKAQAQF 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1502 TKALSMARALDealeaKEEFerlnkqLRAEMEDlisskddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA----- 1576
Cdd:PRK10246 755 DTALQASVFDD-----QQAF------LAALLDE---------ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQhqqhr 814
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1577 ------TEDAKlRLEVNMQAMKAQFdRDLQAR----------DEQNEEKKRALVKQVREMEAELED 1626
Cdd:PRK10246 815 pdgldlTVTVE-QIQQELAQLAQQL-RENTTRqgeirqqlkqDADNRQQQQALMQQIAQATQQVED 878
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
1057-1170 |
3.44e-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: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1057 DLEERLK--KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL----------------------- 1111
Cdd:pfam14362 107 EIDRELLeiQQEEADAAKAQLAAAYRARLAELEAQIAALDAEIDAAEARLDALQAEArceldgtpgtgtgvpgdgpvakt 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558694 1112 -QAVLARGDEEVAQ-KNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1170
Cdd:pfam14362 187 kQAQLDAAQAELAAlQAQNDARLAALRAELARLTAERAAARARSQAAIDGDDGLLARLEAL 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1702-1946 |
3.54e-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: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1702 KSLEAEILQLQEDLASSERARRHAEQERDeladeisnsasgKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1781
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDARE------------QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1782 tmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEeqleqeaKERAAANK 1861
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE-------RELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1862 IVRRTEKKLKEVFMQVEDErrhADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDateasegLSREVN 1941
Cdd:COG4913 360 RRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 688558694 1942 TLKNR 1946
Cdd:COG4913 430 SLERR 434
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1054-1435 |
3.88e-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: 51.82 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1054 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLR 1133
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1134 ELQAQLAELQEDLESekaarnkaeklkrdLSEELEALKTELEDTLDTtaAQQELRSKREQEvaELKKAIDDETRNHESQI 1213
Cdd:pfam07888 126 AHEARIRELEEDIKT--------------LTQRVLERETELERMKER--AKKAGAQRKEEE--AERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1214 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTL------ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1287
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1288 SEGE-----------KVKGELADRTHKIQTELDNVS----CLLEDAEKKGIKLTKdvssLESQLQDTQELLQEETRQKLN 1352
Cdd:pfam07888 268 DRTQaelhqarlqaaQLTLQLADASLALREGRARWAqereTLQQSAEADKDRIEK----LSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1353 LSSrirQLEEEKnnlLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKdmeVTSQKLEEKAI 1432
Cdd:pfam07888 344 LEV---ELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET---VADAKWSEAAL 414
|
...
gi 688558694 1433 AFD 1435
Cdd:pfam07888 415 TST 417
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1548-1724 |
4.01e-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: 50.31 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1548 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDlqaRDEQNEEKKralVKQVREMEAELEDE 1627
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRN---NKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1628 RKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAqmkdyqrELEEARTSRDEIFTQSKENEKKLKSLEAE 1707
Cdd:COG1579 102 KRRIS-------DLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|....*....
gi 688558694 1708 ILQL--QEDLASSERARRH 1724
Cdd:COG1579 168 LAAKipPELLALYERIRKR 186
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1448-1826 |
4.27e-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: 52.05 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1448 LDDLMVDLDHQRQIvsNLEKKQKKFDQMlaeektisaryAEERDRAEaeaREKDTKALSMARALDEALEAKEEFERLNKQ 1527
Cdd:pfam17380 271 LNQLLHIVQHQKAV--SERQQQEKFEKM-----------EQERLRQE---KEEKAREVERRRKLEEAEKARQAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1528 LRAEMEDLisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlevnmqamkaQFDRDLQARDEQNE 1607
Cdd:pfam17380 335 IYAEQERM------------AMERERELERIRQEERKRELERIRQEEIAMEISRMR----------ELERLQMERQQKNE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1608 ekkralvkQVREmeaELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1687
Cdd:pfam17380 393 --------RVRQ---ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1688 DEIFTQsKENEKKLKSLEAEILQLQEDLASSERaRRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEE 1767
Cdd:pfam17380 462 VERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1768 QSNMELLNDRFRKTTMQVDTLNTElagERSAAQKSENARQQLeRQNKDLKSKLQELEGS 1826
Cdd:pfam17380 540 EERRKQQEMEERRRIQEQMRKATE---ERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1712-1950 |
4.68e-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: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1712 QEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTE 1791
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1792 LAGERSAAQKSENARQQLERQNKdLKSKLQeleGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLK 1871
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1872 EVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRRG 1950
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1090-1329 |
4.95e-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: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1090 IAELQAQIDELKIQLAKKEEELQAvlaRGDEEVAQKNNA-LKQlrELQAQLAEL---QEDLES-EKAARNKAEKLKRD-L 1163
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNA---LADKERAEADRQrLEQ--EKQQQLAAIsgsQSQLEStDQNALETNGQAQRDaI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1164 SEELEALKTELE------DTLDTTAAQQELRSK--REQEVAELKKAID---DETRNHES-QIQEMRQRHGTALEEISEQL 1231
Cdd:NF012221 1612 LEESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQeqlDDAKKISGkQLADAKQRHVDNQQKVKDAV 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1232 EQAKRVKGNLEKNKQTLESDnkeltnevksLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1311
Cdd:NF012221 1692 AKSEAGVAQGEQNQANAEQD----------IDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENK 1761
|
250
....*....|....*...
gi 688558694 1312 SCLLEdAEKKGIKLTKDV 1329
Cdd:NF012221 1762 ANQAQ-ADAKGAKQDESD 1778
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
991-1500 |
5.18e-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: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 991 EKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQ 1070
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK----------YLEALNKKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1071 ELEKAKRKLDAettdLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE------ 1144
Cdd:pfam05557 98 QLADAREVISC----LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrik 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1145 -----------------DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETR 1207
Cdd:pfam05557 174 elefeiqsqeqdseivkNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1208 NH--ESQIQE---MRQRHGTAL---EEISEQLEQakrvkgnLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1279
Cdd:pfam05557 254 KEklEQELQSwvkLAQDTGLNLrspEDLSRRIEQ-------LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1280 LQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLED------AEKKGIKLTKDVSSLESQLQDTQ-----------EL 1342
Cdd:pfam05557 327 IEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydkeltMSNYSPQLLERIEEAEDMTQKMQahneemeaqlsVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1343 LQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR-KNLEKQLATLQAQLvetkKKLEDDVGALEgLEEVKRKLQKDME 1421
Cdd:pfam05557 407 EEELGGYKQQAQTLERELQALRQQESLADPSYSKEEvDSLRRKLETLELER----QRLREQKNELE-MELERRCLQGDYD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1422 VTSQK---LEEKAIAfdkleKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERdRAEAEAR 1498
Cdd:pfam05557 482 PKKTKvlhLSMNPAA-----EAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL-RKELESA 555
|
..
gi 688558694 1499 EK 1500
Cdd:pfam05557 556 EL 557
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
903-1361 |
6.52e-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: 51.28 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 903 QLLEEKNILaEQLQAETELfAEAEEMRARLvakkqELEEILHDLESRVEEEEERNQSLQNEKKKMQshiQDLEEQLDEEE 982
Cdd:pfam05557 3 ELIESKARL-SQLQNEKKQ-MELEHKRARI-----ELEKKASALKRQLDRESDRNQELQKRIRLLE---KREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 983 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMmmvdLEERL 1062
Cdd:pfam05557 73 EQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL----LKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1063 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEE-----ELQAVLARGDEEVAQKNNALKQLRELQA 1137
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSElaripELEKELERLREHNKHLNENIENKLLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1138 QLAELQEDLESEKAARNKAEKL---KRDLSEELEALKTELEDTLDTTAAQQELRSK------REQEVAELKKAIDDETRN 1208
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLeleKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqREIVLKEENSSLTSSARQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1209 HESQIQEMRQRHGTALEEISE---QLEQAKRVKGNLEKN-----------KQTLESDNKELTNEVKSLQQAK--SESEHK 1272
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDlnkKLKRHKALVRRLQRRvllltkerdgyRAILESYDKELTMSNYSPQLLEriEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1273 RKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLN 1352
Cdd:pfam05557 389 TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNE 466
|
....*....
gi 688558694 1353 LSSRIRQLE 1361
Cdd:pfam05557 467 LEMELERRC 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1501-1745 |
7.03e-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: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1501 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL------ 1574
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1575 -QATEDAKLRLEV------------NMQAMKAQFDRDLQARDEQNEEKKralvkQVREMEAELEDERKQralAVAAKKKL 1641
Cdd:COG3883 95 lYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKA-----ELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1642 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1721
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260
....*....|....*....|....
gi 688558694 1722 RRHAEQERDELADEISNSASGKAA 1745
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1037-1171 |
8.31e-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: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1037 EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL--KIQLAKKEEELQav 1114
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLerELSEARSEERRE-- 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558694 1115 lARGDEEVAQKNNALKQLR----ELQAQLAELQEDLESEKAARNKaeklkrDLSEELEALK 1171
Cdd:COG2433 461 -IRKDREISRLDREIERLEreleEERERIEELKRKLERLKELWKL------EHSGELVPVK 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
883-1179 |
9.19e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 883 VKERQVKVEnelvEMERKHQQLLEEKNILAEQLQAETELfAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQN 962
Cdd:PRK02224 470 IEEDRERVE----ELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 963 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIllledqnskflkekklleDRVGEMTSQLAEEEEKAK 1042
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI------------------ESLERIRTLLAAIADAED 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1043 NLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDlqDQIAELQAQIDELKIQLAKKEEELQAVLARGDE-- 1120
Cdd:PRK02224 607 EIERLREKRE----ALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDlq 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1121 -EVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLK---RDLSEEL-----EALKTELEDTLD 1179
Cdd:PRK02224 681 aEIGAVENELEELEELRERREALENRVEALEALYDEAEELEsmyGDLRAELrqrnvETLERMLNETFD 748
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
916-1154 |
9.62e-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: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 916 QAETELFAEAEEMRArLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTA 995
Cdd:COG3883 13 FADPQIQAKQKELSE-LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 996 EAKIKKMEE-------------------DILLLEDQNSKFLKEKKLLeDRVGEMTSQLAEEEEKAKNlgKVKNKQEmmmv 1056
Cdd:COG3883 78 EAEIEERREelgeraralyrsggsvsylDVLLGSESFSDFLDRLSAL-SKIADADADLLEELKADKA--ELEAKKA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1057 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQ 1136
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|....*...
gi 688558694 1137 AQLAELQEDLESEKAARN 1154
Cdd:COG3883 231 AAAAAAAAAAAAAASAAG 248
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1549-1753 |
9.78e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1549 LEKSK-RTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1627
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1628 RKQRALAVAAKKKLEMDLKDVEAQIEAANK----------------ARDEAIKQLRKLQAQMKDYQRELEEARTSRDE-- 1689
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1690 -IFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRL 1753
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1066-1342 |
9.93e-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: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1066 EKTRQELEKAkRKLDAETTD----LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1141
Cdd:pfam04108 17 TDARSLLEEL-VVLLAKIAFlrrgLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1142 LQE-----------DLESEKAARNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKreQEVAELKKAIDDETRNH 1209
Cdd:pfam04108 96 PPGeekqktlldfiDEDSVEILRDALKELIDELQAAQESLDSDLKRfDDDLRDLQKELESL--SSPSESISLIPTLLKEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1210 ESQIQEMRQRhgtaLEEIS---EQLEQAKRV-KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA 1285
Cdd:pfam04108 174 ESLEEEMASL----LESLTnhyDQCVTAVKLtEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNS 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1286 RFSEGEKVKGELADrthkIQTELDN-VSCLLEDAEkkgiKLTKDVSSLESQLQDTQEL 1342
Cdd:pfam04108 250 LIDELLSALQLIAE----IQSRLPEyLAALKEFEE----RWEEEKETIEDYLSELEDL 299
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1058-1233 |
1.17e-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: 47.64 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1058 LEERLKKEEKTRQELEK-----AKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLArgdeevaqknnalKQL 1132
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLG-------------QNV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1133 RELQAQLAELQEDLesEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ-----QELRSKREQEVAELKKAIDDETR 1207
Cdd:pfam01442 69 EELRQRLEPYTEEL--RKRLNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*.
gi 688558694 1208 NHESQIQEMRQRHGTALEEISEQLEQ 1233
Cdd:pfam01442 147 EVQAQLSQRLQELREKLEPQAEDLRE 172
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1079-1294 |
1.24e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1079 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1158
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY---DELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1159 LKRDLSEELEALKTEL----EDTLDTTAAQQ-----ELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRhgtaLEEISE 1229
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQisegpDRITKIKDKLKELQHSLEKL----DTAIDELEEI----MDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1230 QLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1294
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLitlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
676-700 |
1.30e-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: 1.30e-05
10 20
....*....|....*....|....*
gi 688558694 676 YKESLTKLMATLRNTNPNFVRCIIP 700
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1053-1307 |
1.32e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1053 MMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQL 1132
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1133 RELQAQLAELQEDLESEKAARNKAEKLKRD---LSEELEALKTELEDTLDTTAAQQEL--RSKR-EQEVAELKKAID--D 1204
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEknE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1205 ETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKKLEAQLQEVM 1284
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD----ELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260
....*....|....*....|...
gi 688558694 1285 ARFSEGEKVKGELADRTHKIQTE 1307
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKRE 259
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1604-1756 |
1.38e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1604 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE--------AANKARD----EAIKQLRKLQA 1671
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREdlarEALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1672 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK- 1750
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK----KDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174
|
....*.
