|
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 ... |
851-1931 |
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: 1473.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 851 TRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDL 930
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 931 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR 1010
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1011 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAK 1090
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1091 KEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQE 1170
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1171 LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAK 1250
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1251 SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE 1330
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1331 TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQK 1410
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1411 LEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALS 1490
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1491 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1570
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1571 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQL 1650
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1651 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAL 1730
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1731 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGS 1810
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1811 VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLE 1890
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 528481573 1891 EAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1931
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-774 |
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: 1443.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMSF 341
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 342 NHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQAD 421
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 422 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 501
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 502 YQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCII 581
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 582 HYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYK 661
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 662 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 741
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 528481573 742 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
102-774 |
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: 1318.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP-GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYR-FLSNGNIPIPGQQDKDNFQETMEAMHIM 339
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 340 SFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQ 419
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 420 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQ 499
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 500 EEYQREGIEWSFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTH-GKFQKPRQLKDKADF 578
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKsKNFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 579 CIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgldqvagmnETAFGAAYKTKKGMFRTVGQ 658
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 659 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 738
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 528481573 739 IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-774 |
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: 1243.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP----GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 257
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 258 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMH 337
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 338 IMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTK 417
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 418 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 497
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 498 EQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD 577
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 578 FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGaAYKTKKGMFRTVG 657
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 658 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 737
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 528481573 738 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-774 |
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: 1201.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMSF 341
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 342 NHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQAD 421
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 422 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 501
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 502 YQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCII 581
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 582 HYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYK 661
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 662 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 741
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 528481573 742 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
102-774 |
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: 1193.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMSF 341
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 342 NHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQAD 421
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 422 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 501
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 502 YQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCII 581
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 582 HYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQLYK 661
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 662 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 741
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 528481573 742 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-774 |
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: 1181.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHN----IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 257
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 258 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMH 337
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 338 IMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTK 417
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 418 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 497
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 498 EQEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD 577
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 578 FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNEtaFGAAYKTKKGMFRTVG 657
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 658 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 737
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 528481573 738 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
102-774 |
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: 1162.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASS---------HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 252
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 253 FDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQET 332
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 333 MEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQ 412
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 493 TMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKpRQL 572
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 573 KDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrIVGLDQVAgMNETAFGAayKTKKGM 652
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 653 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 732
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 528481573 733 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-774 |
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: 1151.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQdKDNFQETMEAMHIMSF 341
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 342 NHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQAD 421
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 422 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 501
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 502 YQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKADFCII 581
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 582 HYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAayKTKKGMFRTVGQLYK 661
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 662 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 741
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 528481573 742 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
90-774 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1108.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 90 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 169
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 170 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 249
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA----GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 250 RINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDN 328
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 329 FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGR 408
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 409 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 488
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 489 LFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQK 568
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 569 PRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQvagmNETAFGAAYKT 648
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAA----NESGKSTPKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 649 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 728
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 528481573 729 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
83-786 |
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: 1011.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 83 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 162
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 163 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipGELERQLLQANPILESFGNAKTVKNDNS 242
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 243 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIP 321
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGcLTVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 322 GQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENT-AAQKLCHLLGMNVMEFTRAIL 400
Cdd:smart00242 235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 401 SPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCIN 480
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 481 YTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQ 560
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 561 GTHGKFQKPRQlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqvagmnet 640
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS---------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 641 afGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 720
Cdd:smart00242 534 --GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 721 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRTGVLAHLEEERD 786
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
39-1347 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 917.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 39 VWVPSERHGFEAASIREERGEEVLVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 113
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 114 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 193
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 194 VIQYLAHVASSHkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 273
Cdd:COG5022 172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 274 AIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKV 352
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 353 VSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATY 432
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 433 ERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFI 512
Cdd:COG5022 406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 513 DFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVDKLVQ--EQGTHGKFQKPRQLKDKadFCIIHYAGRVDYK 590
Cdd:COG5022 485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 591 ADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVgldqvagmnetafgaayktKKGMFRTVGQLYKESLTKLMAT 670
Cdd:COG5022 561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 671 LRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA----IPKGFMDG 746
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 747 KQACERMIRALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDIIIYFQSVCRGYLARKAFAKKQQQLSALKVLQRNC 826
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 827 AAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVkerQVKVENELVEMERKHQQLLEEKNILAEQlqaetelF 906
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL---QKTIKREKKLRETEEVEFSLKAEVLIQK-------F 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 907 AEAEEMRARLVAKKQelEEILHDLESRVEEEEERNQSLQNEKKKMQShiqdleeqldeeeAARQKLQLEKVTAEAKIKKM 986
Cdd:COG5022 852 GRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDVKSISS-------------LKLVNLELESEIIELKKSLS 916
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 987 EEDILLLEDQNSKFLKEKKLLEdrvgemTSQLaeEEEKAKNLGKVKNKQEMMMVDleerlKKEEKTRQELEKAKRKLDAE 1066
Cdd:COG5022 917 SDLIENLEFKTELIARLKKLLN------NIDL--EEGPSIEYVKLPELNKLHEVE-----SKLKETSEEYEDLLKKSTIL 983
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1067 TTDLQDQIAELQAQIDElkiqLAKKEEELQAVlargdeevaqkNNALKQLRELQAQLAELQEDLE------SEKAARNKA 1140
Cdd:COG5022 984 VREGNKANSELKNFKKE----LAELSKQYGAL-----------QESTKQLKELPVEVAELQSASKiissesTELSILKPL 1048
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1141 EKLKRD-------LSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR-----QRHGTAL 1208
Cdd:COG5022 1049 QKLKGLlllennqLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQfivaqMIKLNLL 1128
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1209 EEISEQLEQA----KRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEV-MARFSEGEKVKGELAD 1283
Cdd:COG5022 1129 QEISKFLSQLvntlEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKsKLSSSEVNDLKNELIA 1208
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1284 RTHKIQTElDNVSCLLEDAEKKGIKLT------KDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEE 1347
Cdd:COG5022 1209 LFSKIFSG-WPRGDKLKKLISEGWVPTeystslKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKL 1277
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
102-774 |
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: 859.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL-----SNGNIPIPGQQDKDNFQETMEA 335
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 336 MHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNT--DQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQK 413
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 414 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 493 TMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQL 572
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 573 KDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkdvdrivgldqvagmnetafgaayktkkgm 652
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 653 frtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 732
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 528481573 733 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
102-774 |
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: 778.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVA------SSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 255
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 256 TGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNFQETM 333
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 334 EAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQK 413
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 414 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 493
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 494 MFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPR-- 570
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 571 -QLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdriVGLDQVAgmnETAFGAAYKTK 649
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDSTE---DPKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 650 KGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 728
Cdd:cd14927 550 KAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 528481573 729 QRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
103-774 |
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: 769.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSH--KGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQDKDNFQETMEAMHI 338
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 339 MSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKE 418
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 419 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILE 498
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 499 QEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKPRQLKDKAD 577
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 578 --FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqVAGMNETAFGAAYKTKKG-MFR 654
Cdd:cd14913 477 ahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FATADADSGKKKVAKKKGsSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 655 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 734
Cdd:cd14913 548 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 528481573 735 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14913 628 NASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
102-774 |
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: 750.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQA 420
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 421 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQE 500
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 501 EYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPRQLK---DKA 576
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 577 DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivGLDQVAGMNETAFGAAykTKKGMFRTV 656
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAKGGRG--KKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 657 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 736
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 528481573 737 NAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
102-774 |
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: 729.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHL-RSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQA 420
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 421 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQE 500
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 501 EYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPRQLKDK---A 576
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 577 DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqvagmnETAFGAAYKTKKGM-FRT 655
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 656 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 735
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 528481573 736 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
103-774 |
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: 721.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGrkDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ETQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP-IPGQQDKDNFQETMEAMHIMS 340
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQA 420
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 421 DFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQ 499
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 500 EEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK--FQKPRQLKDKad 577
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 578 FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKfvaelwkdvdrivgldqvagmnetafgaayktKKgmfrTVG 657
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------------KK----TVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 658 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 737
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS 593
|
650 660 670
....*....|....*....|....*....|....*..