gi 688558694 1751 RRLEAR 1756
Cdd:COG1842 175 EEMEAR 180
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1016-1362 |
1.38e-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: 49.96 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1016 FLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQA 1095
Cdd:COG5185 171 ELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1096 QIDELKIQLAKKEEELQAVLARGDEEVA----QKNNALKQLRELQAQLAELQEDLESEKA------------ARNKAEKL 1159
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGENAESSKrlneNANNLIKQFENTKEKIAEYTKSIDIKKAtesleeqlaaaeAEQELEES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1160 KRDLSEELEALKTELEDTLDT-TAAQQELRSKREQEVAELKKAIDDET-RNHESQIQEMRQRHGTALEEiseQLEQAKRV 1237
Cdd:COG5185 331 KRETETGIQNLTAEIEQGQESlTENLEAIKEEIENIVGEVELSKSSEElDSFKDTIESTKESLDEIPQN---QRGYAQEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1238 KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKiqteldnvSCLLED 1317
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEIN--------RSVRSK 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 688558694 1318 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1362
Cdd:COG5185 480 KEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAE 524
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1072-1228 |
1.43e-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: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1072 LEKAKRKLDAETTDLQDQIAELQAQIDelkiQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKA 1151
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1152 ARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQE-LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEIS 1228
Cdd:pfam00529 132 LAPIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
920-1556 |
1.61e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 920 ELFAEAEEMRaRLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKI 999
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1000 KKMEEDILLLED---QNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqemmmvDLEERLKKEEKTRQeleKAK 1076
Cdd:PRK01156 228 NNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYK-----------ELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1077 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ--AVLARGDEEVAQKNnalKQLRELQAQLAELQEDLESEKAARN 1154
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKK---SRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1155 KAEKLK---RDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQL 1231
Cdd:PRK01156 371 SIESLKkkiEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNM 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1232 ------------------EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA-QLQEVMARFSEGEK 1292
Cdd:PRK01156 447 emlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1293 VKGELADRTHKIQTeldnvsclLEDAEKKGIKLTKDVSSLEsqlqdtQELLQEETRQKLNLSSRIRQLEEEknnlleqqe 1372
Cdd:PRK01156 527 ARADLEDIKIKINE--------LKDKHDKYEEIKNRYKSLK------LEDLDSKRTSWLNALAVISLIDIE--------- 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1373 eeeesrknlekqlaTLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNrlqqELDDLM 1452
Cdd:PRK01156 584 --------------TNRSRSNEIKKQLND---LESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN----EIQENK 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1453 VDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEaearekdtkalSMARALDEALEAKEEFERLNKQLRAEM 1532
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLK-----------KSRKALDDAKANRARLESTIEILRTRI 711
|
650 660
....*....|....*....|....
gi 688558694 1533 EDLISSKDDVGKNVHELEKSKRTL 1556
Cdd:PRK01156 712 NELSDRINDINETLESMKKIKKAI 735
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1489-1931 |
1.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1489 ERDRAEAEAREKDTKALsmARALDEALEAKEEFERLNKQLRAEMEDLisskdDVGKNVHELEKSKRTLEQQVEEMRTQLE 1568
Cdd:COG4717 77 EEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1569 ELEDELQATEDaklrLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1648
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1649 EAQIEA-ANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEK--------------KLKSLEAEILQLQE 1713
Cdd:COG4717 226 EEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1714 DLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELA 1793
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1794 GERSAAQKSEnARQQLERQNKDLKSKLQELEGSVKSKFKA-SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKe 1872
Cdd:COG4717 386 ELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELE- 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1873 vfmQVEDERRHADQYKEQmekansrmKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1931
Cdd:COG4717 464 ---QLEEDGELAELLQEL--------EELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1141-1401 |
1.81e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1141 ELQEDLESEK--AARNKAEKLK-RDLSEELEALKTELEDTLDTTAAQQ----ELRSKREQEVAELKKAIDD---ETRNHE 1210
Cdd:PHA02562 154 KLVEDLLDISvlSEMDKLNKDKiRELNQQIQTLDMKIDHIQQQIKTYNknieEQRKKNGENIARKQNKYDElveEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1211 SQIqemrqrhgtalEEISEQLEqakrvkgNLEKNKQTLESDNKELTNEvkslqQAKSESEHKRKKLEAQLQE-------V 1283
Cdd:PHA02562 234 AEI-----------EELTDELL-------NLVMDIEDPSAALNKLNTA-----AAKIKSKIEQFQKVIKMYEkggvcptC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1284 MARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI---KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1360
Cdd:PHA02562 291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDefnEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 688558694 1361 EEEknnlleqqeeeeesRKNLEKQLATLQAQLVETKKKLED 1401
Cdd:PHA02562 371 QAE--------------FVDNAEELAKLQDELDKIVKTKSE 397
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
938-1578 |
1.90e-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: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 938 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEqldeeeaarQKLQLEKVTAEA-------KIKKMEEDILLLE 1010
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA---------QINDLEDVADKAisnddpeEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1011 DQNSKFLKEKKLLEDRVGEM-TSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1089
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIeKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEI 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1090 IAELQAQIDelkiqlAKKEEELQAVLARGDEE---VAQKNNalkqlrelqaqlaelqedlESEKAARNKAEKLKRDLSEE 1166
Cdd:TIGR01612 1263 ENEMGIEMD------IKAEMETFNISHDDDKDhhiISKKHD-------------------ENISDIREKSLKIIEDFSEE 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1167 --LEALKTELEDTLDTTAAQQELRSKREQEVAELK--------KAIDDETRNHESQIQEMRQRHGTALEEiSEQLEQAKR 1236
Cdd:TIGR01612 1318 sdINDIKKELQKNLLDAQKHNSDINLYLNEIANIYnilklnkiKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLIKKIK 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1237 VKGNLEKNKQTLES--DNKELTNEVKSLQQAKSEsehkrkkleaqlqevmarfsegekvkgeladrthkIQTELDNVSCL 1314
Cdd:TIGR01612 1397 DDINLEECKSKIEStlDDKDIDECIKKIKELKNH-----------------------------------ILSEESNIDTY 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1315 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQlatlqaqlv 1393
Cdd:TIGR01612 1442 FKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNdHDFNINELKEHIDKSKGCKDEADKNAKAIEKN--------- 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1394 etkkkleddvgaleglEEVKRKLQKDMEVTSQKLEEKAIAfDKLEKTKNRLQQELDDLMvdlDHQRQIVSNLEKKQKKFD 1473
Cdd:TIGR01612 1513 ----------------KELFEQYKKDVTELLNKYSALAIK-NKFAKTKKDSEIIIKEIK---DAHKKFILEAEKSEQKIK 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1474 QMLAEEKTISARYAEERDRAEA------EAREKDTKALSMARALDEALEAKEEFERLNKQLRA----EMEDLISSKDDVG 1543
Cdd:TIGR01612 1573 EIKKEKFRIEDDAAKNDKSNKAaidiqlSLENFENKFLKISDIKKKINDCLKETESIEKKISSfsidSQDTELKENGDNL 1652
|
650 660 670
....*....|....*....|....*....|....*
gi 688558694 1544 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1578
Cdd:TIGR01612 1653 NSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
881-1902 |
2.21e-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: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 881 IKVKERQVKVENELVEMERKHQQLLEEKNILAEQLqAETELFAEAEEMRAR---LVAKKQELEEILHD--------LESR 949
Cdd:TIGR01612 605 LKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDEL-AKISPYQVPEHLKNKdkiYSTIKSELSKIYEDdidalyneLSSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 950 VEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlekvtaeAKIKKMEEDILLLEDQNSKFLKEKklLEDRVGE 1029
Cdd:TIGR01612 684 VKENAIDNTEDKAKLDDLKSKIDKEY---------------------DKIQNMETATVELHLSNIENKKNE--LLDIIVE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1030 MTSQLAEE--EEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAelqaqIDELKIQLAK- 1106
Cdd:TIGR01612 741 IKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN-----IDNIKDEDAKq 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1107 ---KEEELQAVLARGDEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDtldttaa 1183
Cdd:TIGR01612 812 nydKSKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD------- 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1184 qqELRSKREQEVAELKKAIDDETRNHESQIQEMrqrhgTALEEISEQLEQAKRVKGNLEK--NKQTL--ESDNKEL---- 1255
Cdd:TIGR01612 883 --DKLNDYEKKFNDSKSLINEINKSIEEEYQNI-----NTLKKVDEYIKICENTKESIEKfhNKQNIlkEILNKNIdtik 955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1256 -TNEVK---------SLQQAKSESEHKRKKL-----EAQLQEVMARFSEGEKVKGElaDRTHKIQTELDNVSCLLEDAEK 1320
Cdd:TIGR01612 956 eSNLIEksykdkfdnTLIDKINELDKAFKDAslndyEAKNNELIKYFNDLKANLGK--NKENMLYHQFDEKEKATNDIEQ 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1321 KGIKLTKDVSS---------------LESQLQDTQELLQEETRQKLNLS----SRIRQ----------LEEEKNNLLEQQ 1371
Cdd:TIGR01612 1034 KIEDANKNIPNieiaihtsiyniideIEKEIGKNIELLNKEILEEAEINitnfNEIKEklkhynfddfGKEENIKYADEI 1113
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1372 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVgaleglEEVKRKLQKDMEVTsqkleEKAIAFDKLEKTKNRLQqeldDL 1451
Cdd:TIGR01612 1114 NKIKDDIKNLDQKIDHHIKALEEIKKKSENYI------DEIKAQINDLEDVA-----DKAISNDDPEEIEKKIE----NI 1178
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1452 MVDLDHQRQIVSNLEK------KQKKFDQMLAEEKTISARYAE-------ERDRAEAEAREKDTKAL-SMARALDEALEA 1517
Cdd:TIGR01612 1179 VTKIDKKKNIYDEIKKllneiaEIEKDKTSLEEVKGINLSYGKnlgklflEKIDEEKKKSEHMIKAMeAYIEDLDEIKEK 1258
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1518 KEEFER---LNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNM-QAMKA 1593
Cdd:TIGR01612 1259 SPEIENemgIEMDIKAEMETFNISHDDD-KDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLlDAQKH 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1594 QFDRDLQARDEQN------EEKKRALVKQVREMEAELEDERKQ------RALAVAAKKKLEMDLKDVEAQIEAA--NKAR 1659
Cdd:TIGR01612 1338 NSDINLYLNEIANiynilkLNKIKKIIDEVKEYTKEIEENNKNikdeldKSEKLIKKIKDDINLEECKSKIESTldDKDI 1417
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1660 DEAIKQLRKLQAQMkdyqreLEEaRTSRDEIFTQSKENEKKL----KSLE------AEILQLQEDLASSERARRHAE-QE 1728
Cdd:TIGR01612 1418 DECIKKIKELKNHI------LSE-ESNIDTYFKNADENNENVlllfKNIEmadnksQHILKIKKDNATNDHDFNINElKE 1490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1729 RDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN--DRFRKTTMQVD----------TLNTELAGER 1796
Cdd:TIGR01612 1491 HIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNkfAKTKKDSEIIIkeikdahkkfILEAEKSEQK 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1797 SAAQKSENARQQLERQNKDLKSK----LQELEGSVKSKFkASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK--- 1869
Cdd:TIGR01612 1571 IKEIKKEKFRIEDDAAKNDKSNKaaidIQLSLENFENKF-LKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKeng 1649
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 688558694 1870 -----LKEVFMQVEDERRHADQYKEQMEKANSRMKQLK 1902
Cdd:TIGR01612 1650 dnlnsLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1406-1903 |
2.75e-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: 49.36 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1406 LEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK-KQKKFD--QMLAEEKTI 1482
Cdd:pfam07111 75 LRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEgSQRELEeiQRLHQEQLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1483 SARYAEERDRA----EAEAREKDTKALSMARA--LDEALEAKEEFERLNKQLRAEMEDLISS------------------ 1538
Cdd:pfam07111 155 SLTQAHEEALSsltsKAEGLEKSLNSLETKRAgeAKQLAEAQKEAELLRKQLSKTQEELEAQvtlveslrkyvgeqvppe 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1539 ---------KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEK 1609
Cdd:pfam07111 235 vhsqtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1610 KRALVKQVREMEAELEDERKQRALAVAAKKK-----------LEMDLKDVEAQIEA--------------ANKAR----- 1659
Cdd:pfam07111 315 VFALMVQLKAQDLEHRDSVKQLRGQVAELQEqvtsqsqeqaiLQRALQDKAAEVEVermsakglqmelsrAQEARrrqqq 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1660 --DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL----------KSLEAEILQLQEDLASSERARRHAEQ 1727
Cdd:pfam07111 395 qtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQESCPPPPPAPP 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1728 ERDELADEISNSASGKAALlDEKRRLEARIAQLEEELEEEQSNMELLndRFRKTTMQVDT---------------LNTEL 1792
Cdd:pfam07111 475 VDADLSLELEQLREERNRL-DAELQLSAHLIQQEVGRAREQGEAERQ--QLSEVAQQLEQelqraqeslasvgqqLEVAR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1793 AGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqlEEQLEQEAKERAAANKIVRRT--EKKL 1870
Cdd:pfam07111 552 QGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQIQHRAtqEKER 628
|
570 580 590
....*....|....*....|....*....|...
gi 688558694 1871 KEVFMQVEDERRhadqyKEQMEKANSRMKQLKR 1903
Cdd:pfam07111 629 NQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1659-1824 |
2.79e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1659 RDEAIKQLRKLQAQMKDyQRELEEARTSrdeiftqskenekklkSLEAEILQLQEDLASSERARRHAEQERDELADEISn 1738
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGAGA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1739 SASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS 1818
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKIADLGR 179
|
170
....*....|....
gi 688558694 1819 KL--------QELE 1824
Cdd:PRK09039 180 RLnvalaqrvQELN 193
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
870-1238 |
2.82e-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: 48.98 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 870 EEEMQAKDEELIKVKERQV----KVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRAR--------LVAKKQ 937
Cdd:pfam09731 51 LGEDPPLAPKPKTFRPLQPsvvsAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE--KEATKDAAEakaqlpksEQEKEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 938 ELEEILHDLESRVEEEEERNQSLQNEKKK-MQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEDILLLEDQNSK 1015
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQaVKAHTDSLKEASDTAEISREKaTDSALQKAEALAEKLKEVINLAKQSEEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1016 FLKEKKLLEDRVGEMTS----QLAEEEEKAKNLGKVKNKqemmMVDLEErlKKEEKTRQELEK--------AKRKLDAET 1083
Cdd:pfam09731 209 AAPPLLDAAPETPPKLPehldNVEEKVEKAQSLAKLVDQ----YKELVA--SERIVFQQELVSifpdiipvLKEDNLLSN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1084 TDLQDQIAELQAQIDELKIQLA--KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLA--ELQEDLESEKAARNKAEKL 1159
Cdd:pfam09731 283 DDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRESY 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1160 KRDLSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNHESQIQEMRQRHG---TALEEISEQLEQAKR 1236
Cdd:pfam09731 363 EEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANLKgleKATSSHSEVEDENRK 441
|
..
gi 688558694 1237 VK 1238
Cdd:pfam09731 442 AQ 443
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
993-1197 |
3.08e-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: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 993 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNL-GKVKNKQEmmmvDLEERLKKEEKTRQE 1071
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALqAEIDKLQA----EIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1072 LEKAKRK--------------LDAETTD-----------LQDQIAELQAQIDELKIQLAKKEEELQAVLArgdEEVAQKN 1126
Cdd:COG3883 88 LGERARAlyrsggsvsyldvlLGSESFSdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLA---ELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688558694 1127 NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1197
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1490-1755 |
3.09e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1490 RDRAEAEAREKDTKALSMARALDEA---LEAKEEFERLNKQLRAEMEdlISSKDDVGKnvhELEKSKRTLEQQVEEMRTQ 1566
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEAldkLRSYLPKLNPLREEKKKVS--VKSLEELIK---DVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1567 LEELEDELQATEDAKLRLEVnmqaMKAqFDRDLQARDEQ----------NEEKKRALVKQVREMEAELEDERKQRALAVA 1636
Cdd:PRK05771 109 ISELENEIKELEQEIERLEP----WGN-FDLDLSLLLGFkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1637 AKKKlemdlkdveaqieaanKARDEAIKQLRKLqaqmkDYQR-ELEEARTSRDEIftqsKENEKKLKSLEAEILQLQEDL 1715
Cdd:PRK05771 184 VVLK----------------ELSDEVEEELKKL-----GFERlELEEEGTPSELI----REIKEELEEIEKERESLLEEL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 688558694 1716 ASSerarrhaeqeRDELADEISNSasgKAALLDEKRRLEA 1755
Cdd:PRK05771 239 KEL----------AKKYLEELLAL---YEYLEIELERAEA 265
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
868-1288 |
3.45e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 868 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL------LEEKNILAEQLQAETE-LFAEAEEMRARLVAKKQELE 940
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYnsylksIESLKKKIEEYSKNIErMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 941 EILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDillledqnskFLKEK 1020
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINH----------YNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1021 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVD-LEERLKKEEKTRQELEKAKRKLdAETTDLQDQIAELQAQIDE 1099
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKS 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1100 LKIQL--AKKEEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE 1173
Cdd:PRK01156 558 LKLEDldSKRTSWLNALAVISLIDIetnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSY---IDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1174 LEDTLDTTAAQQELRSKRE---QEVAElKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLES 1250
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDnykKQIAE-IDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRARLESTIEILRT 709
|
410 420 430
....*....|....*....|....*....|....*...
gi 688558694 1251 DNKELTNEVKSLQQaKSESEHKRKKLEAQLQEVMARFS 1288
Cdd:PRK01156 710 RINELSDRINDINE-TLESMKKIKKAIGDLKRLREAFD 746
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1411-1662 |
3.68e-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: 48.22 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1411 EVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisaryaeER 1490
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---------EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1491 DRAEAEAREKDTKALsMARALDEAleakeefERLNKQLRAEMedLISSKDdvgknVHELEKSKRTLEQQVEEMRTQLEEL 1570
Cdd:COG4942 91 EIAELRAELEAQKEE-LAELLRAL-------YRLGRQPPLAL--LLSPED-----FLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1571 E---DELQATEdaklrlevnmQAMKAQFDRDLQARDEQNEEKKR--ALVKQVREMEAELEDERKQRALAVAAKKKLEMDL 1645
Cdd:COG4942 156 RadlAELAALR----------AELEAERAELEALLAELEEERAAleALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*..
gi 688558694 1646 KDVEAQIEAANKARDEA 1662
Cdd:COG4942 226 EALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1203-1433 |
3.73e-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: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1203 DDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQE 1282
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1283 VmarFSEGEKVK-----------GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEetrqkl 1351
Cdd:COG3883 95 L---YRSGGSVSyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1352 nLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKA 1431
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
..
gi 688558694 1432 IA 1433
Cdd:COG3883 245 SA 246
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
864-1095 |
3.75e-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: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 864 LQVTRQE------EEMQAKDEELIKVKERQVKVENELVEMERkhqqlleeknILAEQLQAETELFAEAEEMRARlvakkq 937
Cdd:pfam17380 383 LQMERQQknervrQELEAARKVKILEEERQRKIQQQKVEMEQ----------IRAEQEEARQREVRRLEEERAR------ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 938 ELEEI-LHDLESRVEEEEERNQSLQNEKKKMQshIQDLEEQLDEEEAARQKLqLEKVTAEAKIKKMEEDillledqnskf 1016
Cdd:pfam17380 447 EMERVrLEEQERQQQVERLRQQEEERKRKKLE--LEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEE----------- 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1017 lKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEM---MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAEL 1093
Cdd:pfam17380 513 -RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeerRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
..
gi 688558694 1094 QA 1095
Cdd:pfam17380 592 EA 593
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
999-1226 |
4.07e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 999 IKKMEEDILLLE-------DQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMvDLEERLKKEEKTRQE 1071
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILE-EQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1072 LEKA-KRKLDAETTDLQDQIAELQAQIDELKIQLA--KKEEELQAVLargdeevaQKNNAL--KQLRELQAQLAELQEDL 1146
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIevAETEERVFKL--------EKERSLldASLRELESKFIVAQEDV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1147 esekaarNKAEKLKRD-LSEELEalktELEDTLDTTAAQ-----------QELRSKREQEVAELKKAiddETRNHESQIQ 1214
Cdd:PLN02939 288 -------SKLSPLQYDcWWEKVE----NLQDLLDRATNQvekaalvldqnQDLRDKVDKLEASLKEA---NVSKFSSYKV 353
|
250
....*....|..
gi 688558694 1215 EMRQRHGTALEE 1226
Cdd:PLN02939 354 ELLQQKLKLLEE 365
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
998-1312 |
4.88e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.29 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 998 KIKKMEEDILLLEDQNSK--FLKEKKLL----------EDRVGEMTSQLAE----EEEKAKNLGKVKNKQEMMMVD---- 1057
Cdd:PRK04778 80 SLPDIEEQLFEAEELNDKfrFRKAKHEIneieslldliEEDIEQILEELQEllesEEKNREEVEQLKDLYRELRKSllan 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1058 ----------LEERLKKEEKTRQELEKAK------------RKLDAETTDLQDQIA-----------ELQAQIDELKIQL 1104
Cdd:PRK04778 160 rfsfgpaldeLEKQLENLEEEFSQFVELTesgdyveareilDQLEEELAALEQIMEeipellkelqtELPDQLQELKAGY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1105 AKKEEE--------LQAVLARGDEEVAQKNNALKQLR--ELQAQLAELQED-------LESEKAARNKAEKLKRDLSEEL 1167
Cdd:PRK04778 240 RELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDldEAEEKNEEIQERidqlydiLEREVKARKYVEKNSDTLPDFL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1168 EALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---IDDETRNHE---SQIQEMrqrhgtaLEEISEQL 1231
Cdd:PRK04778 320 EHAKEQNKELKEEIDrvkqsytlNESELESVRqlEKQLESLEKQydeITERIAEQEiaySELQEE-------LEEILKQL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1232 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKL----------------EAQLQEVMARFSEG----E 1291
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSnlpglpedylemffevSDEIEALAEELEEKpinmE 472
|
410 420
....*....|....*....|.
gi 688558694 1292 KVKGELadrtHKIQTELDNVS 1312
Cdd:PRK04778 473 AVNRLL----EEATEDVETLE 489
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1315-1520 |
5.61e-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: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1315 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVE 1394
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1395 TKKKLEDDVGA-----------------------LEGLEEVKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELDDL 1451
Cdd:COG3883 84 RREELGERARAlyrsggsvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKA----ELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1452 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEE 1520
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1458-1949 |
6.61e-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: 48.04 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1458 QRQIVSNLEKKQKkFDQMLAEEKTISAryaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIS 1537
Cdd:TIGR00618 165 KKELLMNLFPLDQ-YTQLALMEFAKKK---SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1538 SKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrDLQARDEQNEEKKRALVKQV 1617
Cdd:TIGR00618 241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA---AHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1618 REMEAELEDERKQRALAVAAKKKLEmdlkdveaqieaankardEAIKQLRKLQAQMKDYQRELEEArTSRDEIFTQSKEN 1697
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIE------------------EQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1698 EKKLKSLEA--EILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN 1775
Cdd:TIGR00618 378 TQHIHTLQQqkTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1776 DRFRKTTMQvdtlntELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSvKSKFKASIAALEAKILQLEEQLEQEAKE 1855
Cdd:TIGR00618 458 KIHLQESAQ------SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1856 RAAANKiVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeaeeeATRANASRRKLQRELDDATEASEG 1935
Cdd:TIGR00618 531 QRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNLQNITVRLQDLTEK 602
|
490
....*....|....
gi 688558694 1936 LSREVNTLKNRLRR 1949
Cdd:TIGR00618 603 LSEAEDMLACEQHA 616
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1096-1264 |
6.71e-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: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1096 QIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELqaqLAELQEDLESEKAARNKAEKLKrdlSEELEALKTELE 1175
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDR---KDALEEELRQLKQLEDELEDCD---PTELDRAKEKLK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1176 DTLDTTAAQQELRSKREQEVAELKKAIDDETrnhesqiqemrqrhgtalEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1255
Cdd:smart00787 215 KLLQEIMIKVKKLEELEEELQELESKIEDLT------------------NKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276
|
....*....
gi 688558694 1256 TNEVKSLQQ 1264
Cdd:smart00787 277 KEQLKLLQS 285
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1086-1733 |
7.33e-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: 47.89 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1086 LQDQIAELQAQIDELKIQLAKKEEELQAVLargdeevaqknNALKQLRElqaqlAELQEDLESEKAARNKAEKLK---RD 1162
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSM-----------NSIKTFWS-----PELKKERALRKEEAARISVLKeqyRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1163 LSEELEALKTELEDTLDTTAAQQELRSKREQEV------AELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQakr 1236
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFttspvdGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1237 VKGNLEKNKQTLESDNKELTN-----EVKSLQQAKSESEHKRKK----LEAQLQEVMARFSEGEKVKGELADRTHK---I 1304
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKllemlQSKGLPKKSGEEDWERTRriaeAEMQLGHLEVLLDQKEKENIHLREELHRrnqL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1305 QTELDNVSCLLEDAEKKGIKltkdVSSLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKN-----NLLEQQEEEE 1375
Cdd:pfam10174 222 QPDPAKTKALQTVIEMKDTK----ISSLERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKShskfmKNKIDQLKQE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1376 ESRKN-----LEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1450
Cdd:pfam10174 298 LSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1451 LMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMArALDEALEAKEE-FERLN 1525
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1526 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ------ATEDAKLR-LEVNMQAMKAQFDR- 1597
Cdd:pfam10174 457 EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSKl 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1598 DLQARDEQNEE----KKRALVKQVREMEAELEDERKQRALAVA-------AKKKLEMDLKDVEAQIEAANKARDEAIKQL 1666
Cdd:pfam10174 537 ENQLKKAHNAEeavrTNPEINDRIRLLEQEVARYKEESGKAQAeverllgILREVENEKNDKDKKIAELESLTLRQMKEQ 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1667 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKlkslEAEILQLQEDLASSERARRHAEQERDELA 1733
Cdd:pfam10174 617 NKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD----NSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1504-1745 |
7.94e-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: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1504 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtleQQVEEMRTQLEELEDELQATEDAKLR 1583
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----EEYNELQAELEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1584 LEVNMQAMKAQFDRdlQARDEQNEEKKRALVKQVreMEAELEDERKQRALAV-----AAKKKLEmDLKDVEAQIEAANKA 1658
Cdd:COG3883 77 AEAEIEERREELGE--RARALYRSGGSVSYLDVL--LGSESFSDFLDRLSALskiadADADLLE-ELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1659 RDEAIKQLRKLQAQMKDYQRELEeartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISN 1738
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELE----------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
....*..
gi 688558694 1739 SASGKAA 1745
Cdd:COG3883 222 AAAAAAA 228
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1129-1473 |
8.05e-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: 47.81 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1129 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTaaQQELRSKREQEVAELKKAIDDETRN 1208
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1209 HESQIQEMRQRHGtalEEISEQLEQAKRVKgNLEKNKQtlesdnKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfs 1288
Cdd:pfam17380 379 ELERLQMERQQKN---ERVRQELEAARKVK-ILEEERQ------RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1289 EGEKVKGELADRTHKIQTELDnvscllEDAEKKGIKLTKDvsslesqlqdtqellQEETRQKLnlssrirqLEEEKnnll 1368
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQ------QEEERKRKKLELE---------------KEKRDRKR--------AEEQR---- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1369 eqqeeeeesRKNLEKQLATLQAQLVETKKK-------LEDDVGALegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK 1441
Cdd:pfam17380 494 ---------RKILEKELEERKQAMIEEERKrkllekeMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKAT 562
|
330 340 350
....*....|....*....|....*....|..