gi 528481573 738 AIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd01380 594 KEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
102-774 |
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: 708.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNFQETMEAMHIM 339
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE-LR-DLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 340 SFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQ 419
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 420 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQ 499
Cdd:cd14929 316 VTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 500 EEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPRQLKDK--A 576
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 577 DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivglDQVAGmNETAFGAAYKTKKGMFRTV 656
Cdd:cd14929 472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAIQFGEKKRKKGASFQTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 657 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 736
Cdd:cd14929 544 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 528481573 737 NAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14929 624 RTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
103-774 |
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: 707.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNFQETMEAMHI 338
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELL-DMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 339 MSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKE 418
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 419 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILE 498
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 499 QEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPRQLKDK-- 575
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKpe 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 576 ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivgldqVAGMNETAFGAAYKTKKG-MFR 654
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAPIEKGKGKAKKGsSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 655 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 734
Cdd:cd14917 548 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 528481573 735 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14917 628 NPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
104-774 |
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: 690.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 183
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 184 GAGKTENTKKVIQYLAHVASSHKGRKDHN--IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQA 420
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 421 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQE 500
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 501 EYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKPRQLKDKAD-- 577
Cdd:cd14918 402 EYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEah 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 578 FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdrivgldqVAGMNETAFGAAYKTKKGMFRTVG 657
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 658 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 737
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 528481573 738 AIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14918 631 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
103-774 |
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: 689.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 258
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 259 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMH 337
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 338 IMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTK 417
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 418 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 497
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 498 EQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKPRQLKDKA 576
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKGKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 577 D--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagmnETAFGAAYK--TKKG- 651
Cdd:cd14912 478 EahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG--------ASAGGGAKKggKKKGs 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 652 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 731
Cdd:cd14912 550 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 528481573 732 EILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14912 630 KVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
103-774 |
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: 689.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVAS-SHKGRKD--HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 259
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 260 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsDLLLEGFN--SYRFLSNGNIPIPGQQDKDNFQETMEAMH 337
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELL-DMLLVTNNpyDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 338 IMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTK 417
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 418 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 497
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 498 EQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPRQLKDK- 575
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGKq 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 576 -ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdrivgldQVAGMNETAFGAAYKTKKGMFR 654
Cdd:cd14916 477 eAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSSFQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 655 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 734
Cdd:cd14916 550 TVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 528481573 735 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14916 630 NPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
103-774 |
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: 684.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 258
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 259 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMH 337
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 338 IMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTK 417
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 418 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 497
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 498 EQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPRQLKDK- 575
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGKv 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 576 -ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdrivgldqVAGMNETAFGAAYKTKKG-MF 653
Cdd:cd14910 478 eAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGKKKGsSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 654 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 733
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 528481573 734 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14910 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-774 |
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: 681.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHN---IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 260 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYR--FLSNGNIPIPGQQDKDNFQETMEAMH 337
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 338 IMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTK 417
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 418 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 497
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 498 EQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLV-QEQGTHGKFQKPRQLKDKA 576
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGKA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 577 D--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVdriVGLDQVAGMNETAFGaayKTKKGMFR 654
Cdd:cd14923 477 EahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---KKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 655 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 734
Cdd:cd14923 551 TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 528481573 735 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14923 631 NASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
103-774 |
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: 674.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 258
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEaasgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 259 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLrSDLLLEGFNSYRF--LSNGNIPIPGQQDKDNFQETMEAM 336
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 337 HIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQT 416
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 417 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 496
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 497 LEQEEYQREGIEWSFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQ-GTHGKFQKPRQLKDK 575
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 576 AD--FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivglDQVAGMNETAFGAAYKTKKGMF 653
Cdd:cd14915 477 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 654 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 733
Cdd:cd14915 550 QTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 528481573 734 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14915 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
103-774 |
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: 649.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 262
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 263 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--HLRSDLLLEGFNSYRFLS-NGNIPIPGQQDKDNFQETMEAMHIM 339
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 340 SFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK-LCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKE 418
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKiVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 419 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILE 498
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 499 QEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKADF 578
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 579 CIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrIVGLDQVAGMNETAfGAAYKTKKGMfRTVGQ 658
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD-TTSRGTSKGK-PTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 659 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 738
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 528481573 739 IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14883 626 RSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
103-774 |
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: 643.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 262
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 263 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQETMEAMHIMSF 341
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 342 NHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQAD 421
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 422 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 501
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 502 YQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlkDKAdFCII 581
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER---GGA-FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 582 HYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdrivgldqVAGMNETAFGAAYKTKKGMF----RTVG 657
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF------------ASKMLDASRKALPLTKASGSdsqkQSVA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 658 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 737
Cdd:cd01383 532 TKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPE 611
|
650 660 670
....*....|....*....|....*....|....*..
gi 528481573 738 AIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd01383 612 DV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
103-774 |
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: 638.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSHKGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 262
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER-----VKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 263 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQETMEAMHIMSF 341
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 342 NHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVG---RDYVQKAQTKE 418
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 419 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILE 498
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 499 QEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVDKLVQEQGTHGKFQKPRQLKD--K 575
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 576 ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgldqvagmnetafgaayKTKKGMFRT 655
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 656 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 735
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 528481573 736 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
102-774 |
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: 614.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAHVA--SSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGgrAVTEGRS-------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 259 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQETMEAMH 337
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 338 IMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAILSpRIKVGRD-YVQK 413
Cdd:cd01384 234 VVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIVTPDgIITK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 414 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 493
Cdd:cd01384 313 PLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 494 MFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlK 573
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--L 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 574 DKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgldqvagmnetafgaaYKTKKGM- 652
Cdd:cd01384 467 SRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------------EGTSSSSk 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 653 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 732
Cdd:cd01384 529 FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFG 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 528481573 733 ILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 774
Cdd:cd01384 609 LLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
102-774 |
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: 611.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKK--ERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKE 418
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 419 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 496
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 497 LEQEEYQREGIEWSFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDK 575
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 576 AdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkDVDRIVGLDqvagmnetafgAAYKTKkgmfrT 655
Cdd:cd01381 468 S-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TRKKSP-----T 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 656 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 735
Cdd:cd01381 530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 528481573 736 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd01381 610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
102-774 |
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: 573.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLegfnsyrflsngnipIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKKERNT-------DQASMPENTAAQKlchLLGMNVMEF-----TRAILSPRIKVGR 408
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 409 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 488
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 489 LFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQK 568
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 569 PRQ--------LKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagmnet 640
Cdd:cd01382 450 PRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 641 afGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 720
Cdd:cd01382 520 --DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 528481573 721 RIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd01382 598 RTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
102-774 |
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: 570.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGfnSYRFLSNGN-IPIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA--AYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCH---LLGMNVMEFTRAILSPRIKV-GRDYVQKAQT 416
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIkGCDPTRIPLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 417 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 496
Cdd:cd14872 310 PAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 497 LEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKA 576
Cdd:cd14872 390 LEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 577 DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrivgLDQvagmnetafgaayKTKKGmfrTV 656
Cdd:cd14872 467 EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQ-------------KTSKV---TL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 657 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtP 736
Cdd:cd14872 527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-V 605
|
650 660 670
....*....|....*....|....*....|....*....
gi 528481573 737 NAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14872 606 KTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
102-774 |
1.08e-174 |
|
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: 546.66 E-value: 1.08e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHkgrkdhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 261
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG-NIPIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ---ASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTK 417
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 418 EQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 497
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 498 EQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQlkDKAD 577
Cdd:cd01387 391 EQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 578 FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNetafgAAYKTKKGMFRTVG 657
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGK-----GRFVTMKPRTPTVA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 658 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 737
Cdd:cd01387 541 ARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL 620
|
650 660 670
....*....|....*....|....*....|....*...
gi 528481573 738 AIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 774
Cdd:cd01387 621 KLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
102-774 |
1.74e-174 |
|
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: 546.30 E-value: 1.74e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 176
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 177 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFG 246
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGeaaseaieqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 247 KFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDK 326
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 327 DNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKErntDQASMPEN-TAAQKLCH---LLGMNVMEFTRAILSP 402
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE---NDTTVLEDaTTLQSLKLaaeLLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 403 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYT 482
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 483 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVDKLVQE 559
Cdd:cd14890 397 NEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHAS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 560 QGT-------------HGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvaelwkdvd 626
Cdd:cd14890 475 FGRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 627 rivgldqvagmnetafgaayKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNG 706
Cdd:cd14890 542 --------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSG 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 707 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14890 600 MMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
102-774 |
6.07e-170 |
|
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: 533.97 E-value: 6.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRsdLLLEGFNSYRFL-SNGNIPIPGQQDKDNFQETMEAMHIM 339
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 340 SFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASM--PENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTK 417
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 418 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 497
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 498 EQEEYQREGIEWSFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKLVqeqGTHGKFQK----PRqlK 573
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPR--T 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 574 DKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrIVGLDQVAGMNETAFGAAYKTKKGMF 653
Cdd:cd14903 461 SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 654 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 733
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 528481573 734 LTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 774
Cdd:cd14903 618 FLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-774 |
4.23e-167 |
|
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: 527.33 E-value: 4.23e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLahVASSHKGrkdHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG--SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKKER-NTDQASMPENTAAQKL-CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKE 418
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 419 QADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 494
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 495 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPrQLKD 574
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 575 KAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdriVGLDQVA----GMNETAFGAAY---- 646
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAvfrwAVLRAFFRAMAafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 647 ----------------------------KTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLV 698
Cdd:cd01385 541 agrrraqrtaghsltlhdrttksllhlhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELV 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 699 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd01385 619 LRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
102-772 |
7.60e-164 |
|
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: 517.42 E-value: 7.60e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 173
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 174 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 252 NFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL--SNGNIPIPGQQDKDNF 329
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 330 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-KKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGR 408
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 409 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 487
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 488 QLFNHTMFILEQEEYQREGIEWSFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTH 563
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 564 GKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdvdrivgldqvagmnetafg 643
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 644 aayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 723
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 724 FQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrIGQSKIF 772
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
102-774 |
2.10e-163 |
|
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: 515.88 E-value: 2.10e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLS-NGNIPIPGQQDKDNFQETMEAMHIM 339
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 340 SFNHEEILSMLKVVSAVLQFGNIVFKkerNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQ 419
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 420 ADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILE 498
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 499 QEEYQREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDkaDF 578
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 579 CIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrivgldqvAGMNETAFGAAYKTKKgmfRTVGQ 658
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSKHRR---PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 659 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 738
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 528481573 739 IPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
103-774 |
3.32e-163 |
|
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: 514.52 E-value: 3.32e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVAsshkgrKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 262
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG------KANN--RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 263 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGagehLRSDLLLEGFNS-------YRFLSNGNIPIPGQQD--KDNFQETM 333
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKLpenkpprYLQNDGLTVQDIVNNSgnREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 334 EAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENTAA-QKLCHLLGMNVMEFTRAILSPRIKVGRD 409
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEALTSHSVVTRGE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQ 487
Cdd:cd01379 310 TIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 488 QLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVDKLvqEQGTHGKF 566
Cdd:cd01379 390 YYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF--HNNIKSKY 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 567 QKpRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAElwkdvdrivgldqvagmnetafgaay 646
Cdd:cd01379 464 YW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 647 ktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 726
Cdd:cd01379 517 --------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFAD 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481573 727 FRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 774
Cdd:cd01379 589 FLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
102-736 |
7.81e-163 |
|
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: 515.01 E-value: 7.81e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVT---- 256
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 257 -----GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIP------------ 319
Cdd:cd14888 155 msgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 320 ------------IPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKL--- 384
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 385 CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIA 464
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 465 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWF 544
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 545 PKATDKTFVDKLVQEQGTHGKFQKPRqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKD 624
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 625 -VDRIVGLdqvagmnetafgaayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 703
Cdd:cd14888 550 yLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|...
gi 528481573 704 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 736
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
102-774 |
6.82e-161 |
|
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: 509.30 E-value: 6.82e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 174
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 175 QSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 250
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 251 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPGQQDKDNF 329
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 330 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQ----ASMPENTAAQKLCHLLGMNVMEFTRAILSPRIK 405
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 406 VGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIFQLNSFE 475
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 476 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KATDKTFVD 554
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 555 KLVQEQ-GTHGKFQKPRQLKDkaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkdvdrivgldq 633
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 634 vagmnetafgaayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRI 713
Cdd:cd14892 536 -------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 714 CRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELDPNLYRIGQSKIFFR 774
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-774 |
4.10e-159 |
|
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: 503.45 E-value: 4.10e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAHVASShkgrkdhnIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS--------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQD-------KDNFQETM 333
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 334 EAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQK 413
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 414 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 489
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 490 FNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKP 569
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 570 rqLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdvdrivgldqvagmnetafgaayktk 649
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 650 kgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 729
Cdd:cd14897 522 --------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 528481573 730 RYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 774
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
103-734 |
1.26e-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: 463.24 E-value: 1.26e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 168
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 169 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHV------ASSHKGRKDHNIPGelerQLLQANPILESFGNAKTVKND 240
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSGIAA----KVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 241 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEhlrsdlllegfnsyrflsngnipi 320
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE------------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 321 pGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPENTAAQKL------CHLLGMNVM 393
Cdd:cd14900 214 -AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 394 EFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAGFEIF 469
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 470 QLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATD 549
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 550 KTFVDKLVQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDplndnvatLLHQSTdkfvaelwkdVDriv 629
Cdd:cd14900 450 TTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD--- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 630 gldqvagmnetafgaayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 709
Cdd:cd14900 509 ----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660
....*....|....*....|....*
gi 528481573 710 GIRICRQGFPNRIVFQEFRQRYEIL 734
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
104-774 |
4.59e-143 |
|
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: 460.14 E-value: 4.59e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 104 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 179
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 180 TGESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYI 259
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 260 VGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN--GNIPIPgQQDKDNFQETMEAMH 337
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNgaGCKREV-QYWKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 338 IMSFNHEEILSMLKVVSAVLQFGNIVFkkERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKA 414
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKTLTCTVTFTRGEQIQRH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 415 QTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14889 310 HTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 493 TMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQL 572
Cdd:cd14889 390 HIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 573 KDKadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWK-DVDRIVGLDQVAGM---NETAFGAAYKt 648
Cdd:cd14889 467 SPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLpqaGSDNFNSTRK- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 649 kkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 728
Cdd:cd14889 544 -----QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFA 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481573 729 QRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 774
Cdd:cd14889 619 ERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-737 |
3.13e-140 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 452.56 E-value: 3.13e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 172
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 173 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE-----------LERQLLQANPILESFGNAKTVKNDN 241
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 242 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLE----GFNSYRFLSNG 316
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 317 NIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFK-KERNTDQASMPENTAA-QKLCHLLGMNVME 394
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 395 FTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 467
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 468 IFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WSFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 545
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 546 KATDKTFVDKLVQEQGTHGKFQKPRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWkdv 625
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 626 driVGLDQVAGMNETAFGAAYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 705
Cdd:cd14907 554 ---SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 528481573 706 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 737
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
102-774 |
1.81e-138 |
|
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: 446.80 E-value: 1.81e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 174
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 175 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGRKDHNI--------PGELERQLLQANPILESFGNAKTVKNDNSSR 244
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQsskkrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 245 FGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN-IPIPG 322
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGcVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 323 QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQK----LCHLLGMNVMEFTRA 398
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEalatAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 399 ILSPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFQL-NSFEQ 476
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 477 LCINYTNEKLQQLFNHTMFILEQEEYQREGIE-----WSfidfglDLQPCIDLIErpANPPGVLALLDEECWFPKATDKT 551
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 552 FVDKLVQEQGTHGKFQKPRQlKDKAD-FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQStDKFvaelwkdvdrivg 630
Cdd:cd14891 466 LNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-AKF------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 631 LDQVAGMNEtafgaayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEG 710
Cdd:cd14891 531 SDQMQELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQT 580
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 711 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14891 581 CEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
102-774 |
4.20e-137 |
|
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: 443.07 E-value: 4.20e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 261
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL-----RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI-PIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVFKKERNTDQ--ASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKE 418
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 419 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFIL 497
Cdd:cd14896 312 GAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 498 EQEEYQREGIEWSFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQlkDKAD 577
Cdd:cd14896 392 EEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLPV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 578 FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGmnetafgaayktkkgmfrTVG 657
Cdd:cd14896 467 FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------------TLA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 658 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpN 737
Cdd:cd14896 529 SRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-S 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 528481573 738 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14896 608 ERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
102-774 |
2.24e-136 |
|
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: 441.30 E-value: 2.24e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFL--SNGNIPIPGQQDKDNFQETMEAMHI 338
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 339 MSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASmpenTAAQKLCHLLGMNVMEFTR--AILSPRIKVGR-DYVQKAQ 415
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRI----SNGSQLSQVAKMLGLPTTRieEALCNRSVVTRnESVTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 416 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 495
Cdd:cd14904 309 APVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 496 ILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVDKL---VQEQGTHGKFQKPRQl 572
Cdd:cd14904 389 KTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 573 kDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDrivgldqvaGMNETAFGAAYKTKKGM 652
Cdd:cd14904 464 -KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKAP 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 653 fRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 732
Cdd:cd14904 534 -KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYA 612
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481573 733 ILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 774
Cdd:cd14904 613 IMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
102-774 |
3.66e-133 |
|
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: 433.57 E-value: 3.66e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 171
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 172 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE---LERQLLQANPILESFGNAKTVKNDNSSRFGKF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 249 IRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGE--------HLRSDLLLEGFNSYRFLSNGNIPI 320
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 321 PGQ-QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPE---NTAAQKLCHLLGMNVMEFT 396
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 397 RAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFEIFQLNSF 474
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 475 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFV 553
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 554 DKLV--------QEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLM-KNMDPLNdnvatllhqstdkfvaelwkd 624
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 625 vdrivgldqvagmnetafgaayKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRC 704
Cdd:cd14908 536 ----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 705 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQACERMIRALELDPNL---- 763
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSMKNIpedt 671
|
730
....*....|.
gi 528481573 764 YRIGQSKIFFR 774
Cdd:cd14908 672 MQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
102-736 |
7.74e-133 |
|
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: 433.55 E-value: 7.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 171
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 172 REDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 250
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 251 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN---GNIPIPGQQDKD 327
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 328 N--FQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKE-RNTDQASMPENTAAQ--KLCHLLGMNVMEFTRAILSP 402
Cdd:cd14902 241 AqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 403 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAGFEIFQLNSF 474
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 475 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVD 554
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 555 KLVQEQGTHGKfqkprqlkdkadFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDkfvaelwkDVDRIVGLDQV 634
Cdd:cd14902 478 KFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 635 AGMNETAFGAAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 712
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660
....*....|....*....|....
gi 528481573 713 ICRQGFPNRIVFQEFRQRYEILTP 736
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
100-827 |
1.07e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 425.60 E-value: 1.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 100 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 179 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 258
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 259 IVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHI 338
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 339 MSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASM--PENTAA-QKLCHLLGMNVMEFTRAILSPRIKVGRDYVQK 413
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 414 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 493
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 494 MFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLK 573
Cdd:PTZ00014 500 VFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDS 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 574 DKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagmnetafgaayKTKKGMF 653
Cdd:PTZ00014 577 NK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQL 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 654 rtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 733
Cdd:PTZ00014 640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 734 LTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFF-RTGV--LAHLEEERDLKITDIIIYFQSVCRGYLARKAFA 810
Cdd:PTZ00014 718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkKDAAkeLTQIQREKLAAWEPLVSVLEALILKIKKKRKVR 797
|
730
....*....|....*..
gi 528481573 811 KKqqqlsaLKVLQRNCA 827
Cdd:PTZ00014 798 KN------IKSLVRIQA 808
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
103-735 |
3.18e-128 |
|
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: 420.13 E-value: 3.18e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 170
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 171 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGElerQLLQANPILESFGNAKTVKNDNSSR 244
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 245 FGKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNS--YRFLSNGN 317
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAqeFQYISGGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 318 IPI--PGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTD---------------QASMPENTA 380
Cdd:cd14895 232 CYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 381 AQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK------ 451
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 452 ----RQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPCIDLIEr 527
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 528 pANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRqlKDKAD--FCIIHYAGRVDYKADEWLMKNMDPLNDN 605
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 606 VATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKGmfrtVGQLYKESLTKLMATLRNTNPNFVRCIIPN 685
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYIRCIKPN 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 528481573 686 HEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 735
Cdd:cd14895 623 DESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-774 |
5.36e-127 |
|
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: 416.33 E-value: 5.36e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnipgeLERQLLQA-NPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV--------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSyrflSNGNIPIPGQQDKD------NFQETME 334
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDkqkaaaAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 335 AMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAI------------LSP 402
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 403 RIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGfeiFQLN---------S 473
Cdd:cd01386 309 SGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPG---FQNPahsgsqrgaT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 474 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERP---ANPP---------GVLALLDEE 541
Cdd:cd01386 385 FEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 542 CWFPKATDKTFVDKLVQEQG--THGKFQKPRQLKDKA-DFCIIHYAGR--VDYKADEWLMK-NMDPLNDNVATLLHQSTD 615
Cdd:cd01386 465 ALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 616 KFvaelwkdvdrivgldqvagmnetafgAAYKtKKGMFRTVgqlyKESLTKLMATLRNTNPNFVRCIIPNHEkrAGKLEP 695
Cdd:cd01386 545 ET--------------------------AAVK-RKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHN--AGKDER 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 696 H--------------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACERMIRA 756
Cdd:cd01386 592 StsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEE 671
|
730
....*....|....*...
gi 528481573 757 LELDPNLYRIGQSKIFFR 774
Cdd:cd01386 672 LDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
102-772 |
1.05e-125 |
|
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: 410.92 E-value: 1.05e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 180
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMS 340
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 341 FNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMPENTAAQKL---CHLLGMNVMEFTRAILSPRIKVGRDYVQKAQ 415
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 416 TKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 494
Cdd:cd14876 314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 495 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFqKPRQLKD 574
Cdd:cd14876 392 FERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKVDS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 575 KADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGldqvagmnetafgaayKTKKGMFr 654
Cdd:cd14876 468 NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------KIAKGSL- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 655 tVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 734
Cdd:cd14876 531 -IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
650 660 670
....*....|....*....|....*....|....*...
gi 528481573 735 TPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 772
Cdd:cd14876 610 DLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-736 |
1.21e-120 |
|
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: 396.91 E-value: 1.21e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 177
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 178 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 257
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 258 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIpgqqDKDNFQETMEAMH 337
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 338 IMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTA---AQKLCHLLGMNVMEFTRAILSPRIKVGRDYV--Q 412
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 413 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 492
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 493 TMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQL 572
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 573 KDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLDQVAGMNETAfgaayktkkgm 652
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAP----------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 653 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 732
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
....