gi 688558694 1442 NRlQQELDDLMVDLDHQRQIVSNlEKKQKKFD 1473
Cdd:pfam17380 563 EE-RSRLEAMEREREMMRQIVES-EKARAEYE 592
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1159-1289 |
8.07e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1159 LKRDLSEELEALKTELEDTLDttAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtalEEISEQLEQAKRVK 1238
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR-------NELQKLEKRLLQKE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 688558694 1239 GNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1289
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1055-1151 |
8.68e-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: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1055 MVDLEERLKKEEKTRQELEKAKRKLDAET-TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNnalkQLR 1133
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG----KIP 488
|
90
....*....|....*...
gi 688558694 1134 ELQAQLAELQEDLESEKA 1151
Cdd:COG0542 489 ELEKELAELEEELAELAP 506
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1488-1715 |
8.69e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1488 EERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL 1567
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1568 EELEDELQATEDAKLRLEvNMQAMKAQFDRDLQARDeQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKD 1647
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRA-ELKE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1648 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDL 1715
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1124-1427 |
8.80e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1124 QKNNALKQLRELQA-QLAELQEDLESEKAarNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEVAELKKAI 1202
Cdd:PRK05771 17 YKDEVLEALHELGVvHIEDLKEELSNERL--RKLRSLLTKLSEALDKLRSYLP------KLNPLREEKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1203 DDetrnhesqiqemrqrhgtaLEEISEQLEqaKRVKGnleknkqtLESDNKELTNEVKSLQQAKSESEhkrkKLEAqLQE 1282
Cdd:PRK05771 89 KD-------------------VEEELEKIE--KEIKE--------LEEEISELENEIKELEQEIERLE----PWGN-FDL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1283 VMARFSEGEKVKGELAdRTHKIQTE----LDNVSCLLEDAEKKG------IKLTKDVSSLESQLQDTqELLQEETRQKLN 1352
Cdd:PRK05771 135 DLSLLLGFKYVSVFVG-TVPEDKLEelklESDVENVEYISTDKGyvyvvvVVLKELSDEVEEELKKL-GFERLELEEEGT 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1353 LSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGL--EEVKRKLQKDMEVTSQKL 1427
Cdd:PRK05771 213 PSELIREIKEEL--------------EEIEKERESLLEELKELAKKYLEELLALYEYleIELERAEALSKFLKTDKT 275
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1091-1345 |
9.34e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1091 AELQAQIDELKiqlakKEEELQAvlargDEEVAQKNnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1170
Cdd:PRK11281 39 ADVQAQLDALN-----KQKLLEA-----EDKLVQQD--LEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1171 KTELEDTLDTTAAQQELRSkREQEVAELkkaiddetrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEs 1250
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQ-LESRLAQT-----------LDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1251 dnkELTNEVKSLQQAKSESEHKRK-KLEAQLQEVMARFSEGekvkgeladrthkiQTELDNVSCLLEDAEKKGIKLTKDV 1329
Cdd:PRK11281 174 ---QIRNLLKGGKVGGKALRPSQRvLLQAEQALLNAQNDLQ--------------RKSLEGNTQLQDLLQKQRDYLTARI 236
|
250
....*....|....*.
gi 688558694 1330 SSLESQLQDTQELLQE 1345
Cdd:PRK11281 237 QRLEHQLQLLQEAINS 252
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1604-1727 |
9.36e-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: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1604 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE------------AANKARDEAIKQLRKLQA 1671
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKkleekaqaaltkGNEELAREALAEKKSLEK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1672 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQ 1727
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK----KNLLKARLKAAKAQEA 149
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
997-1277 |
1.08e-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: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 997 AKIKKMEEDILLLEDqnskFLKEKKLLEDRVGEMTSQLAEEEEKAkNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKak 1076
Cdd:pfam18971 567 AKGLSLQEANKLIKD----FLSSNKELAGKALNFNKAVAEAKSTG-NYDEVKKAQK----DLEKSLRKREHLEKEVEK-- 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1077 rKLDAETTDLQDQIAELQA--QIDELkIQLAKKEEElqavlaRGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARN 1154
Cdd:pfam18971 636 -KLESKSGNKNKMEAKAQAnsQKDEI-FALINKEAN------RDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFD 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1155 KAEKLK-RDLS---EELEALKTELED----------TLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqeMRQRH 1220
Cdd:pfam18971 708 EFKNGKnKDFSkaeETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVI--INQKV 785
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1221 GTALEEISEQLEQAKRVkGNLEKNKQTLeSDNKELTNEVKSLQQAKSESEHKRKKLE 1277
Cdd:pfam18971 786 TDKVDNLNQAVSVAKAM-GDFSRVEQVL-ADLKNFSKEQLAQQAQKNEDFNTGKNSE 840
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1015-1451 |
1.15e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1015 KFLKEKKLLEDRVGEMTSQ-LAEEEEKAKNLGkvknkqemMMVDLEERLKKEEKTRQELEkakrklDAETTDLQDQIAEL 1093
Cdd:pfam06160 7 KIYKEIDELEERKNELMNLpVQEELSKVKKLN--------LTGETQEKFEEWRKKWDDIV------TKSLPDIEELLFEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1094 QAQIDELKIQLAKKE-EELQAVLARGDEEVAQKNNALKQLrelqaqlaelqedLESEKAARNKAEKLK---RDLSEELEA 1169
Cdd:pfam06160 73 EELNDKYRFKKAKKAlDEIEELLDDIEEDIKQILEELDEL-------------LESEEKNREEVEELKdkyRELRKTLLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1170 LKTELEDTLDTTAAQ-QELRSKREQEVaELKKAID-DETRNHESQIQEMrqrhgtaLEEISEQLEqakRVKGNLEKNKQT 1247
Cdd:pfam06160 140 NRFSYGPAIDELEKQlAEIEEEFSQFE-ELTESGDyLEAREVLEKLEEE-------TDALEELME---DIPPLYEELKTE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1248 LESDNKELTNEVKSLQQAKSESEH-----KRKKLEAQLQEVMARFSEGE--KVKGELADrthkIQTELDNVSCLLE---D 1317
Cdd:pfam06160 209 LPDQLEELKEGYREMEEEGYALEHlnvdkEIQQLEEQLEENLALLENLEldEAEEALEE----IEERIDQLYDLLEkevD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1318 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQkLNLSSRIRQLEEEKNnlleqqeeeeesrKNLEKQLATLQAQLVETKK 1397
Cdd:pfam06160 285 AKKYVEKNLPEIEDYLEHAEEQNKELKEELER-VQQSYTLNENELERV-------------RGLEKQLEELEKRYDEIVE 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 1398 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1451
Cdd:pfam06160 351 RLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEF 404
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1484-1803 |
1.30e-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: 46.81 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1484 ARYAEERDRaEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1563
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1564 RTQLEELEDELQATEDAKLRLEVNMQAMKaqfdrdlqardeqneEKKRALVKQVREMEAElederkqralavaaKKKLEM 1643
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAE--------------RKQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1644 DLKDVEAQIEAANKardeAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERArr 1723
Cdd:pfam07888 179 KLQQTEEELRSLSK----EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1724 hAEQERDELADEISNSASGKAALldEKRRLEAR----------------IAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1787
Cdd:pfam07888 253 -VEGLGEELSSMAAQRDRTQAEL--HQARLQAAqltlqladaslalregRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330
....*....|....*.
gi 688558694 1788 LNTELAGERSAAQKSE 1803
Cdd:pfam07888 330 LEERLQEERMEREKLE 345
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1646-1842 |
1.40e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1646 KDVEAQIEAANKARDeaikqlrkLQAQMKDYQRELEEARTSRDEIFTQSKENE---KKLKSLEAEILQLQEDLASSERAr 1722
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETEqlkQQLAQAPAKLRQAQAELEALKDD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1723 rhaeqerdelADEISNSASGKAALldekRRLEARIAQLEEELEEEQSNMELLNDrfrkttmQVDTLNTelAGERSAAQKS 1802
Cdd:PRK11281 110 ----------NDEETRETLSTLSL----RQLESRLAQTLDQLQNAQNDLAEYNS-------QLVSLQT--QPERAQAALY 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 688558694 1803 ENAR--QQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKI 1842
Cdd:PRK11281 167 ANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQN 208
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1425-1949 |
1.43e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1425 QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKD 1501
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1502 TKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR-----------------TLEQQVEEMR 1564
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1565 TQLEELEDELQATEDAKLRLEVnMQAMKAQFDRDLQARDEQN---------EEKKRALVKQVREMEAELEDERKQR---- 1631
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNnqilelegyEMDYNSYLKSIESLKKKIEEYSKNIerms 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1632 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQS----------------- 1694
Cdd:PRK01156 391 AFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhi 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1695 -KENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1773
Cdd:PRK01156 471 iNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1774 LNDRFRKTTMQ-VDTLNTELAgeRSAAQKS----ENARQQLERQNK---DLKSKLQELEGS---VKSKFKASIAALEAKI 1842
Cdd:PRK01156 551 IKNRYKSLKLEdLDSKRTSWL--NALAVISlidiETNRSRSNEIKKqlnDLESRLQEIEIGfpdDKSYIDKSIREIENEA 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1843 LQLEEQLEQEAKERAAANKIvRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEeaeeeatRANASRRKL 1922
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKL-RGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-------DAKANRARL 700
|
570 580
....*....|....*....|....*..
gi 688558694 1923 QRELDDATEASEGLSREVNTLKNRLRR 1949
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLES 727
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1648-1902 |
1.64e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1648 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFT--QSKENEKKLKSLEAEILQLQEDLASSERARRHA 1725
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1726 EQERDELADEISNSASGKAAlldekRRLEARIAQleeeleeeqsnmellndrfrkttmqvdtLNTELAGERSAAQKSENA 1805
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVI-----QQLRAQLAE----------------------------LEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1806 RQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqleeqleqeakerAAANKIVRRTEKKLKEvFMQVEDE----R 1881
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQARE--------------ASLQAQLAQLEARLAE-LPELEAElrrlE 357
|
250 260
....*....|....*....|.
gi 688558694 1882 RHADQYKEQMEKANSRMKQLK 1902
Cdd:COG3206 358 REVEVARELYESLLQRLEEAR 378
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1078-1759 |
1.71e-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: 46.74 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1078 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNnalkQLRELQAQLAELQEDLESEKAARNKAE 1157
Cdd:pfam10174 175 KSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHL----REELHRRN----QLQPDPAKTKALQTVIEMKDTKISSLE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1158 KLKRDLSEELEALKTELEdtLDTTAAQQELRSkreqevAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEqakrv 1237
Cdd:pfam10174 247 RNIRDLEDEVQMLKTNGL--LHTEDREEEIKQ------MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLE----- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1238 kgnleknkqTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVkgeLADRTHKIQteldnvsclled 1317
Cdd:pfam10174 314 ---------TLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESF---LNKKTKQLQ------------ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1318 aekkgiKLTKDVSSLESQLQDTQELLQEETRqKLNLssrirqleeeknnlleqqeeeeesrknLEKQLATLQAQLVETKK 1397
Cdd:pfam10174 370 ------DLTEEKSTLAGEIRDLKDMLDVKER-KINV---------------------------LQKKIENLQEQLRDKDK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1398 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDlmvDLDHQRQIVSNLEKKQKKFDQMLA 1477
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELT 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1478 EEKTISARYAEERDRAEAEAREKDTKALSMARALDealEAKEEFERLNKQLraemedlisskddvgKNVHELEKSKRTLE 1557
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE---QKKEECSKLENQL---------------KKAHNAEEAVRTNP 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1558 QQVEemRTQLEELEDELQATEDAKLRLEVnmqamkaqfDRDLQA-RDEQNEekKRALVKQVREMEAELEDERKQRALAVA 1636
Cdd:pfam10174 555 EIND--RIRLLEQEVARYKEESGKAQAEV---------ERLLGIlREVENE--KNDKDKKIAELESLTLRQMKEQNKKVA 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1637 AKKKLEMDLK------DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL- 1709
Cdd:pfam10174 622 NIKHGQQEMKkkgaqlLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRk 701
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 688558694 1710 QLQEDLASSERARRHAEQERDELADEISNSASGK-------AALLDEKRRLEARIAQ 1759
Cdd:pfam10174 702 QLEEILEMKQEALLAAISEKDANIALLELSSSKKkktqeevMALKREKDRLVHQLKQ 758
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
933-1115 |
1.81e-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: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 933 VAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 1012
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1013 NSKFLKEKklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1092
Cdd:COG1579 82 LGNVRNNK--------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|...
gi 688558694 1093 LQAQIDELKIQLAKKEEELQAVL 1115
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPEL 176
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1506-1859 |
1.84e-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: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1506 SMARALDEALEAKEEFERLNKQLRAEMEDLISSKddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLe 1585
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELPQAK----SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1586 vnmQAMKAQFDRDLQARDEQNEEKK---RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEA 1662
Cdd:pfam19220 89 ---VARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1663 IKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASS----ERARRHAEQERDELADEISN 1738
Cdd:pfam19220 166 RERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEqaerERAEAQLEEAVEAHRAERAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1739 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQ------ 1812
Cdd:pfam19220 246 LRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraelee 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1813 -----NKDLKSKLQELEGSVKS-------------KFKASIAALEAKILQLEEQLEQEAKERAAA 1859
Cdd:pfam19220 326 raemlTKALAAKDAALERAEERiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
865-1344 |
1.92e-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: 46.27 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 865 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETEL---FAEAEEMRARLVAKKQELEE 941
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 942 IlHDLESRVeeeeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKL-QLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1020
Cdd:pfam05557 199 I-PELEKEL-------ERLREHNKHLNENIENKLLLKEEVEDLKRKLeREEKYREEAATLELEKEKLEQELQSWVKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1021 KLLEDRVGE-MTSQLAEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDE 1099
Cdd:pfam05557 271 TGLNLRSPEdLSRRIEQLQQREIVLKEENS-------SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1100 L--KIQLAKKEEE-LQAVLARGDEEVAQKN---NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTE 1173
Cdd:pfam05557 344 LqrRVLLLTKERDgYRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1174 LedTLDTTAAQQELRSKREQEVAELKKAIDDetrnhesqIQEMRQRhgtaLEEISEQLEqakrvkgnLEKNKQTLESDNK 1253
Cdd:pfam05557 424 L--QALRQQESLADPSYSKEEVDSLRRKLET--------LELERQR----LREQKNELE--------MELERRCLQGDYD 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1254 ELTNEVKSLQQ-AKSESEHKRKKLEAQLQEVMARfsegekvkgeLADRTHKIQTELDNVSCL----LEDAEKKGIKLTKD 1328
Cdd:pfam05557 482 PKKTKVLHLSMnPAAEAYQQRKNQLEKLQAEIER----------LKRLLKKLEDDLEQVLRLpettSTMNFKEVLDLRKE 551
|
490
....*....|....*.
gi 688558694 1329 VSSLESQLQDTQELLQ 1344
Cdd:pfam05557 552 LESAELKNQRLKEVFQ 567
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1596-1719 |
2.05e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1596 DRDLQARDEQNEEKKRALVKQVREMEAELEDE---RKQRALAVAAKKKLEMDLKDVEAQIEAANK------ARDEAIKQL 1666
Cdd:COG1566 78 PTDLQAALAQAEAQLAAAEAQLARLEAELGAEaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgavsqqELDEARAAL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 688558694 1667 RKLQAQMKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAEILQLQEDLASSE 1719
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLREE-EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1377-1585 |
2.09e-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: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1377 SRKNLEKQLATLQAQ------LVETKKKLEDDVgalEGLEEVKRK--LQK-DMEVTSQKLEEKaiafdkLEKTKNRLQQE 1447
Cdd:pfam15066 340 SNLYLEKKVKELQMKitkqqvFVDIINKLKENV---EELIEDKYNviLEKnDINKTLQNLQEI------LANTQKHLQES 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1448 lddlmvdldhqrqivsnleKKQKKFDQMlaEEKTISARYAEERDRAEAEAREKDtKALSMARALDEALEAKE-EFERLnK 1526
Cdd:pfam15066 411 -------------------RKEKETLQL--ELKKIKVNYVHLQERYITEMQQKN-KSVSQCLEMDKTLSKKEeEVERL-Q 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1527 QLRAEMEDLISSKDDVgknvheLEKSKRTLEQQVEEMRTQLEELEDE-LQATEDAKLRLE 1585
Cdd:pfam15066 468 QLKGELEKATTSALDL------LKREKETREQEFLSLQEEFQKHEKEnLEERQKLKSRLE 521
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1418-1662 |
2.13e-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: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1418 KDMEVTSQKLEEKAIAfdklEKTKNRLQQELDDLmvdLDHqrqiVSNLEKKQKKFDQmLAEEKTISAryaeERDRAEAEA 1497
Cdd:NF012221 1552 KQDDAAQNALADKERA----EADRQRLEQEKQQQ---LAA----ISGSQSQLESTDQ-NALETNGQA----QRDAILEES 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1498 REKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIssKDDVGKnvhELEKSKRTLEQQVEEMRTQLE----ELEDE 1573
Cdd:NF012221 1616 RAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQE---QLDDAKKISGKQLADAKQRHVdnqqKVKDA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1574 LQATEDAKLRLEVNMQAMKAQFDrdlQARDEQNEEKKRALVKQVREMEAElederkQRALAVAAKKKLEMDlKDVEAQIE 1653
Cdd:NF012221 1691 VAKSEAGVAQGEQNQANAEQDID---DAKADAEKRKDDALAKQNEAQQAE------SDANAAANDAQSRGE-QDASAAEN 1760
|
....*....
gi 688558694 1654 AANKARDEA 1662
Cdd:NF012221 1761 KANQAQADA 1769
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1079-1233 |
2.26e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1079 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEK 1158
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDL----QDSVANLRASLSAAEAERSRLQALLAELA---GAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1159 LKRDLSEELEALKTELEDTLDTTAA-QQELRSKREQeVAELKKAIDD-ETRNHESQ--IQEMRQRHGTALEEISEQLEQ 1233
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELlNQQIAALRRQ-LAALEAALDAsEKRDRESQakIADLGRRLNVALAQRVQELNR 194
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1638-1819 |
2.53e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1638 KKKLEMDLKDVEAqieAANKARDEAIKQL---------RKLQAQ-MKDYQRELEE----ARTSRDEIFTQSKE-----NE 1698
Cdd:PRK10929 25 EKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEprsvpPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1699 KKLKSLEAEILQLQEDLAssERARRhAEQERDElADEISNSASGKAALLDEKRRL----EARI-AQLEEELEEEQSNMEL 1773
Cdd:PRK10929 102 MSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLAQAQLTA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 688558694 1774 LNDRFRKTTMQVDTLntELagersaAQKSENARQQLERQNKDLKSK 1819
Cdd:PRK10929 178 LQAESAALKALVDEL--EL------AQLSANNRQELARLRSELAKK 215
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1070-1298 |
2.77e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1070 QELEKAKRKLD------AETTDLQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQKNNALkQLRELQAQLAELQ 1143
Cdd:PRK11281 63 QDLEQTLALLDkidrqkEETEQLKQQLAQAPAKLRQAQ-------AELEALKDDNDEETRETLSTL-SLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1144 EDLESekaarnkaekLKRDLSE---ELEALKTELEDtldttaAQQEL--RSKREQEVAELKKAIDDETRNHESQIQEMRQ 1218
Cdd:PRK11281 135 DQLQN----------AQNDLAEynsQLVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1219 RHGTALEEISEQLEQakrvkgNLEKNKQTLESDNKELtnEVKSLQQAKSESE---------HKRKKL------EAQLQEV 1283
Cdd:PRK11281 199 AEQALLNAQNDLQRK------SLEGNTQLQDLLQKQR--DYLTARIQRLEHQlqllqeainSKRLTLsektvqEAQSQDE 270
|
250
....*....|....*
gi 688558694 1284 MARFSEGEKVKGELA 1298
Cdd:PRK11281 271 AARIQANPLVAQELE 285
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1569-1841 |
3.25e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1569 ELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElederkqrALAVAAKKKLEMDLKDV 1648
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAAEARAAKDKDAVAA--------ALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1649 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskENEKKlKSLEAEIlqlqedlassERAR-RHAEQ 1727
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAA------------ADPKK-AAVAAAI----------ARAKaKKAAQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1728 ErDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmqvdtlnTELAGERSAAQKSENARQ 1807
Cdd:PRK05035 565 Q-AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA---------VAAAIARAKAKKAEQQAN 634
|
250 260 270
....*....|....*....|....*....|....
gi 688558694 1808 QLERQNKDLKsklqelegsvKSKFKASIAALEAK 1841
Cdd:PRK05035 635 AEPEEPVDPR----------KAAVAAAIARAKAR 658
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
932-1308 |
3.57e-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: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 932 LVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK----------LQLEKVTAEA---- 997
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKylllqkqleqLQEENFRLETardd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 998 ---KIKKMEEDILLLEDQNSKFLK---EKKLLED----------RVGEMTSQLAEEEEKAKNLG----KVKNKQEMMM-- 1055
Cdd:pfam05622 85 yriKCEELEKEVLELQHRNEELTSlaeEAQALKDemdilressdKVKKLEATVETYKKKLEDLGdlrrQVKLLEERNAey 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1056 ----VDLEERLKKEEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNN---A 1128
Cdd:pfam05622 165 mqrtLQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTlreT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1129 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLseeleaLKTELEDTLdttaaqqeLRSKREQEVAELKKAIDDETRn 1208
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI------MPAEIREKL--------IRLQHENKMLRLGQEGSYRER- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1209 hesqiqemrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE-------SEHKRKKLEAQLQ 1281
Cdd:pfam05622 306 ---------------LTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEqgskaedSSLLKQKLEEHLE 370
|
410 420
....*....|....*....|....*..
gi 688558694 1282 EVMARFSEGEKVKGELADRTHKIQTEL 1308
Cdd:pfam05622 371 KLHEAQSELQKKKEQIEELEPKQDSNL 397
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1476-1632 |
3.64e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1476 LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED----LISSKDDVGKNVHELEK 1551
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1552 SKRTLEQQVEEMRTQLEELE------DELQATEDAKLRLEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELE 1625
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEkkeeelEELIEEQLQELERISGLTAEEAK----EILLEKVEEEARHEAAVLIKEIEEEAK 183
|
....*..
gi 688558694 1626 DERKQRA 1632
Cdd:PRK12704 184 EEADKKA 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
898-1231 |
3.73e-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: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 898 ERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQ--SLQNEKKkmqsHIQDLE 975
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELE----RLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 976 EQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknlgkvknkqemmm 1055
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--------------- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1056 vDLEERLKKEEKTRQELEKAKRkldaettdLQDQIAELQAQIDELKIQLAKKEEELQ----AVLARGDEEVAQKNNALKQ 1131
Cdd:COG4913 750 -LLEERFAAALGDAVERELREN--------LEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLAL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1132 LRELQAQ-LAELQEDLESEKAARNKAEK--LKRDLSEELEALKTELE---DTL------DTTAAQQELRSKREQEVAELK 1199
Cdd:COG4913 821 LDRLEEDgLPEYEERFKELLNENSIEFVadLLSKLRRAIREIKERIDplnDSLkripfgPGRYLRLEARPRPDPEVREFR 900
|
330 340 350
....*....|....*....|....*....|..
gi 688558694 1200 KAIDDETRNHESQIQEMRQRHGTALEEISEQL 1231
Cdd:COG4913 901 QELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
964-1345 |
4.11e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 964 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVT----------------------AEAKIKKMEEDILLLEDQNSK--FLKE 1019
Cdd:PRK04778 24 RKRNYKRIDELEERKQELENLPVNDELEKVKklnltgqseekfeewrqkwdeiVTNSLPDIEEQLFEAEELNDKfrFRKA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1020 KKLLedrvGEMTSQLAEEEEKAKNLgkvknKQEMM-MVDLEERLKKE-EKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1097
Cdd:PRK04778 104 KHEI----NEIESLLDLIEEDIEQI-----LEELQeLLESEEKNREEvEQLKDLYRELRKSLLANRFSFGPALDELEKQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1098 DELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDT 1177
Cdd:PRK04778 175 ENLEEEFSQFVELTES----GDYVEAR-----EILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1178 ---LDTTAAQQELRSKREQeVAELKKAID----DETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEKNKQTLES 1250
Cdd:PRK04778 246 gyhLDHLDIEKEIQDLKEQ-IDENLALLEeldlDEAEEKNEEIQE-------RIDQLYDILEREVKARKYVEKNSDTLPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1251 D-------NKELTNEVKSLQQAK--SESE-HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK 1320
Cdd:PRK04778 318 FlehakeqNKELKEEIDRVKQSYtlNESElESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEK 397
|
410 420
....*....|....*....|....*
gi 688558694 1321 KGIKLTKDVSSLESQLQDTQELLQE 1345
Cdd:PRK04778 398 EQEKLSEMLQGLRKDELEAREKLER 422
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1062-1362 |
4.45e-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: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1062 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAqlae 1141
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTR---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1142 lQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQElrskreqevaelkkaiddetrNHESQIQEMrQRHg 1221
Cdd:pfam15905 137 -VNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQE---------------------GMEGKLQVT-QKN- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1222 taLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLeAQLQEVMArfsegekvkgELADRT 1301
Cdd:pfam15905 193 --LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDI-AQLEELLK----------EKNDEI 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1302 HKIQTELDNVSCLLEdaekkgiKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEE 1362
Cdd:pfam15905 260 ESLKQSLEEKEQELS-------KQIKDLNEKCKLLEsEKEELLREYEEKEQTLNAELEELKE 314
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1597-1806 |
4.57e-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: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1597 RDLQARDEQNEEKKRALVKQVREMEAELEDerkqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1676
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1677 QRELEEARTSRD--EIFTQSKENEKKLKSLEA----------EILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1744
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSESFSDFLDRLSAlskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1745 ALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENAR 1806
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1095-1205 |
4.68e-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: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1095 AQIDELKIQLAKKEEELQAVLARGDEEVAQKnnalkqLRELQAQLAELQEDLESEKaARNKAEKlkrDLSEELEALKTEL 1174
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALK-ARWEAEK---ELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 688558694 1175 EDTLDTTAAQQELRSKREQEVAELKKAIDDE 1205
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1059-1279 |
5.40e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1059 EERLKKEEKTRQEleKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQ 1138
Cdd:PRK05035 459 QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAE 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1139 LAELQEDLESEKA-----ARNKAEKLKR-----DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRN 1208
Cdd:PRK05035 537 KQAAAAADPKKAAvaaaiARAKAKKAAQqaanaEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1209 HESQIQEMR-QRHGTALEEISEQLEQAK--RVKGNLEKNK-----QTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1279
Cdd:PRK05035 617 VAAAIARAKaKKAEQQANAEPEEPVDPRkaAVAAAIARAKarkaaQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
877-1175 |
6.12e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 877 DEELIKVKERQVKVENELVEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLVAKkqELEEILHDLESRVEE 952
Cdd:PRK05771 27 ELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklRSYLPKLNPLREEKKKVSVKSLEELIK--DVEEELEKIEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 953 EEERNQSLQNEKKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDIllledqnsKFLKEKKLLEDRVGEMTS 1032
Cdd:PRK05771 105 LEEEISELENEIKELEQEIE----------------RLEPW------GNFDLDL--------SLLLGFKYVSVFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1033 QLAEEEEKAKNLGKV----KNKQEMMMV---------DLEERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDE 1099
Cdd:PRK05771 155 DKLEELKLESDVENVeyisTDKGYVYVVvvvlkelsdEVEEELKKLGFERLELE-EEGTPSELIREIKEELEEIEKERES 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1100 LK---IQLAKKEEELQAVLARGDEEVAQKNNALKQLRE------LQA-----QLAELQEDLesEKAARNKAEKLKRDLSE 1165
Cdd:PRK05771 234 LLeelKELAKKYLEELLALYEYLEIELERAEALSKFLKtdktfaIEGwvpedRVKKLKELI--DKATGGSAYVEFVEPDE 311
|
330
....*....|
gi 688558694 1166 ELEALKTELE 1175
Cdd:PRK05771 312 EEEEVPTKLK 321
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1023-1107 |
6.19e-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: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1023 LEDRVGEMTSQLAEEEEKAKNLGKVKNkqEMMMVDLEERLK----------KEEKTRQELEKAKRKLDAETTDLQDQIAE 1092
Cdd:cd23165 11 LNARLHELKEELKAKKKELENLEDASD--ELELADDDEPVPykigevfvhlSLEEAQERLEKAKEELEEEIEKLEEEIDE 88
|
90
....*....|....*
gi 688558694 1093 LQAQIDELKIQLAKK 1107
Cdd:cd23165 89 IEEEMKELKVQLYAK 103
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1054-1193 |
6.44e-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: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1054 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLR 1133
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLA-------TERSARREAEAELE 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1134 ELQAQLAELQEDLESEKAARnkaEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ 1193
Cdd:pfam09787 118 RLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQ 174
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
986-1186 |
6.62e-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: 43.13 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 986 QKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqemmMVDLEERLKKE 1065
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA----------LTKGNEELARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1066 EKTR-QELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARgdEEVAQKNNALKQLR---------EL 1135