gi 528481573 733 ILTP 736
Cdd:cd14880 623 LLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-737 |
1.15e-118 |
|
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: 393.58 E-value: 1.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 179
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 180 TGESGAGKTENTKKVIQYLAHVASS--HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 257
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 258 YIV-GANIETYLLEKSR-AIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEG-FNSYRFL--------------SNGNIPI 320
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 321 PGQQDKD-NFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQAS--MPENTAA-QKLCHLLGMNVMEFT 396
Cdd:cd14906 241 NNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 397 RAILSPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQGASFIGILDIA 464
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 465 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPANppGVLALLDEECWF 544
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 545 PKATDKTFVDKLVQE-QGTHGKFQkpRQLKdKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWK 623
Cdd:cd14906 478 PKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 624 dvdrivgldqvagMNETAFGAAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLR 703
Cdd:cd14906 555 -------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLR 620
|
650 660 670
....*....|....*....|....*....|....
gi 528481573 704 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 737
Cdd:cd14906 621 NVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
102-774 |
4.98e-114 |
|
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: 377.69 E-value: 4.98e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 176 SILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 255
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 256 TGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNI-PIPGQQDKDNFQETME 334
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 335 AMHIMsFNHEEILSMLKVVSAVLQFGNIVFKKERN--TDQASMPENTAA-QKLCHLLGMNVMEFTRAILSPRIKVGRDYV 411
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 412 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 488
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLLINYANERLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 489 LFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVdklvqeQGTHGKFQK 568
Cdd:cd14886 388 YFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFT------SSCKSKIKN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 569 PRQLKDKA---DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIVGLdqvagmnetafgaa 645
Cdd:cd14886 459 NSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 646 yktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 725
Cdd:cd14886 525 ---MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFE 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 528481573 726 EFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14886 600 EFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-774 |
1.87e-112 |
|
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: 373.76 E-value: 1.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 178
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 179 CTGESGAGKTENTKKVIQYLAHVASSHKGR-KDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFD-VT 256
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 257 GYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDL-LLEGFNSYRFLSNGNI----PIPGQ--QDKDNF 329
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 330 QETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNtDQASMPENTAAQKLCHLLGMNVMEFTRAILsprIKVGRD 409
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 488
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 489 LFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGK-FQ 567
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPyFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 568 KPRQLKDKaDFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdrivgLDQVAGMNETAfgaayk 647
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LSTEKGLARRK------ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 648 tkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 727
Cdd:cd14875 538 ------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 528481573 728 RQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSKIFFR 774
Cdd:cd14875 612 CRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
102-731 |
1.52e-104 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 352.86 E-value: 1.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 170
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 171 DREDQSILCTGESGAGKTENTKKVIQYLA-------HVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDN 241
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 242 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-----AGEHLRSDLLLEGFNSYRFLSN 315
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 316 G--NIPIPGQQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF-----KKERNT--DQASMPENTAA----- 381
Cdd:cd14899 241 SlcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 382 QKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT----------- 450
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 451 ---KRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIER 527
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 528 paNPPGVLALLDEECWFPKATDKTFVDKL---VQEQGTHGKFQKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLND 604
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 605 NVATLLHQSTDKFVAELWK-DVDRIVGLDQVAGMNETAFGAAYKTKKGMFrTVGQLYKESLTKLMATLRNTNPNFVRCII 683
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAgSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 528481573 684 PNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 731
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
102-774 |
2.90e-97 |
|
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: 331.61 E-value: 2.90e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 173
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 174 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 254 DVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLL-EGFnsyrflsngnipiPGQQDKDNFQET 332
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGD-------------PESTDLRRITAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 333 MEAMHIMSFNHEEIlsmLKVVSAVLQFGNIVFKKERNTDQASMPENTA--------AQKLCHLL-------GMNVMEFTR 397
Cdd:cd14887 224 MKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 398 AILS--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR----- 452
Cdd:cd14887 301 KHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesd 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 453 --------QGASFIGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREG--IEWSFIDFGLDLQ 519
Cdd:cd14887 381 sdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFPFSFP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 520 PCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVDKLVQ--EQGTHGKFQKPR 570
Cdd:cd14887 461 LASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKniINSAKYKNITPA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 571 QLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLhQSTDKFVaelwkdvdRIVGLDQVAGMNetafgaAYKTKK 650
Cdd:cd14887 541 LSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGVR------AISSRR 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 651 gmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 730
Cdd:cd14887 606 ---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRR 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 528481573 731 YEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14887 683 YETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
103-738 |
1.43e-96 |
|
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: 324.93 E-value: 1.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 182
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvtGYIVGA 262
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT---------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 263 NIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLlegfNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMSFN 342
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKYKMTCSAMKSLGIANFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 343 HEEILSMlkvvsAVLQFGNIVFKKERNTDQASmpeNTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADF 422
Cdd:cd14898 223 SIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 423 AVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 502
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 503 QREGIEWSFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVDKLvqeqgthGKFQKPRqLKDKADFCII- 581
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-INTKARDKIKv 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 582 -HYAGRVDYKADEWLMKNMDplndnvatllhqstdkfvaelwkdvdrivgldqvaGMNETAFGAAYKTKKGMFRTVGQLY 660
Cdd:cd14898 440 sHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDEGSKEDLVKYF 484
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 661 KESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 738
Cdd:cd14898 485 KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
99-773 |
6.26e-95 |
|
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: 322.19 E-value: 6.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 99 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 168
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 169 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGK 247
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 248 FIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGN----IPIPGQ 323
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGchplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 324 QDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF--KKERNTDQASMpENTAA-QKLCHLLGMNVMEFtRAIL 400
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 401 SPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGfeiFQL---- 471
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPG---FQNrsst 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 472 --NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIERPanPPGVLALLDEEC-WFPKAT 548
Cdd:cd14879 383 ggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTrRMPKKT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 549 DKTFVDKLVQEQGTHGKFQKPRQLKDKAD---FCIIHYAGRVDYKADEWLMKNMDPLndnvatllhqSTDkFVAelwkdv 625
Cdd:cd14879 460 DEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN------ 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 626 drivgldqvagmnetafgaayktkkgMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCN 705
Cdd:cd14879 523 --------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSL 575
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 706 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMIRALELDPNLYRIGQSKIFF 773
Cdd:cd14879 576 GLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
102-774 |
7.67e-92 |
|
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: 313.68 E-value: 7.67e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 178
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 179 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTG 257
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 258 YIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNG----NIPIPGQQDKDNFQETM 333
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredVSTAERSLNREKLAVLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 334 EAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQK 413
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 414 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 490
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 491 NHTMFILEQEEYQREGIewsfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATDKTFVDKL--- 556
Cdd:cd14878 393 NEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLqsl 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 557 VQEQGTHGKFQKPRQ------LKDK-ADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELwkdvdriv 629
Cdd:cd14878 460 LESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 630 gldqvagmnetafgaaYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLE 709
Cdd:cd14878 532 ----------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLE 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 710 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALELDPNL--YRIGQSKIFFR 774
Cdd:cd14878 593 MVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVLQQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-774 |
5.21e-89 |
|
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: 305.02 E-value: 5.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAhvasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 261
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 262 ANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIMSF 341
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 342 nHEEILSMLKVVSAVLQFGNIVFK---KERNTDQASMPENT--AAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQT 416
Cdd:cd14937 228 -HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 417 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 496
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 497 LEQEEYQREGIEWSFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKa 576
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 577 DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRIvglDQVAGMNETAFGaayktkkgmfrtv 656
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVS---ESLGRKNLITFK------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 657 gqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEILTP 736
Cdd:cd14937 525 ---YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDY 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 528481573 737 NAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 774
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
102-726 |
6.04e-81 |
|
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: 282.57 E-value: 6.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 173
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 174 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 253
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT---ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 254 D---------VTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAG-AGEHLRSDLLLEGFNSYRFLSN-------- 315
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 316 --GNIPIPG----------QQDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKerntdqasmpentaaqk 383
Cdd:cd14884 234 vkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 384 LCHLLGMNVMEFTRAILSPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-------- 455
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 456 ---SFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIDLIERpanpp 532
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 533 gVLALLDE-----ECWFPKATDKTFVD-------KLVQEQGTHGK-------FQKPRQLKDKADFCIIHYAGRVDYKADE 593
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRYllnnerqQQLEGKVSYGFvlnhdadGTAKKQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 594 WLMKNMDPLNDNVATLLHQSTDKFVAElwkdvdrivgldqvagmnetafgAAYKTKKGMFRTVGQLYKESLTKLMATLRN 673
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 528481573 674 TNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 726
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
103-761 |
1.87e-76 |
|
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: 267.75 E-value: 1.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 175
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 176 SILCTGESGAGKTENTKKVIQYLAHVASshkgrkdhnipGELE----RQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 251
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG-----------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 252 NFdVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFN--SYRFLSNGNIPIPGQQDKDNF 329
Cdd:cd14881 139 QV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 330 QETMEAMHIMSFnheEILSMLKVVSAVLQFGNIVFkKERNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRD 409
Cdd:cd14881 218 QAWKACLGILGI---PFLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 410 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFQLNSFEQLCINY 481
Cdd:cd14881 294 LVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 482 TNEKLQQLFNHTMFILEQEEYQREGIEWSF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDKTFVDKLVQEQ 560
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQH 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 561 GTHGKFQKPRQLKDKAdFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTdkfvaelwkdvdrivgldqvagmneT 640
Cdd:cd14881 446 RQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-------------------------C 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 641 AFGaayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPN 720
Cdd:cd14881 500 NFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPH 570
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 528481573 721 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 761
Cdd:cd14881 571 RMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
105-773 |
6.15e-72 |
|
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: 257.59 E-value: 6.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 105 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 174
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 175 QSILCTGESGAGKTENTKKVIQYLAHVASS----HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 250
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 251 INFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAgEH---LRSDLLL-EGFNSYRFLSN-----GNIPIp 321
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadplaTNFAL- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 322 gqqDKDNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVF------KKERN-------TDQASMPENTAAQKL--CH 386
Cdd:cd14893 242 ---DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGgansttvSDAQSCALKDPAQILlaAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 387 LLGMNVMEF-----TRAILSpriKVGRDYVQ--KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQG- 454
Cdd:cd14893 319 LLEVEPVVLdnyfrTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNi 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 455 ---ASFIGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWSFIDFGLDLQPCI 522
Cdd:cd14893 396 vinSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 523 DLIERPanPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQLKDKAD------------FCIIHYAGRVDYK 590
Cdd:cd14893 476 QLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYN 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 591 ADEWLMKNMDPLNDNVATLLHQSTDKfvaelwkdVDRIVGLDQVAGmNETAFGAAYKTKKG----MFRTVGQLYKESLT- 665
Cdd:cd14893 554 GKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAA-ASSEKAAKQTEERGstssKFRKSASSARESKNi 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 666 -------------KLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYe 732
Cdd:cd14893 625 tdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY- 703
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 528481573 733 iltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 773
Cdd:cd14893 704 --------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
103-774 |
2.52e-71 |
|
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: 253.86 E-value: 2.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnipgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 260
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY---------ILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSN-GNIPIPGQQDKDNFQETMEAMHIM 339
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 340 SFNHEEILSMLKVVSAVLQFGNIVFKKERNtdQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYVQKAqtkeq 419
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR----- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 420 adfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQ 499
Cdd:cd14905 304 -----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 500 EEYQREGIEW-SFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVDKLVQEQGTHGKF-QKPRQlkdkad 577
Cdd:cd14905 377 REYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 578 FCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKF-------------VAELWKDVD----------RIVGL--- 631
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakksplSIVKVlls 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 632 ------DQVAGMNETAFGAAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAGKLEPHLVLDQLR 703
Cdd:cd14905 524 cgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481573 704 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSKIFFR 774
Cdd:cd14905 604 SLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
102-739 |
1.46e-69 |
|
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: 247.48 E-value: 1.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 102 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 180
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 181 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgelerqllQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIV 260
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSS----------AIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 261 GANIE-TYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDKDNFQETMEAMHIM 339
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 340 SFNHEEILSMLKVVSAVLQFGNIVFKKERNTD-QASMPE--NTAAQKLCHLLGMNVMEFTRAILSPRIKVGrdyvqKAQT 416
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSEDG-----TTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 417 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFI 496
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 497 LEQEEYQREGIEwsfIDF----GLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVDKLVQEQGTHGKFQKPRQl 572
Cdd:cd14874 373 DQLVDYAKDGIS---VDYkvpnSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 573 KDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKdvdrivgldqvagmNETAfgaaykTKKGM 652
Cdd:cd14874 447 KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE--------------SYSS------NTSDM 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 653 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 732
Cdd:cd14874 507 IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYR 586
|
....*..