Cdd:pfam04012 88 ALAEkKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTSLgslstssatDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 688558694 1136 QAQLAELQEDLESEKAARNKAEKlKRDLSEELEALKTELEDTLDTTAAQQE 1186
Cdd:pfam04012 166 FERIEEKIEEREARADAAAELAS-AVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1212-1363 |
6.97e-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: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1212 QIQEMR----QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1287
Cdd:pfam10168 540 ATQVFReeylKKHDLAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1288 -------SEGEKvkgELADRTHKIQTELDNVSCLLEDAEKK------------GIKLTKDVSSLESQLQDTQELLQEETR 1348
Cdd:pfam10168 620 nsqlpvlSDAER---EMKKELETINEQLKHLANAIKQAKKKmnyqryqiaksqSIRKKSSLSLSEKQRKTIKEILKQLGS 696
|
170
....*....|....*
gi 688558694 1349 QKLNLSSRIRQLEEE 1363
Cdd:pfam10168 697 EIDELIKQVKDINKH 711
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1704-1842 |
7.05e-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: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1704 LEAEILQLQEDLASSERARRHAEQERD---ELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1780
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDrlqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1781 TTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS---KLQELEGSVKSKFKASIAALEAKI 1842
Cdd:pfam00529 136 GGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQsaaENQAEVRSELSGAQLQIAEAEAEL 200
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1052-1186 |
7.60e-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: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1052 EMMMVDLEERLKKE--EKTRQELEKAKRKLDAETTDLQD------------QIAELQAQIDELKIQLAKKEEELQAVLAR 1117
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1118 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLkrdlsEELEALKTEL---EDTLDTTAAQQE 1186
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1548-1733 |
9.02e-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: 43.68 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1548 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDE 1627
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1628 RKQRALAVAAKKKLEmdlkdveaqiEAANKARDEAIKqlrKLQAQMKdyqRELEEARTSRDEIFTQSKENEKKLKSLEAE 1707
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 688558694 1708 ILQLQEDLASSERARRHAEQERDELA 1733
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1662-1949 |
9.41e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1662 AIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAE---QERDELADEISN 1738
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1739 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttmqvdtlntelAGERSAAQKSENARQQLERQNKDLKS 1818
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1819 KLQELEgSVKSKFKASIAALEAKIlqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANsRM 1898
Cdd:PRK03918 308 ELREIE-KRLSRLEEEINGIEERI-----------KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-EL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 688558694 1899 KQLKRQLeeaeeeatrANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1949
Cdd:PRK03918 375 ERLKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1276-1625 |
9.84e-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: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1276 LEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKgikLTKDVSSLESQLQDTQELLQEETRQKLNLSS 1355
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE---LESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1356 RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE------DDVGALEGLEEVKRK-LQKDMEVTSQKLE 1428
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELErmkeraKKAGAQRKEEEAERKqLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1429 EKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1508
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1509 RALDEALEAKEEFERLNKQL--------------RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1574
Cdd:pfam07888 269 RTQAELHQARLQAAQLTLQLadaslalregrarwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVEL 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1575 QATEDAKL----RLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELE 1625
Cdd:pfam07888 349 GREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1032-1170 |
9.99e-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: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1032 SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEEL 1111
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-APAWLAA 607
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1112 QAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1170
Cdd:COG3096 608 QDALERLREQSGE---ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1631-1840 |
1.13e-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: 43.13 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1631 RALAVAAKKKLEMDLKD-----VEAQIEAANKARDEA---IKQLRKLQAQMKDYQRELEEARTSRDEIFTQ--SKENEKK 1700
Cdd:cd22656 101 DDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAakvVDKLTDFENQTEKDQTALETLEKALKDLLTDegGAIARKE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1701 LKSLEAEILQLQEDLAsserarRHAEQERDELADEISNsasgkaalLDEKRRLEARIaqleeeleeeQSNMELLNDrfrk 1780
Cdd:cd22656 181 IKDLQKELEKLNEEYA------AKLKAKIDELKALIAD--------DEAKLAAALRL----------IADLTAADT---- 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1781 ttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEA 1840
Cdd:cd22656 233 ---DLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
881-1110 |
1.18e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 881 IKVKERQVKVENELVEMERKHQQLLEEKN--ILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQ 958
Cdd:PHA02562 183 IQTLDMKIDHIQQQIKTYNKNIEEQRKKNgeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 959 SLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvTAEAKIKKmeedillLEDQNSKFLKEKKLLEDRVGEMTSQLAEEE 1038
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQIS--EGPDRITK-------IKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1039 EKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEE 1110
Cdd:PHA02562 334 EQSKKLLELKNKIS----TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
963-1165 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 963 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVtaEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAK 1042
Cdd:pfam06160 231 EHLNVDKEIQQLEEQLEENLALLENLELDEA--EEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1043 NLgkvknKQEMMMVDLEERLKKEEKTRQElekakrkldaettDLQDQIAELQAQIDELKIQLAKKE---EELQAVLargd 1119
Cdd:pfam06160 309 EL-----KEELERVQQSYTLNENELERVR-------------GLEKQLEELEKRYDEIVERLEEKEvaySELQEEL---- 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 688558694 1120 eevaqkNNALKQLRELQAQLAELQEDLES----EKAARNKAEKLKRDLSE 1165
Cdd:pfam06160 367 ------EEILEQLEEIEEEQEEFKESLQSlrkdELEAREKLDEFKLELRE 410
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1066-1352 |
1.33e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1066 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQED 1145
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1146 LESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE 1225
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1226 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHkRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ 1305
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL-SALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 688558694 1306 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN 1352
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1037-1581 |
1.37e-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: 43.59 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1037 EEEKAKNLGKVKNKQEMMMVDL----EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ 1112
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1113 A-----------VLARGDEEVAQKNNALKQlRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELE 1175
Cdd:pfam07111 215 AqvtlveslrkyVGEQVPPEVHSQTWELER-QELLDTMQHLQEDRADLQATvellqvRVQSLTHMLALQEEELTRKIQPS 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1176 DTLD---TTAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1252
Cdd:pfam07111 294 DSLEpefPKKCRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1253 ---KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKK--GIK-LT 1326
Cdd:pfam07111 373 msaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhTIKgLM 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1327 KDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeeSRKNLEKQLATLQAQLvETKKKLEDDVGAL 1406
Cdd:pfam07111 453 ARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREER------------NRLDAELQLSAHLIQQ-EVGRAREQGEAER 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1407 EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSnlekkqKKFDQMLAEEKTISARY 1486
Cdd:pfam07111 520 QQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYG------QALQEKVAEVETRLREQ 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1487 AEERDRAEAEAREKDTKALSMARALDEalEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR----TLEQQVEE 1562
Cdd:pfam07111 594 LSDTKRRLNEARREQAKAVVSLRQIQH--RATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNlmlaTLQQEGLL 671
|
570
....*....|....*....
gi 688558694 1563 MRTQLEELEDELQATEDAK 1581
Cdd:pfam07111 672 SRYKQQRLLAVLPSGLDKK 690
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1626-1816 |
1.43e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1626 DERKQRALAVAAKKKLEMDLK---DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN----- 1697
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrq 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1698 -EKKLKSLEAEILQLQEDLAS-----------SERARR---HAEQERDELADEISNSASGKAALLDEKR-RLEARIAQle 1761
Cdd:PRK11281 126 lESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQAEQAL-- 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1762 eeleeeqsnMELLNDrFRKTTMQVDTLNTELaGERSAAQKSENArQQLERQNKDL 1816
Cdd:PRK11281 204 ---------LNAQND-LQRKSLEGNTQLQDL-LQKQRDYLTARI-QRLEHQLQLL 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1017-1688 |
1.44e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1017 LKEKKLLEDRVGEMTSQLAE----------EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL 1086
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSEleqrlrqqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1087 QDQIAELQAQIDELKiQLAKKEEELQAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1166
Cdd:PRK04863 585 RQQLEQLQARIQRLA-ARAPAWLAAQDALARLREQSGE---EFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1167 LEALkteledTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISeqleqakRVKGNLEK 1243
Cdd:PRK04863 661 IERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLS-------DAAEQLAG 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1244 NKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE--GEKVKGELA--DRTHKIQTELDNVSCLLEdae 1319
Cdd:PRK04863 728 LEDCPE-DLYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRfpEVPLFGRAAreKRIEQLRAEREELAERYA--- 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1320 kkgiKLTKDVSSLESQLQDTQELLQ-----------EETRQKLNlsSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1388
Cdd:PRK04863 804 ----TLSFDVQKLQRLHQAFSRFIGshlavafeadpEAELRQLN--RRRVELERALADHESQEQQQRSQLEQAKEGLSAL 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1389 QAQLVETKKKLEDDVGalEGLEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQ---QELDDLMVDLDHQRQIVSNL 1465
Cdd:PRK04863 878 NRLLPRLNLLADETLA--DRVEEIREQL-DEAEEAKRFVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDA 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1466 ekKQKKFDqmlaeektisarYAEERDRAEAEAREKDTKALSMARALDEALEAK-EEFERLNKQLRAEMEDLISSKDDVGK 1544
Cdd:PRK04863 955 --KQQAFA------------LTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRlEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1545 NVHELEKSKRTLEQQVEEMRTQLEELedELQATEDAklrlevnmqAMKAQFDRD-LQARDEQNEEKKRALVKQVREMEAE 1623
Cdd:PRK04863 1021 VLASLKSSYDAKRQMLQELKQELQDL--GVPADSGA---------EERARARRDeLHARLSANRSRRNQLEKQLTFCEAE 1089
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1624 LEDERKQralavaaKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-----EEARTSRD 1688
Cdd:PRK04863 1090 MDNLTKK-------LRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELaylsaDELRSMSD 1152
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1097-1279 |
1.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1097 IDELKIQLAKKEEELQAvlargdEEVAQKNNALKQLRELQAQ--LAELQEDLESE-KAARNKAEKLKRDLSEELEALKTE 1173
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIL------EEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1174 LEDTLDTTA---AQQELRSKREQEVAELKKaiddetrnhesQIQEMRQRHGTALEEISE-QLEQAKRVKgnLEKNKQTLE 1249
Cdd:PRK12704 102 LELLEKREEeleKKEKELEQKQQELEKKEE-----------ELEELIEEQLQELERISGlTAEEAKEIL--LEKVEEEAR 168
|
170 180 190
....*....|....*....|....*....|
gi 688558694 1250 SDNKELTNEVKslQQAKSESEHKRKKLEAQ 1279
Cdd:PRK12704 169 HEAAVLIKEIE--EEAKEEADKKAKEILAQ 196
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1057-1212 |
1.68e-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: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1057 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLREL 1135
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAAL 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688558694 1136 QAQLAELQEDLESeKAARNKAEKLKRDL-SEELEALKTELEdtldttAAQQELRSKREQEVAELKKAIDDETRNHESQ 1212
Cdd:pfam12795 162 KAQIDMLEQELLS-NNNRQDLLKARRDLlTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
913-1319 |
1.69e-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: 43.30 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 913 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshiqdleeqldeeeaarqklqlek 992
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT----------------------------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 993 vtaeakikkmeedillLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEE--------KAKnlgKVKNKQEMMMVDLEERLkk 1064
Cdd:pfam06160 137 ----------------LLANRFSYGPAIDELEKQLAEIEEEFSQFEEltesgdylEAR---EVLEKLEEETDALEELM-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1065 eEKTRQELEKAKRKLDAETTDLQDQIAELQAQ---IDELKI-----QLAKKEEELQAVLARGDEEVAQKNNalkqlRELQ 1136
Cdd:pfam06160 196 -EDIPPLYEELKTELPDQLEELKEGYREMEEEgyaLEHLNVdkeiqQLEEQLEENLALLENLELDEAEEAL-----EEIE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1137 AQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---ID 1203
Cdd:pfam06160 270 ERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELErvqqsytlNENELERVRglEKQLEELEKRydeIV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1204 DETRNHE---SQIQEMrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKseSEHKRKKLEAQL 1280
Cdd:pfam06160 350 ERLEEKEvaySELQEE-------LEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL--REIKRLVEKSNL 420
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 688558694 1281 ----QEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1319
Cdd:pfam06160 421 pglpESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQ 463
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1666-1829 |
1.72e-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: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1666 LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEisnsasgKAA 1745
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE-------KDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1746 LLDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEG 1825
Cdd:pfam07888 120 LLAQRAAHEARIRE--------------LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
....