gi 528481573 733 ILTPNAI 739
Cdd:cd14874 587 CLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
103-734 |
1.40e-64 |
|
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: 233.09 E-value: 1.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 182
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 183 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPGELERqllqANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 262
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRVES----SIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 263 NIETYLLEKSRAIRQAKDERTFHVFYQLLAG--AGEHLRSDLLLEGFNsYRFL--SNGNIPIPGQQDKDN-------FQE 331
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRN-YRYLriPPEVPPSKLKYRRDDpegnverYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 332 TMEAMHIMSFNHEEILSMLKVVSAVLQFGNIVFKKerNTDQASMPENTAAQKLCHLLGMNVMEFTRAILSPRIKVGRDYV 411
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 412 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFQLNSFEQLCINYTNEKL 486
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 487 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIErpANPPGVLALLDEECwfPKATDKTFVDKLVQEQgtHGKF 566
Cdd:cd14882 387 QYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYIMDRIKEK--HSQF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 567 QKPrqlKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDvdrivglDQVAGMnetafgaay 646
Cdd:cd14882 460 VKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM--------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 647 KTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIV 723
Cdd:cd14882 521 RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650
....*....|.
gi 528481573 724 FQEFRQRYEIL 734
Cdd:cd14882 595 FQEFLRRYQFL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
124-258 |
1.01e-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: 200.26 E-value: 1.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 124 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 202
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481573 203 SSHKGRKDHN-------IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 258
Cdd:cd01363 81 FNGINKGETEgwvylteITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
103-772 |
6.43e-58 |
|
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: 215.09 E-value: 6.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 103 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 181
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 182 ESGAGKTENTKKVIQYLAHVA----------SSHKGRKDHNIP-----GELERQLLQANPILESFGNAKTVKNDNSSRFG 246
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrrlptnlNDQEEDNIHNEEntdyqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 247 KFIRINFDvTGYIVGANIETYLLEKSRAIRQAKDERTFHVFYQLLAGAGEHLRSDLLLEGFNSYRFLSNGNIPIPGQQDK 326
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 327 DNFQETMEAMHIMSFNHEEILSMLKVVSAVLQFGNI-----VFKKE---------------------RNTDQASMPENTA 380
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 381 AQKL-CHLLGMNVMEFTRAILSPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 457
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 458 IGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIERPANppGVLAL 537
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 538 LDEECWFPKATDKT-FVDKLVQEQGTHGKF-QKPRQLKDKADFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTD 615
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 616 KFVAELWKDVDRIVGLDQVAGMNETAFGAAYKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFVRCIIPNHEKRA- 690
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 691 GKLEPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIRALELDPNLYRIGQSK 770
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 528481573 771 IF 772
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1078-1937 |
7.63e-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: 146.35 E-value: 7.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1078 QAQIDELkiqLAKKEEELQAVLargdEEVA-------QKNNALKQLRELQAQLA-------ELQEDLESEKAARNKAEKL 1143
Cdd:TIGR02168 143 QGKISEI---IEAKPEERRAIF----EEAAgiskykeRRKETERKLERTRENLDrledilnELERQLKSLERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1144 KrDLSEELEALKTELEdTLDTTAAQQELRSKREQEvaelkkaiddetrnheSQIQEMRQRHGTALEEISEQLEQAKRVKG 1223
Cdd:TIGR02168 216 K-ELKAELRELELALL-VLRLEELREELEELQEEL----------------KEAEEELEELTAELQELEEKLEELRLEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1224 NLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1303
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1304 KKGIKLTKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEeknnlleqqeeeeesrknlekQLATLQAQLVETKKKL 1383
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLET-------LRSKVAQLEL---------------------QIASLNNEIERLEARL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1384 EDDVGALEGLEEVKRKLQKDMEvtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQivsNLEKKQKKFDQMLAEE 1463
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAEREL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1464 KTISAR-YAEERDRAEAEAREKDTKALSMARA--------LDEALEAKEEFER-LNKQLRAEMEDLI-SSKDDVGKNVHE 1532
Cdd:TIGR02168 485 AQLQARlDSLERLQENLEGFSEGVKALLKNQSglsgilgvLSELISVDEGYEAaIEAALGGRLQAVVvENLNAAKKAIAF 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1533 LEKSK--------------RTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF---DRDLQARDEQNEEKKR 1595
Cdd:TIGR02168 565 LKQNElgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPG 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1596 ALV-----KQVREMEAELEDERKQRALAVAAK---KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1667
Cdd:TIGR02168 645 YRIvtldgDLVRPGGVITGGSAKTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1668 RTsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQleee 1747
Cdd:TIGR02168 725 SR-------QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---- 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1748 leeEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSkFKASIAALEAKIL 1827
Cdd:TIGR02168 794 ---LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIE 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1828 QLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAS-RRKL 1906
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEY 949
|
890 900 910
....*....|....*....|....*....|....*...
gi 528481573 1907 QRELDDA-------TEASEGLSREVNTLKNRLRRGGPV 1937
Cdd:TIGR02168 950 SLTLEEAealenkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
864-1695 |
1.53e-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: 145.20 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 864 LIKVKERQVKVENELVEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARL-VAKKQELEEILHDLESRVEEEEERNQ 942
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 943 SLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEE 1022
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1023 EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG 1102
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1103 DEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEvael 1182
Cdd:TIGR02168 417 ERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQALDAAEREL---- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1183 kkaidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNK-ELTNEV---KSLQQAKSESEHKRK 1258
Cdd:TIGR02168 485 -----AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEAalgGRLQAVVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1259 K-LEAQLQEVMAR--FSEGEKVKG-ELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQE-ETRQ 1333
Cdd:TIGR02168 560 KaIAFLKQNELGRvtFLPLDSIKGtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNAlELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1334 KLNLSSRIRQLEEEK-----------NNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1402
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1403 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERDRAEAEAR 1482
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE-----------------AEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1483 EKDTKALSMARALDEALEAKEEFERLNKQ---LRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ 1559
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1560 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEkKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEaa 1639
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSE-LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-- 939
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1640 nkardeaikqlRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQL 1695
Cdd:TIGR02168 940 -----------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1041-1807 |
2.90e-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: 140.96 E-value: 2.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1041 DLEERLKKEEKTRQELEKAKRKLDAettdLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQ 1120
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1121 AQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttaaqqELRSKREQEVAELKKAiDDETRNHESQIQEM 1200
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE----------ELKEELESLEAELEEL-EAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1201 RQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLqqakseSEHKRKKLEAQLQEVMARFSEGEKVKGE 1280
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI------EELLKKLEEAELKELQAELEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1281 LADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEetrqKLNLSSRIRQLEEEKNNLLEQQEEEEE 1360
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1361 S---RKNLEKQLAT-----LQAQLVETKKKLEDDVGALEGLEEVK-----------RKLQKDMEVTSQKLEEKAIAFDKL 1421
Cdd:TIGR02168 528 LisvDEGYEAAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRvtflpldsikgTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1422 EKTKNRLQQELDDLmvdLDHQRqIVSNLE-----KKQKKFDQML--AEEKTISARYAEERdraeaEAREKDTKALSMARA 1494
Cdd:TIGR02168 608 VKFDPKLRKALSYL---LGGVL-VVDDLDnalelAKKLRPGYRIvtLDGDLVRPGGVITG-----GSAKTNSSILERRRE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1495 LDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQA 1574
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1575 MKAQFDRDLQARDEQNEEKKRAlvkqvremEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ 1654
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEA--------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1655 AQMKDYQRELEEARTsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK 1734
Cdd:TIGR02168 831 RRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1735 RRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSA--------AQKSENARQQLERQNKDLKSKLQE 1806
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtleeaealENKIEDDEEEARRRLKRLENKIKE 983
|
.