gi 688558694 1826 SVKS 1829
Cdd:pfam07888 186 ELRS 189
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1442-1876 |
1.84e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.97 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1442 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaeEKTISARYAEERDRAEAEAREKDTKALsMARALDEALEAKEEF 1521
Cdd:COG5278 89 DELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRARLLLLALAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1522 ERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQA 1601
Cdd:COG5278 166 AALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1602 RDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE 1681
Cdd:COG5278 246 LAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAAL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1682 EARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLE 1761
Cdd:COG5278 326 AALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1762 EELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAK 1841
Cdd:COG5278 406 AAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALA 485
|
410 420 430
....*....|....*....|....*....|....*
gi 688558694 1842 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQ 1876
Cdd:COG5278 486 EAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1607-1880 |
1.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1607 EEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTS 1686
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1687 RDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1766
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1767 EQSNMELLNDRFRKTTMQ-VDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQL 1845
Cdd:COG4372 190 KEANRNAEKEEELAEAEKlIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270
....*....|....*....|....*....|....*
gi 688558694 1846 EEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDE 1880
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1533-1707 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1533 EDLISSKDDvGKNVHELEkSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRA 1612
Cdd:pfam09787 24 EKLIASLKE-GSGVEGLD-SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1613 LVKQV---REMEAEL-----------EDERKQRALAVAAKKKLEMDLKDVEAQIEA---ANKARDEAIKQLRKLQAQMKD 1675
Cdd:pfam09787 102 LATERsarREAEAELerlqeelryleEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQ 181
|
170 180 190
....*....|....*....|....*....|..
gi 688558694 1676 YQRELEEARTSRDEIFTQSKENEKKLKSLEAE 1707
Cdd:pfam09787 182 KQTMLEALSTEKNSLVLQLERMEQQIKELQGE 213
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1548-1759 |
1.90e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1548 ELEKSKRTLEQQVEEMRTQLEELED-ELQATEDAKLRLEVNMQAmkaqfdrdlqardeqNEEKKRALVKQVREMeaeL-E 1625
Cdd:COG0497 176 ELRADEAERARELDLLRFQLEELEAaALQPGEEEELEEERRRLS---------------NAEKLREALQEALEA---LsG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1626 DERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE---------EARTSR--------- 1687
Cdd:COG0497 238 GEGGALDLLGQALRALE-RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdperleevEERLALlrrlarkyg 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1688 ---DEIFTQSKENEKKLKSLEAeilqLQEDLASSERARRHAEQERDELADEISNsASGKAAlldekRRLEARIAQ 1759
Cdd:COG0497 317 vtvEELLAYAEELRAELAELEN----SDERLEELEAELAEAEAELLEAAEKLSA-ARKKAA-----KKLEKAVTA 381
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1016-1171 |
2.19e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1016 FLKEKKLLEDRvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELqa 1095
Cdd:PRK12705 24 LLKKRQRLAKE-AERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1096 qiDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQ---LRELQAQ---LAELQEDLESEKAARNKAEKLKRDLSEELEA 1169
Cdd:PRK12705 101 --DNLENQLEEREKALSARELELEELEKQLDNELYRvagLTPEQARkllLKLLDAELEEEKAQRVKKIEEEADLEAERKA 178
|
..
gi 688558694 1170 LK 1171
Cdd:PRK12705 179 QN 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
865-1050 |
2.20e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 865 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERK----HQQLLEEKNILAEQLQA--------------ETELFAEAE 926
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 927 EMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQShiqdleeQLDEEEAARQKLQLEKVTAEAKIKKMEEDI 1006
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 688558694 1007 LLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1050
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1222-1720 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1222 TALEEISEQLEQAKRVKGNLEKN-------KQTLESDNKELTNEVKSLQQAKSESEHKRKKleaQLQEVMARFSEgEKVK 1294
Cdd:pfam15818 7 TSLLEALEELRMRREAETQYEEQigkiiveTQELKWQKETLQNQKETLAKQHKEAMAVFKK---QLQMKMCALEE-EKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1295 GELADRTHkiQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQdTQELLQEETRQKLNlssrirQLEEEKNNLLEQQEEE 1374
Cdd:pfam15818 83 YQLATEIK--EKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQ-LHLLAKEDHHKQLN------EIEKYYATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1375 EESRKNLEKQLA---TLQAQLVETKKKLEDDVGAL-EGLEEVKRKLQKDmEVTSQ-KLEEKAIAFDKLEKTKNRLQQELD 1449
Cdd:pfam15818 154 KENHGKLEQNVQeaiQLNKRLSALNKKQESEICSLkKELKKVTSDLIKS-KVTCQyKMGEENINLTIKEQKFQELQERLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1450 -DLMVDLDHQRQIVSNLEKKQKKFdqmlaeektISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERlnKQL 1528
Cdd:pfam15818 233 mELELNKKINEEITHIQEEKQDII---------ISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQR--EKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1529 RAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrdlqarDEQNEE 1608
Cdd:pfam15818 302 KENEEKFLNLQN-------EHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQ--------KKFEED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1609 KKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQReLEeaRTSRD 1688
Cdd:pfam15818 367 KKFQNVPEVNNENSEMSTEKSENLIIQKYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQV-LE--KSFKN 443
|
490 500 510
....*....|....*....|....*....|..
gi 688558694 1689 EIFTQSKENEKKLKSLEAEILQLQEDLASSER 1720
Cdd:pfam15818 444 EIDTSVPQDKNQSEISLSKTLCTDKDLISQGQ 475
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1060-1169 |
2.51e-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: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1060 ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEELQAvlARGDEEVAQKNNALKQLRELQAQL 1139
Cdd:COG2268 220 NREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEAAYEIAE--ANAEREVQRQLEIAEREREIELQE 296
|
90 100 110
....*....|....*....|....*....|...
gi 688558694 1140 AELQEDLESEKA---ARNKAEKLKRDLSEELEA 1169
Cdd:COG2268 297 KEAEREEAELEAdvrKPAEAEKQAAEAEAEAEA 329
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1320-1585 |
2.51e-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: 42.11 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1320 KKGIKLTKDVSSLESQlqdTQELLQEETRQklnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKL 1399
Cdd:pfam15905 66 QKNLKESKDQKELEKE---IRALVQERGEQ----DKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1400 EDDVGALEGLEEVKRKLQKDMEVTS--QKLEEKA-IAFDKLEKTKNRLQQelddLMVDLDHQRQIVSNLEKKQKKFDQML 1476
Cdd:pfam15905 139 ELLKAKFSEDGTQKKMSSLSMELMKlrNKLEAKMkEVMAKQEGMEGKLQV----TQKNLEHSKGKVAQLEEKLVSTEKEK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1477 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtl 1556
Cdd:pfam15905 215 IEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK--- 291
|
250 260
....*....|....*....|....*....
gi 688558694 1557 EQQVEEMRTQLEELEDELQATEDaKLRLE 1585
Cdd:pfam15905 292 EELLREYEEKEQTLNAELEELKE-KLTLE 319
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1147-1364 |
2.78e-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: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1147 ESEKAARNKAEKLKRdlSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNhESQIQEMRQRHGTALEE 1226
Cdd:TIGR00927 637 EAEHTGERTGEEGER--PTEAEGENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEG-EGEIEAKEADHKGETEA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1227 ISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGEL-ADRTHKIQ 1305
Cdd:TIGR00927 713 EEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIqAGEDGEMK 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1306 TElDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1364
Cdd:TIGR00927 793 GD-EGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEK 850
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1065-1197 |
2.80e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1065 EEKTRQELEKAKrKLDAE-TTDLQDQIAELQAqidELKIQLAKKEEELQAVLARGDEEvaqknNALKQLRELQAQLAELQ 1143
Cdd:PTZ00491 642 DERTRDSLQKSV-QLAIEiTTKSQEAAARHQA---ELLEQEARGRLERQKMHDKAKAE-----EQRTKLLELQAESAAVE 712
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1144 ---------------EDLESE---KAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1197
Cdd:PTZ00491 713 ssgqsraealaeaeaRLIEAEaevEQAELRAKALRIEAEAELEKLRKRQELELEYEQAQNELEIAKAKELAD 784
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1020-1183 |
2.82e-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: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1020 KKLLEDRVGEMTSQLAEEEEKAKnlgKVKNKqemmMVDLEERLKKEEKTRQELEKA-KRKLDAETTDL-QDQIAELQAQI 1097
Cdd:cd22656 116 KKTIKALLDDLLKEAKKYQDKAA---KVVDK----LTDFENQTEKDQTALETLEKAlKDLLTDEGGAIaRKEIKDLQKEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1098 DELK----IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLK---RDLSEELEAL 1170
Cdd:cd22656 189 EKLNeeyaAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIG---PAIPALEKLQgawQAIATDLDSL 265
|
170
....*....|...
gi 688558694 1171 KTELEDTLDTTAA 1183
Cdd:cd22656 266 KDLLEDDISKIPA 278
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1507-1635 |
2.86e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1507 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVgknVHELEKSKRTLEQQVEEMRTQLEELEDEL---QATEDAKLR 1583
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQ---VERLEAEVEELEAELEEKDERIERLERELseaRSEERREIR 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1584 LEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAV 1635
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 ... |
1641-1811 |
2.91e-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: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1641 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQ---RELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLAs 1717
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1718 seRARRHAEQE---RDELADEISNSASGKAALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELag 1794
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL-- 200
|
170
....*....|....*..
gi 688558694 1795 ersaaqksENARQQLER 1811
Cdd:pfam00529 201 --------KLAKLDLER 209
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1071-1171 |
3.39e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1071 ELEKAKRKLDAETTDLQ---DQIAELQAQIDELKiQLAKK----EEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1143
Cdd:COG0497 276 ELEEAASELRRYLDSLEfdpERLEEVEERLALLR-RLARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAE 354
|
90 100 110
....*....|....*....|....*....|....
gi 688558694 1144 EDLEsEKAA------RNKAEKLKRDLSEELEALK 1171
Cdd:COG0497 355 AELL-EAAEklsaarKKAAKKLEKAVTAELADLG 387
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1059-1238 |
3.43e-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: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1059 EERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKI------QLAKKEEEL---QAVLARGDEEVaqknnal 1129
Cdd:pfam10168 546 EEYLKKHDLAREEIQKRVKLLKLQK---EQQLQELQSLEEERKSlseraeKLAEKYEEIkdkQEKLMRRCKKV------- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1130 kqLRELQAQLAELqedLESEkaarnkaeklkRDLSEELEALKTELEdTLDttAAQQELRSKREQEVAELKKAIDDETRN- 1208
Cdd:pfam10168 616 --LQRLNSQLPVL---SDAE-----------REMKKELETINEQLK-HLA--NAIKQAKKKMNYQRYQIAKSQSIRKKSs 676
|
170 180 190
....*....|....*....|....*....|....*.
gi 688558694 1209 ------HESQIQEMRQRHGtalEEISEQLEQAKRVK 1238
Cdd:pfam10168 677 lslsekQRKTIKEILKQLG---SEIDELIKQVKDIN 709
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1329-1549 |
3.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1329 VSSLESQLqDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEG 1408
Cdd:PHA02562 190 IDHIQQQI-KTYNKNIEEQRKK---NGENIARKQNKYDELVEEA------KTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1409 LEEVKRKLQKDME----------------VTSQKLEEKAiafDKLEKTKNR---LQQELDDLMVDLDHQRQIVSNLEKKQ 1469
Cdd:PHA02562 260 LNTAAAKIKSKIEqfqkvikmyekggvcpTCTQQISEGP---DRITKIKDKlkeLQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1470 KKFDQMLAEEKTISARYAEERDRAeaeareKDTKALsMARALDEALEAKEEFERLNKQLraemEDLISSKDDVGKNVHEL 1549
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKA------KKVKAA-IEELQAEFVDNAEELAKLQDEL----DKIVKTKSELVKEKYHR 405
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
964-1360 |
4.01e-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: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 964 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVTA----------------------EAKIKKMEEDILLLEDQNSK--FLKE 1019
Cdd:pfam06160 5 RKKIYKEIDELEERKNELMNLPVQEELSKVKKlnltgetqekfeewrkkwddivTKSLPDIEELLFEAEELNDKyrFKKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1020 KKLLEdrvgEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ-------IAE 1092
Cdd:pfam06160 85 KKALD----EIEELLDDIEEDIKQILE----------ELDELLESEEKNREEVEELKDKYRELRKTLLANrfsygpaIDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1093 LQAQIDELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALK- 1171
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTES----GDYLEAR-----EVLEKLEEETDALEELMEDIPPL---YEELKTELPDQLEELKe 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1172 --TELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEK 1243
Cdd:pfam06160 219 gyREMEeegyalEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1244 NKQTLESD-------NKELTNEVKSLQQ----AKSESEHKR------KKLEAQLQEVMARFSEGEKVKGELADRTHKIQT 1306
Cdd:pfam06160 292 NLPEIEDYlehaeeqNKELKEELERVQQsytlNENELERVRglekqlEELEKRYDEIVERLEEKEVAYSELQEELEEILE 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 688558694 1307 ELDNVsclledaEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1360
Cdd:pfam06160 372 QLEEI-------EEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1406-1915 |
4.04e-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: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1406 LEGLEEVKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISAR 1485
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHG----KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1486 YaeerdraeaearekdtkalsmaRALDEALEAKEEFERLNKQLRAEMEDLISSKddvgkNVHELEKSKRTLEQQVEEMRT 1565
Cdd:TIGR00618 245 L----------------------TQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1566 QLEELEDELQATEDAKLRLEVNMQAM-KAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKK---L 1641
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1642 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1721
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1722 RRHAEQERDELADEISNSASGKAALLDEKRRLEARIAqleeELEEEQSNMELLNDRFRKTTMQVdTLNTELAGERSAAQK 1801
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMQR 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1802 SENARQQLERQNKDLKSKLQELE---GSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1878
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510
....*....|....*....|....*....|....*..