gi 528481573 1807 L 1807
Cdd:TIGR02168 984 L 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1004-1743 |
3.38e-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: 134.42 E-value: 3.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1004 KKLLEDRVGemTSQLAEEEEKAKN-LGKVKNKQEMMMVDLEERLKKEEKTRQELEKA-------KRKLDAETTDLQDQIA 1075
Cdd:TIGR02169 156 RKIIDEIAG--VAEFDRKKEKALEeLEEVEENIERLDLIIDEKRQQLERLRREREKAeryqallKEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1076 ELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnkaekLKRDLsEELEALK 1155
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKL----TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-----VKEKI-GELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1156 TELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESD 1235
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1236 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMarfSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvss 1315
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQ---EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1316 lESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE 1395
Cdd:TIGR02169 454 -EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1396 VKRKLQKDME-----------VTSQKLEEKAIAFDKLEKTK-------NRLQQELDDL--------------MVDLDHQR 1443
Cdd:TIGR02169 533 VGERYATAIEvaagnrlnnvvVEDDAVAKEAIELLKRRKAGratflplNKMRDERRDLsilsedgvigfavdLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1444 Q-----------IVSNLEKKQKKFDQM--------LAE-----------EKTISARYAEERDRAEAEAREKDtkalSMAR 1493
Cdd:TIGR02169 613 EpafkyvfgdtlVVEDIEAARRLMGKYrmvtlegeLFEksgamtggsraPRGGILFSRSEPAELQRLRERLE----GLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1494 ALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ 1573
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1574 AMKAQFDrdlQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKL 1653
Cdd:TIGR02169 769 ELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1654 QAQMKDYQRELEEARTSRDEIFTQSKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1726
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELeaalrdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810
....*....|....*..
gi 528481573 1727 KAALLDEKRRLEARIAQ 1743
Cdd:TIGR02169 926 LEALEEELSEIEDPKGE 942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
980-1861 |
3.56e-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: 134.42 E-value: 3.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 980 EAKIKKMEEDIllleDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKtrQELEKA 1059
Cdd:TIGR02169 169 DRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR----EYEGYELLKEK--EALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1060 KRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLRELQAQLAELQEDLESEKAARN 1138
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1139 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaidDETRNHESQIQEMRQRHGTALEEIS---EQL 1215
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK----EELEDLRAELEEVDKEFAETRDELKdyrEKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1216 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1295
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1296 SCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRI-------RQLEEEKNNLLEQQEEEEESRknlekq 1368
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNR------ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1369 latLQAQLVETKkklEDDVGALEGLEEVK---------RKLQKDMEVTSQKLEEKAIAF-----DKLEKTKNRLQQELDD 1434
Cdd:TIGR02169 549 ---LNNVVVEDD---AVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDGVIGFavdlvEFDPKYEPAFKYVFGD 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1435 LMV--DLDHQRQIVSN----------LEKKQKKFDQMLAEEKTISaRYAEERDRAEAEAREKDtkalSMARALDEALEAK 1502
Cdd:TIGR02169 623 TLVveDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1503 EEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrd 1582
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1583 lQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQR 1662
Cdd:TIGR02169 776 -KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1663 ELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIA 1742
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1743 QLEEELEEEQSNMELLNDrFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfkasiaal 1822
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLE-------------- 999
|
890 900 910
....*....|....*....|....*....|....*....
gi 528481573 1823 eakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQV 1861
Cdd:TIGR02169 1000 ---------------EERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
832-1626 |
2.25e-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: 128.25 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 832 LRHWQWWRLftkvkpLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEE 911
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 912 MRARLVAKKQELEEILHDLESrveEEEERNQSLQNEKKKmqshiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDIL 991
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLER---QLEELEAQLEELESK------------------LDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 992 LLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLq 1071
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1072 dQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEEL 1151
Cdd:TIGR02168 434 -ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1152 EAlKTELEDTLDTTAAQQELRSKREQEV-AELKKAIDD-ETRNHESQIQ----------------EMRQRHGTALEeiSE 1213
Cdd:TIGR02168 513 KN-QSGLSGILGVLSELISVDEGYEAAIeAALGGRLQAvVVENLNAAKKaiaflkqnelgrvtflPLDSIKGTEIQ--GN 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1214 QLEQAKRVKGNLEKNKQTLESDNK---------ELTNEVKSLQQAksesEHKRKKLEAQLQEVMA---RFSEGEKVKGEL 1281
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKlrkalsyllGGVLVVDDLDNA----LELAKKLRPGYRIVTLdgdLVRPGGVITGGS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1282 ADRTHKI---QTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1358
Cdd:TIGR02168 666 AKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1359 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSqkleekaIAFDKLEKTKNRLQQELDDLMVD 1438
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK-------EELKALREALDELRAELTLLNEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1439 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1518
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1519 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ-----ATEDAKLRLEVnMQAMKAQFDRDLQARDEQNEEK 1593
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEE-AEALENKIEDDEEEARRRLKRL 977
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 528481573 1594 KRAL----------VKQVREMEAELEDERKQRALAVAAKKKLE 1626
Cdd:TIGR02168 978 ENKIkelgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
969-1743 |
4.91e-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: 124.02 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 969 RQKLQLEKVTAEA----KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEE 1044
Cdd:TIGR02169 200 LERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1045 RLKKEEKTRQ-ELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG---DEEVAQKNNALKQL---- 1116
Cdd:TIGR02169 280 KIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelEREIEEERKRRDKLteey 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1117 RELQAQLAELQEDLES-EKAARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhES 1195
Cdd:TIGR02169 360 AELKEELEDLRAELEEvDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1196 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF---- 1271
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRavee 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1272 ---SEGEKVKGELAD-----RTHKIQTE------LDNVSCLLEDAEKKGIKLTKDVsslesQLQDTQELLQEETRQKLNL 1337
Cdd:TIGR02169 515 vlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNVVVEDDAVAKEAIELLKRR-----KAGRATFLPLNKMRDERRD 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1338 SSRIR------------QLEEEKNNLLEQQEEEEESRKNLEKQLATL-QAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1404
Cdd:TIGR02169 590 LSILSedgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1405 EVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAE 1480
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1481 AREKDTKALSMARaLDEALEAKEefERLNKqLRAEMEDLisSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1560
Cdd:TIGR02169 750 EQEIENVKSELKE-LEARIEELE--EDLHK-LEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1561 TEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAAN 1640
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1641 KARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKE------NEKKLKSLEAEILQLQEDLASSERARRHAEQERD 1714
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
810 820
....*....|....*....|....*....
gi 528481573 1715 ELADEISNSASGKAALLDEKRRLEARIAQ 1743
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
221-715 |
1.59e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 118.69 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 221 LLQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------KDERTFHVFYQ 289
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 290 LLAGAGEH-----LRSDLLLEGFN--SYRFLSNGNIPIPG--------QQDKDNFQETMEAMHIMSFNHEEILSMLKVVS 354
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 355 AVLQFGNIVFKKERNTDQASMPEN---TAAQKLCHLLGMNVMEFTRAIL---SPRIKVGRDYVQKAQTKEQADFAVEALA 428
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLmtkSVSLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 429 KATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFQLNSFEQLCINYTNEKLQQlfnh 492
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 493 tmfileqEEYQREGIEWSFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATD----------KTFVDKLVQEQGT 562
Cdd:cd14894 565 -------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 563 HGKfQKPRQLKDKA----------DFCIIHYAGRVDYKADEWLMKNMDPLNDNVATLLHQSTDKFVAELWKDVDRivgLD 632
Cdd:cd14894 638 RLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ---LG 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 633 QVAGMNETAFGAAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLEPHLVLDQLRCNGVLEGIR 712
Cdd:cd14894 714 WSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQME 792
|
...
gi 528481573 713 ICR 715
Cdd:cd14894 793 ICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1365-1937 |
6.30e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.96 E-value: 6.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1365 LEKQLATLQAQ---------LVETKKKLEDDVGAL--EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELD 1433
Cdd:COG1196 198 LERQLEPLERQaekaeryreLKEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1434 DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1513
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1514 AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfDRDLQARDEQNEEK 1593
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1594 KRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE 1673
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1674 IftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE-----LADEISNSASGKAALLDEKRRLEARIAQLEEEL 1748
Cdd:COG1196 517 A--GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDevaaaAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1749 EEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKilq 1828
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL--- 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1829 leEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQR 1908
Cdd:COG1196 672 --AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
570 580 590
....*....|....*....|....*....|...
gi 528481573 1909 ELDDATEAS----EGLSREVNTLKNRLRRGGPV 1937
Cdd:COG1196 750 EEALEELPEppdlEELERELERLEREIEALGPV 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1547 |
2.63e-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: 115.15 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 849 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 928
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 929 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1008
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1009 DRVGEMTSQLAEEEEKAKNLGKVKNKQEM--------MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI---AEL 1077
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELaqlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEGY 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1078 QAQIDelkiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE----DLESEKAARNKAEKLKRDLSEELEA 1153
Cdd:TIGR02168 536 EAAIE------AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLVK 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1154 LKTELEDTL-----------DTTAAQQELRSKREQEVAELKK--------AIDDETRNHESQIQEMRQRhgtaLEEISEQ 1214
Cdd:TIGR02168 610 FDPKLRKALsyllggvlvvdDLDNALELAKKLRPGYRIVTLDgdlvrpggVITGGSAKTNSSILERRRE----IEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1215 LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDN 1294
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1295 VSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQA 1374
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1375 QLVETKKKLEDDVGALEGLEEVKRKLQKD-------MEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1447
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1448 NLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1526
Cdd:TIGR02168 926 QLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFL 1005
|
730 740
....*....|....*....|.
gi 528481573 1527 GKNVHELEKSKRTLEQQVEEM 1547
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEI 1026
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1115-1862 |
1.30e-24 |
|
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: 112.90 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1115 QLRELQAQLAELQEDLESEKAARNKAEKlkrDLSEELEALKTELEDTLDT----TAAQQELRSKREQEVAELKKA---ID 1187
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVI---DLQTKLQEMQMERDAMADIrrreSQSQEDLRNQLQNTVHELEAAkclKE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1188 DETRNHESQIQEMRQ---RHGTALEEISEQLEQAKRVKGnleknKQTLESDNKElTNEVKSLQQAKSESehkRKKLEAQL 1264
Cdd:pfam15921 163 DMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFEEASG-----KKIYEHDSMS-TMHFRSLGSAISKI---LRELDTEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1265 QEVMAR-FSEGEKVKGELADRTHKI----QTELDNVSCLLEDAEKKGIKLTKDVSSLESQ---LQDTQELLQEETRQKLn 1336
Cdd:pfam15921 234 SYLKGRiFPVEDQLEALKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1337 lSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLVETKKKLEDDVgalegleevkRKLQKDMEVTSQKLEEKAI 1416
Cdd:pfam15921 313 -SMYMRQLSD------------------LESTVSQLRSELREAKRMYEDKI----------EELEKQLVLANSELTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1417 AFDKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKTISARYAEERDR-AEAEAREKDTKAL---- 1489
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEALLKAMksec 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1490 --SMARALdEALEAKEEFERLNKQLRAEMEdliSSKDDVGKNVHELEKSKRTLE---QQVEEMRTQLEELEDELQAT--E 1562
Cdd:pfam15921 443 qgQMERQM-AAIQGKNESLEKVSSLTAQLE---STKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1563 DAKLRLEVNMQAMKAQFDRdlqardeqNEEKkralvkQVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIE-AANK 1641
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLK--------NEGD------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQlVGQH 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1642 ARDEAIKQLRK--LQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADE 1719
Cdd:pfam15921 582 GRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNE 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1720 ISNSASGKAALLDEKRRLEARIaqleeelEEEQSNMELLNDRFRkttMQVDTLNTELAGERSAAQKSENA---------- 1789
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNF-------RNKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSMEGSdghamkvamg 731
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1790 -RQQLER---QNKDLKSKLQELEGSVK--SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1862
Cdd:pfam15921 732 mQKQITAkrgQIDALQSKIQFLEEAMTnaNKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
922-1684 |
2.11e-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: 112.08 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 922 ELEEILHDLEsRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQ--------LEKVTAEAKIKKMEEDILLL 993
Cdd:TIGR02169 171 KKEKALEELE-EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyellKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 994 EDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1073
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1074 IAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELqedlesEKAARNKAEKLKrDLSEELEA 1153
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV------DKEFAETRDELK-DYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1154 LKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLE 1233
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1234 SDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF-------SEGEKVKGELAD-----RTHKIQTE------LDNV 1295
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveevlkASIQGVHGTVAQlgsvgERYATAIEvaagnrLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1296 SCLLEDAEKKGIKLTKDVS------------------------------------------------------------- 1314
Cdd:TIGR02169 553 VVEDDAVAKEAIELLKRRKagratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaa 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1315 ----------SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1384
Cdd:TIGR02169 633 rrlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1385 DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1464
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1465 TISARyaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQV 1544
Cdd:TIGR02169 793 IPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1545 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDR------DLQARDEQNEEKKRALVKQVREMEAELEdERKQRALA 1618
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleaqieKKRKRLSELKAKLEALEEELSEIEDPKG-EDEEIPEE 949
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1619 VAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEI--FTQSKENEKK 1684
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIleRIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
910-1540 |
2.37e-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: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 910 EEMRARL--------VAKK-QELEEILHDLESRVeeeeernqsLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE 980
Cdd:COG1196 196 GELERQLeplerqaeKAERyRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 981 AKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKAK 1060
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1061 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKA 1140
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1141 EKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR 1220
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1221 VKGNLEKNKQTLESDNKELTNEVkslQQAKSESEHKRKKLEAQL---------QEVMARFSEGEKVKGELADRTHKIQTE 1291
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGL---AGAVAVLIGVEAAYEAALeaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1292 L------------DNVSCLLEDAEKKGIK-LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEE 1358
Cdd:COG1196 577 LpldkiraraalaAALARGAIGAAVDLVAsDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1359 EESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1438
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEE-------LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1439 LDHQRQIVSNLEkkqkkFDQMLAEEKTISARYAEERDRAEAEAREKDTKAlSMAR-------ALDEALEAKEEFERLNKQ 1511
Cdd:COG1196 730 LEAEREELLEEL-----LEEEELLEEEALEELPEPPDLEELERELERLER-EIEAlgpvnllAIEEYEELEERYDFLSEQ 803
|
650 660
....*....|....*....|....*....
gi 528481573 1512 LraemEDLISSKDDVGKNVHELEKSKRTL 1540
Cdd:COG1196 804 R----EDLEEARETLEEAIEEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1324-1889 |
3.16e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1324 QELLQEETRQKLNLSS-RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1402
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1403 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1482
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1483 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1562
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1563 DAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRAlvKQVREMEAELEDERKQRALAVAAKKKLEM---------DLKDVE 1633
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavaVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1634 AQIEAANKARDEAIKQ--LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQ 1711
Cdd:COG1196 534 AAYEAALEAALAAALQniVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1712 ERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEeqsnMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQ 1791
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE----GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1792 QLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQY 1871
Cdd:COG1196 690 EEELELEEALLAEEEEE-----------RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 528481573 1872 KEQMEKANSRMKQLKRQL 1889
Cdd:COG1196 759 PPDLEELERELERLEREI 776
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
969-1558 |
3.64e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 107.84 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 969 RQKLQLEKV-TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1047
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1048 KEEKTRQELEKAKRkldaETTDLQDQIAELQAQIDELKIQLAKKEEELqavlargdEEVAQKNNALKQLRELQAQLAELQ 1127
Cdd:PRK03918 232 ELEELKEEIEELEK----ELESLEGSKRKLEEKIRELEERIEELKKEI--------EELEEKVKELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1128 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ---EVAELKKAID--DETRNHESQIQEMRQ 1202
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1203 RH-GTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE---------------SEHKRKKLeaqLQE 1266
Cdd:PRK03918 380 RLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKEL---LEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1267 VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK--KGIKLTKDVSSLESQLQ--DTQELLQ-----EETRQKLN- 1336
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKkyNLEELEKkaeeyEKLKEKLIk 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1337 LSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAI 1416
Cdd:PRK03918 537 LKGEIKSLKKE-----------LEKLEELKKKLAELEKKLDELEEELAE---LLKELEELGFESVEELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1417 AFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErdraeaEAREKDTKALSMARALD 1496
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELA 676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481573 1497 EALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1558
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
854-1614 |
2.55e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 105.15 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 854 EEEMQAKDEELIKVKERQVKVE-------NELVEMERKHQQLLEEKNILAEQLQAE-TELFAEAEEMRARLVAKKQELEE 925
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDliidekrQQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 926 ILHDLESRVEEEEERNQSLqNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEakIKKMEEDILLLEDQNSKFLKEKK 1005
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRL-EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1006 LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK 1085
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1086 IQLAKKEEELQavlaRGDEEVAQKNNALKQLRELQAQLAELQED-----------LESEKAARNKAEKLKRDLSEELEAL 1154
Cdd:TIGR02169 406 RELDRLQEELQ----RLSEELADLNAAIAGIEAKINELEEEKEDkaleikkqewkLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1155 KTELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE----------------EIS 1212
Cdd:TIGR02169 482 EKELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1213 EQLEQAKRVKG-------------------------------------------------------NLEKNKQ------- 1230
Cdd:TIGR02169 562 EAIELLKRRKAgratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvveDIEAARRlmgkyrm 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1231 -TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1309
Cdd:TIGR02169 642 vTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1310 TKDVSSLESQLQDTQELLQEetrqklnLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDD--- 1386
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSrip 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1387 --VGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK 1464
Cdd:TIGR02169 795 eiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1465 TISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTlEQQV 1544
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSL 953
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481573 1545 EEMRTQLEELEDELQATEDaklrleVNMQAMKaQFDRDLQARDEQnEEKKRALV---KQVREMEAELEDERKQ 1614
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEP------VNMLAIQ-EYEEVLKRLDEL-KEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
810-1452 |
1.39e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 810 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRLftkvkpllQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL 888
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 889 LEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshIQDLEEQLDEEEAA 968
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 969 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK 1048
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1049 EEKTRQELEKAKRKLDAEttdlqdqIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE 1128
Cdd:COG1196 433 LEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1129 DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAL 1208
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1209 EEISEQLEQAKRVKGNLEKNKQTLESDNK----ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADR 1284
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARyyvlGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1285 THKIQTEldnvscLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1364
Cdd:COG1196 666 SRRELLA------ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1365 LEKQLATLQAQLVETKKKLEDDVGALEG-LEEVKRKLQK----DMEVtsqkLEEkaiaFDKLEKTKNRLQQELDDLMVDL 1439
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELEReLERLEREIEAlgpvNLLA----IEE----YEELEERYDFLSEQREDLEEAR 811
|
650
....*....|...
gi 528481573 1440 DHQRQIVSNLEKK 1452
Cdd:COG1196 812 ETLEEAIEEIDRE 824
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1197-1808 |
4.25e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.17 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1197 IQEMRQRHGTaLEEISEQLEQAKRVKGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGE 1275
Cdd:COG1196 195 LGELERQLEP-LERQAEKAERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1276 KVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQD-TQELLQEEtrqklnlsSRIRQLEEEKNNLLEQ 1354
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEElEEELAELE--------EELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1355 QEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1434
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1435 LMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalsmARALDEALEAKEEFERLNKQLRA 1514
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL--------LEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1515 EMEDLISSKDDVGKNVHELEKSKRtLEQQVEEMRTQLEELEDELQATEDAKLRLEVNmqamkaqfDRDLQARDEQNEEKK 1594
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1595 RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDyqRELEEARTSRDEI 1674
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE--AALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1675 FTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSN 1754
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 528481573 1755 MELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1808
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1133-1691 |
5.75e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 100.52 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1133 EKAARNKAEKLKrdlseELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID---DETRNHESQIQEMRQRHGTaLE 1209
Cdd:PRK03918 161 ENAYKNLGEVIK-----EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINeisSELPELREELEKLEKEVKE-LE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1210 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQ 1289
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1290 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEEKNNLLEQQ------------ 1355
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekel 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1356 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdmEVTSQKLEEkaiafDKLEKTKNRLQQELDDL 1435
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC----PVCGRELTE-----EHRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1436 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRA- 1514
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSl 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1515 -----EMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR-TQLEELEDELQATE----------DAKLRLEVNMQAMKAQ 1578
Cdd:PRK03918 545 kkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkDAEKELEREEKELKKL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1579 FDRDLQARDEQNEEKKRA--LVKQVREMEAELEDERKQRAlaVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQ 1656
Cdd:PRK03918 625 EEELDKAFEELAETEKRLeeLRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
570 580 590
....*....|....*....|....*....|....*...
gi 528481573 1657 ---MKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAE 1691
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 ... |
1002-1876 |
8.79e-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: 100.43 E-value: 8.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1002 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQE--------------LEKAKRKLDAET 1067
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAkkaleyyqlkekleLEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1068 TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDL 1147
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1148 SEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHgtaLEEISEQLEQAKRVKGNLEK 1227
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKLQ---EKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1228 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQlqevMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI 1307
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL----KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1308 KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDV 1387
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1388 GALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD--------------HQRQIVSNLEKKQ 1453
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIavleidpilnlaqlDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1454 KKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHEL 1533
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1534 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERK 1613
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1614 QRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQaqmKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1693
Cdd:pfam02463 782 KTEKLKVEEEKEE-KLKAQEEELRALEEELKEEAELLEEEQ---LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1694 QLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1773
Cdd:pfam02463 858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1774 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1853
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
890 900
....*....|....*....|...