gi 688558694 1879 DERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRA 1915
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1020-1202 |
4.47e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1020 KKLLEDRVGEMTSQLAE-EEEKAKNLGKVKnKQEMMMVDLEERLKK-EEKTRQELEKA-----------KRKLDAETTDL 1086
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEaRQALAQVIANQK-RLERQLEELEAEAEKwEEKARLALEKGredlarealerKAELEAQAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1087 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNAlkqlrELQAQLAELQEDLESEKAAR--NKAEKLKRDLS 1164
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-----KAQEKVNEALSGIDSDDATSalERMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 688558694 1165 EELEALKT-ELEDTLDTTAAQQELRSKREQEVAELKKAI 1202
Cdd:COG1842 179 ARAEAAAElAAGDSLDDELAELEADSEVEDELAALKAKM 217
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1018-1174 |
4.93e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1018 KEKKL--LEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKakrkLDAEttdLQDQIAELQA 1095
Cdd:PRK09039 51 KDSALdrLNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERSRLQA----LLAE---LAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688558694 1096 QIDELKIQLAkkeeELQAVLARgdeevaqknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTEL 1174
Cdd:PRK09039 117 RAGELAQELD----SEKQVSAR----------ALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1020-1171 |
5.01e-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: 41.16 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1020 KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD----AETTDLQDQIAELQA 1095
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEdcdpTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1096 QIDELKIQLAKKEEELQAVlargdEEVAQKNNALKQlrELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALK 1171
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 ... |
1646-1750 |
5.16e-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: 38.96 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1646 KDVEAQIEAANKARDEAIKQLrklqaqmKDYQRELEEARTSRDEIFTQSKENEKKLKslEAEILQLQEDLASS-ERARRH 1724
Cdd:cd06503 33 EKIAESLEEAEKAKEEAEELL-------AEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAE 103
|
90 100
....*....|....*....|....*.
gi 688558694 1725 AEQERDELADEISNSASGKAALLDEK 1750
Cdd:cd06503 104 IEQEKEKALAELRKEVADLAVEAAEK 129
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1608-1903 |
5.26e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1608 EKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1687
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1688 DEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKaALLDEKRRLEARIAQLEEELEEE 1767
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1768 QSNMELLNdRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKAsIAALEAKILqlee 1847
Cdd:COG1340 160 EKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK-ADELHEEII---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1848 qleqeakeraAANKIVRRTEKKLKEVFMQVEDERRHADQyKEQMEKANSRMKQLKR 1903
Cdd:COG1340 234 ----------ELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1509-1943 |
5.27e-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: 41.76 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1509 RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELqatedaklrlEVNM 1588
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDEL----------EKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1589 QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQ-RALAVAAKKKLEMDLKDVEA---QIEAANKA--RDEA 1662
Cdd:pfam06160 156 AEIEEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyrEMEEEGYAleHLNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1663 IKQLRKLQAQMKDYQRELEEARTsrdeiftqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1742
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLEL---------DEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1743 KAALLDEKRRLeariaqleeeleeeQSNMELLND---RFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1819
Cdd:pfam06160 307 NKELKEELERV--------------QQSYTLNENeleRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1820 LQELEGSVKsKFKASIAALEakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEdeRRH----ADQYKEQMEKAN 1895
Cdd:pfam06160 373 LEEIEEEQE-EFKESLQSLR--------------KDELEAREKLDEFKLELREIKRLVE--KSNlpglPESYLDYFFDVS 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 688558694 1896 SRMKQLKRQLeeaeeeatraNASR---RKLQRELDDATEASEGLSREVNTL 1943
Cdd:pfam06160 436 DEIEDLADEL----------NEVPlnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1046-1169 |
5.50e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1046 KVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQK 1125
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS---FERLAELRDELAELE-------EELEALKARWEAEKELI 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 688558694 1126 NNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1169
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1539-1702 |
5.56e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1539 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEdaKLRLEVNMQAmkaqfdrdlqardEQNEEKKRALVkqvr 1618
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE--KLKEELEEKK-------------EKLQEEEDKLL---- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1619 emeAELEDERKQRalavaakkklemdlkdveaqIEAANKARDEAIKQLRKLQA---------QMKDYQRELEEARTSRDE 1689
Cdd:PRK00409 569 ---EEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKggyasvkahELIEARKRLNKANEKKEK 625
|
170
....*....|...
gi 688558694 1690 IFTQSKENEKKLK 1702
Cdd:PRK00409 626 KKKKQKEKQEELK 638
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1252-1481 |
5.57e-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: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1252 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG-----EKVKGELADRTHKIQTELDNVSC---------LLED 1317
Cdd:pfam05667 249 LKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSsttdtGLTKGSRFTHTEKLQFTNEAPAAtsspptkveTEEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1318 AEKKGiklTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQlVETKK 1397
Cdd:pfam05667 329 LQQQR---EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEEL--------------EELKEQNEELEKQ-YKVKK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1398 KLeddVGALEGLEEVKRKLQKDMEVTSQKLEE-------------------KAIAFDKLEKTKNRLQ--QELDDLMvdld 1456
Cdd:pfam05667 391 KT---LDLLPDAEENIAKLQALVDASAQRLVElagqwekhrvplieeyralKEAKSNKEDESQRKLEeiKELREKI---- 463
|
250 260
....*....|....*....|....*
gi 688558694 1457 hqRQIVSNLEKKQKKFDQMLAEEKT 1481
Cdd:pfam05667 464 --KEVAEEAKQKEELYKQLVAEYER 486
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1597-1732 |
5.79e-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: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1597 RDLQARDEQNEEKKRALVKQVREMEAELEDERkqralavaakkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1676
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEE----------------IRRLEEQVERLEAEVEELEAELEEKDERIERL 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 688558694 1677 QRELEEARTSRDEiftqSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDEL 1732
Cdd:COG2433 447 ERELSEARSEERR----EIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1069-1171 |
5.90e-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: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1069 RQELEKAKRKLDAETTDLQDQIAELQAQIDELkIQLAKKEEELQAVLArgDEEVAQKNNALKQLRELQAQLAELQEDLES 1148
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAY-AAAQAALATAQKELA--NAQAQALQTAQNNLATAQAALANAEARLAK 336
|
90 100
....*....|....*....|...
gi 688558694 1149 EKAArnkAEKLKRDLSEELEALK 1171
Cdd:TIGR04320 337 AKEA---LANLNADLAKKQAALD 356
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1518-1670 |
6.31e-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: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1518 KEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA--TEDAKLRLEVNMQAMKAQF 1595
Cdd:cd22656 109 DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDllTDEGGAIARKEIKDLQKEL 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1596 DrdlQARDEQNEEKKRALvKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeaankarDEAIKQLRKLQ 1670
Cdd:cd22656 189 E---KLNEEYAAKLKAKI-DELKALIADDEAKLAAALRLIADLTAADTDLDNLLALI-------GPAIPALEKLQ 252
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1488-1737 |
6.50e-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: 40.40 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1488 EERDRAEAEAREKDTKalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKskrtLEQQVEEMRTQL 1567
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEE----AEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1568 EELEDELQATEDAKLRLEVNMQAMKAqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKD 1647
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKE--------IAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1648 V-------EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskenEKKLKSLEAEILQLQEDLASSER 1720
Cdd:pfam00261 153 VgnnlkslEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFA--------------ERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|....*..
gi 688558694 1721 ARRHAEQERDELADEIS 1737
Cdd:pfam00261 219 KYKAISEELDQTLAELN 235
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
1065-1175 |
7.02e-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: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1065 EEKTRQELEKAKRkldaettdlqDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQE 1144
Cdd:pfam16516 1 EELKRKEMEKVYK----------DEIDCLQAQLQAAEEALAAKQREIDEL----KQEIAQKEEDLETISVLKAQAEVYRS 66
|
90 100 110
....*....|....*....|....*....|.
gi 688558694 1145 DLESEKAARNKAEKLKRDLSEELEALKTELE 1175
Cdd:pfam16516 67 DFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
870-1204 |
7.05e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 870 EEEMQAKDEELIKVKERQVKVENELVE--------MERKHQQLLEEKNILAEQLQAETELFAEAEEMRA-RLVAKKQELE 940
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINksineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 941 EILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarqklqlekvtaeakIKKMEEDILLLEDQNSKFLKEK 1020
Cdd:PRK01156 569 SWLNALAVISLIDIETNRSRSNEIKKQLNDL---------------------------ESRLQEIEIGFPDDKSYIDKSI 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1021 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvdleeRLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL 1100
Cdd:PRK01156 622 REIENEANNLNNKYNEIQENKILIEKLRGKID--------NYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1101 KIQLAKKEEELQAVLARgdeevaqknnalkqLRELQAQLAELQEDLESEKaarnKAEKLKRDLSEELEALKTELEDTLDT 1180
Cdd:PRK01156 694 KANRARLESTIEILRTR--------------INELSDRINDINETLESMK----KIKKAIGDLKRLREAFDKSGVPAMIR 755
|
330 340
....*....|....*....|....
gi 688558694 1181 TAAQQELRSKREQEVAELKKAIDD 1204
Cdd:PRK01156 756 KSASQAMTSLTRKYLFEFNLDFDD 779
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1185-1447 |
7.07e-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: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1185 QELRSKREQEVAELK--KAIDDETRN--HESQIQEMRQRHGTA-LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTnEV 1259
Cdd:pfam15905 59 LELKKKSQKNLKESKdqKELEKEIRAlvQERGEQDKRLQALEEeLEKVEAKLNAAVREKTSLSASVASLEKQLLELT-RV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1260 KSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDT 1339
Cdd:pfam15905 138 NELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1340 QELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1419
Cdd:pfam15905 218 KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE 297
|
250 260
....*....|....*....|....*...
gi 688558694 1420 MEVTSQKLEEkaiafdKLEKTKNRLQQE 1447
Cdd:pfam15905 298 YEEKEQTLNA------ELEELKEKLTLE 319
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1553-1707 |
7.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1553 KRTLEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFDRDLQARDEQNEEKKRALVKQVREMEAELED 1626
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1627 ERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE--LEEAR-TSRDEIFTQSKENEKKLKs 1703
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEeEARHEAAVLIKEIEEEAK- 183
|
....
gi 688558694 1704 LEAE 1707
Cdd:PRK12704 184 EEAD 187
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1489-1732 |
7.64e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1489 ERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEmedlisskdDVGKNVHELEKSKRTLEQQVEEmRTQLE 1568
Cdd:COG5022 829 EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYL---------QSAQRVELAERQLQELKIDVKS-ISSLK 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1569 E--LEDELQATEdaklrlevnmqaMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEM-DL 1645
Cdd:COG5022 899 LvnLELESEIIE------------LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVEsKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1646 KDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqsKENEKKLKSLEAEILQLQ--EDLASSERARR 1723
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAL----QESTKQLKELPVEVAELQsaSKIISSESTEL 1042
|
....*....
gi 688558694 1724 HAEQERDEL 1732
Cdd:COG5022 1043 SILKPLQKL 1051
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1215-1536 |
8.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1215 EMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1294
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1295 GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknNLLEQQEEE 1374
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1375 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1454
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1455 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1534
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
..
gi 688558694 1535 LI 1536
Cdd:COG4372 335 LL 336
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
865-1166 |
8.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 865 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 944
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 945 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1024
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1025 DRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQL 1104
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688558694 1105 AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1166
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1052-1282 |
9.56e-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: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1052 EMMMVDLEERLkkeekTRQELEKAKRKLDAETTDlQDQIAELQAQIDELKIQLAKKEEELQAvlargdeevaqknnALKQ 1131
Cdd:pfam05622 274 EIMPAEIREKL-----IRLQHENKMLRLGQEGSY-RERLTELQQLLEDANRRKNELETQNRL--------------ANQR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1132 LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTeledtldttaAQQELRSKREQeVAELKKAIDDETRNHES 1211
Cdd:pfam05622 334 ILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHE----------AQSELQKKKEQ-IEELEPKQDSNLAQKID 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688558694 1212 QIQEMRQRHgtalEEISEQLEQakRVKGNLEKNK---QTLESD-NKELTNEVKSLQQAKSESEHKRKKLEAQLQE 1282
Cdd:pfam05622 403 ELQEALRKK----DEDMKAMEE--RYKKYVEKAKsviKTLDPKqNPASPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1009-1401 |
9.96e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1009 LEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGK-----VKNKQEMMMV---------DLEERLKKEEKTRQELEK 1074
Cdd:PRK10246 535 LEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQeeqalTQQWQAVCASlnitlqpqdDIQPWLDAQEEHERQLRL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1075 AKRKLDaettdLQDQIAELQAQIDELKIQLAKKEEELQAVLAR--------GDEEV------------AQKNNALKQLRE 1134
Cdd:PRK10246 615 LSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqeDEEASwlatrqqeaqswQQRQNELTALQN 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1135 LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEalktelEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQ 1214
Cdd:PRK10246 690 RIQQLTPLLETLPQSDDLPHSEETVALDNWRQVH------EQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVF 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1215 EMRQRHGTAL--EEISEQLEQakrvkgnlekNKQTLESDnkeltnevksLQQAKSESEHKRKKLEAQLQevmarfsegek 1292
Cdd:PRK10246 764 DDQQAFLAALldEETLTQLEQ----------LKQNLENQ----------RQQAQTLVTQTAQALAQHQQ----------- 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1293 vkgeladrthkiqteldnvsclledAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqe 1372
Cdd:PRK10246 813 -------------------------HRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNR-------- 859
|
410 420
....*....|....*....|....*....
gi 688558694 1373 eeeesrknleKQLATLQAQLVETKKKLED 1401
Cdd:PRK10246 860 ----------QQQQALMQQIAQATQQVED 878
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1619-1712 |
9.96e-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: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688558694 1619 EMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLR-KLQAQMKDYQRELEEARTSRDEIFT--QSK 1695
Cdd:cd16269 195 EKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKeKMEEERENLLKEQERALESKLKEQEalLEE 274
|
90
....*....|....*..
gi 688558694 1696 ENEKKLKSLEAEILQLQ 1712
Cdd:cd16269 275 GFKEQAELLQEEIRSLK 291
|
|
| |