gi 528481573 1854 LKEVFMQVEDERRHADQYKEQME 1876
Cdd:pfam02463 1018 RLKEFLELFVSINKGWNKVFFYL 1040
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
875-1246 |
5.69e-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: 97.43 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 875 ENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSH 954
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 955 IQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1034
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1035 QEMMMVDLEERLKKEEKTRQELEkakrkldAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK 1114
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1115 QLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR----SKREQEVAELKKAIDDET 1190
Cdd:TIGR02168 909 KRSELRRELEELREKLA---QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKELG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1191 RNHESQIQEmrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSL 1246
Cdd:TIGR02168 986 PVNLAAIEE--------YEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1002-1724 |
6.07e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.90 E-value: 6.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1002 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQElEKAKRKLDAETTDLQDQIAELQAQI 1081
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA-EDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1082 DELKIQLAKKEEEL-QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARnKAEKLKRDLSE---------EL 1151
Cdd:PTZ00121 1174 DAKKAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEakkaeeernNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1152 EALKTELEDTLDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQT 1231
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1232 LESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA--RFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL 1309
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1310 TKdvSSLESQLQDTQELLQEETRQKLNLSSRI---RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDd 1386
Cdd:PTZ00121 1411 KK--AAAAKKKADEAKKKAEEKKKADEAKKKAeeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE- 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1387 vgALEGLEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQI--VSNLEKKQKKFDQMLAEEk 1464
Cdd:PTZ00121 1488 --AKKKAEEAKKK--------ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEE- 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1465 tisARYAEERDRAEAEAREKDTKALSMARAlDEALEAKEEfeRLNKQLRAEMEDLISSKDDVGKnvHELEKSKRTLEQQV 1544
Cdd:PTZ00121 1557 ---LKKAEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEA--RIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1545 EEMRTQLEELEDELQatEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAlaVAAKKK 1624
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEA--EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKA 1704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1625 LEMDLKDVEA--QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDE---IFTQSKENEKKLKSLEAEILQLQEDL 1699
Cdd:PTZ00121 1705 EELKKKEAEEkkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
730 740
....*....|....*....|....*
gi 528481573 1700 ASSERARRHAEQERdELADEISNSA 1724
Cdd:PTZ00121 1785 LDEEDEKRRMEVDK-KIKDIFDNFA 1808
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1002-1586 |
1.21e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 96.26 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1002 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKakrkLDAETTDLQDQIAE----- 1076
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAEterer 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1077 --LQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLE----SEKAARNKAEKLKRD---- 1146
Cdd:PRK02224 275 eeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDaddl 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1147 ------LSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIddetrnhesqiqemrqrhgtalEEISEQLEQAKR 1220
Cdd:PRK02224 355 eeraeeLREEAAELESELEEA-------REAVEDRREEIEELEEEI----------------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1221 VKGNLEKNKQTLESDNKELTNEVKSlqqaksesehkrkkLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLE 1300
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAE--------------LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1301 DAEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEknnlleqqeeeeesRKNLEKQLATLQAQLVETK 1380
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLEER--------------REDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1381 KKLE---DDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFD-KLEKTKNRLQQ--ELDDLMVDLDHQRQIVSNLEKKQK 1454
Cdd:PRK02224 537 ERAEelrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNsKLAELKERIESleRIRTLLAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1455 KFDQMLAEEKTisaRYAEERDRAEAEAREKDtkalsmARALDEALEAKEEFERLNKQLRAEMEDLISSKDDvgknvheLE 1534
Cdd:PRK02224 617 ALAELNDERRE---RLAEKRERKRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQ 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1535 KSKRTLEQQVEEmrtqLEELEDELQATEDAKLRLEV------NMQAMKAQFDRDLQAR 1586
Cdd:PRK02224 681 AEIGAVENELEE----LEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQR 734
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
872-1460 |
2.86e-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: 94.70 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 872 VKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKM 951
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 952 QSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1027
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1028 LGKVKNKQEMMMVDLEERLKKEEKTRqELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVA 1107
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1108 QKNNALKQLRELQAQLAELQEDL-----ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL 1182
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLnqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1183 KKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA 1262
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1263 QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIR 1342
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1343 QLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE--DDVGALEGLEEVKRKLQKDMEVTSQ-------KLEE 1413
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQtqkslkkKQEE 586
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 528481573 1414 KAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1460
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1209-1920 |
3.02e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.13 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1209 EEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEH----KRKKLEAQLQEVMARFSEGEKVKGELADR 1284
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1285 THKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKL-NLSSRIRQLEEEKNNLLEQQEEEEESRK 1363
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIgELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1364 NLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQR 1443
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1444 QIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSK 1523
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1524 DDVGKNVHELEKSKRTLEQQVEEMRTQLEEL--------------------------------------EDELQATEDAK 1565
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaqlgsvgeryataievaagnrlnnvvvEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1566 LRLEVN-----------MQAMKA------------------QFDRDLQA------RDE---QNEEKKRALVKQVR--EME 1605
Cdd:TIGR02169 566 LLKRRKagratflplnkMRDERRdlsilsedgvigfavdlvEFDPKYEPafkyvfGDTlvvEDIEAARRLMGKYRmvTLE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1606 AELEDE--------RKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1677
Cdd:TIGR02169 646 GELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1678 SKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQsnMEL 1757
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE--LSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1758 LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSV------KSKFKASIAALEAKILQLEE 1831
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1832 QLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRqLEEAEEEATRANASRRKLQRELD 1911
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-PKGEDEEIPEEELSLEDVQAELQ 961
|
....*....
gi 528481573 1912 DATEASEGL 1920
Cdd:TIGR02169 962 RVEEEIRAL 970
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1122-1741 |
4.02e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.72 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1122 QLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttaaqqelrskrEQEVAELKKAIDDetrnHESQIQEMR 1201
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIE----------------EKEEKDLHERLNG----LESELAELD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1202 qrhgTALEEISEQLEQAKRVKGN----LEKNKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKV 1277
Cdd:PRK02224 220 ----EEIERYEEQREQARETRDEadevLEEHEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1278 KGELADRTHKIQTELDNVSCLLEDaekkgikLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqee 1357
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREE-------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA--------- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1358 eeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMV 1437
Cdd:PRK02224 359 -----EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1438 DLdhqrqivSNLEKKQKKFDQMLAEEKTISAryaeerdraeaearEKDTKALSMARALDEALEAKEEferlnkqLRAEME 1517
Cdd:PRK02224 434 TL-------RTARERVEEAEALLEAGKCPEC--------------GQPVEGSPHVETIEEDRERVEE-------LEAELE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1518 DLISSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqfdrDLQARDEQNEEKKRAL 1597
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIA----------------------ERRETIEEKRERAEEL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1598 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1677
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1678 SKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKR-RLEARI 1741
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 ... |
850-1737 |
1.48e-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: 93.11 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 850 VTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlVAKKQELEEILHD 929
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 930 LESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLED 1009
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1010 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLdaettdLQDQIAELQAQiDELKIQLA 1089
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL------EKLQEKLEQLE-EELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1090 KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTtaaqQ 1169
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----Q 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1170 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKR---VKGNLEKNKQTLESDNKELTNEVKSL 1246
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglkVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1247 QQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ--TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1324
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKlrLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1325 ELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDM 1404
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1405 EVTSQKLEEKAIAfdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREK 1484
Cdd:pfam02463 697 RQLEIKKKEQREK--EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1485 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDA 1564
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1565 KLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARD 1644
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1645 EAIKQLRKLQAQMKDYQRELEEartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSA 1724
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKE---------EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 528481573 1725 SGKAALLDEKRRL 1737
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
856-1547 |
2.91e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 856 EMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVE 935
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 936 EEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEdillledqNSKFLKEKKLLEDRVGEM 1014
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEE--------KKKADEAKKAEEKKKADE 1306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1015 TSQLAEEEEKAKNLGK----VKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAettdlqdqiAELQAQIDELKIQLAK 1090
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKkaeeAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA---------AEEKAEAAEKKKEEAK 1377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1091 KEEElqaVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRdlseeLEALKTELEDTLDTTAA 1167
Cdd:PTZ00121 1378 KKAD---AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeaKKKAEEKKK-----ADEAKKKAEEAKKADEA 1449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1168 QQELRSKREQEvaELKKAIDDETRNHESQIQEMRQRHGTAL----EEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1243
Cdd:PTZ00121 1450 KKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAkkkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1244 KSLQQAKS-----ESEHKRKKLEAQLQEVMARFSEGEKVkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1318
Cdd:PTZ00121 1528 KKAEEAKKadeakKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1319 QLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLVETKKKLEDDVGALEGLEE 1395
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEelkKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1396 VKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELD--DLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisARYAEE 1473
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEAEEDKKKAEE----AKKDEE 1754
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528481573 1474 RDRAEAEAREKDTKALSMARALDEALeAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1547
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM 1827
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
897-1275 |
4.30e-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: 91.28 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 897 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEK 976
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 977 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEmtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQEL 1056
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1057 EKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA 1136
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1137 RNKAEKLKRDLSEELEALKTELedtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtALEEIS---- 1212
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEEL--------SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-----ALEPVNmlai 978
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528481573 1213 EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKR-KKLEAQLQEVMARFSEGE 1275
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAfEAINENFNEIFAELSGGT 1042
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1287-1933 |
1.10e-17 |
|
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: 90.23 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1287 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1366
Cdd:pfam01576 16 KVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1367 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1446
Cdd:pfam01576 96 NEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1447 SNLEKKQKKFDQMLAEektisaryAEERDRAEAEAREkdtkalsmaraldealeakeEFERLNKQLRAEMEDLISSKDDv 1526
Cdd:pfam01576 176 KSLSKLKNKHEAMISD--------LEERLKKEEKGRQ--------------------ELEKAKRKLEGESTDLQEQIAE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1527 gknvhelekskrtLEQQVEEMRTQLEELEDELQAtedAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEA 1606
Cdd:pfam01576 227 -------------LQAQIAELRAQLAKKEEELQA---ALARLE------------EETAQKNNALKKIRELEAQISELQE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1607 ELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE-EARTSRDEIFTQSKENEKKL 1685
Cdd:pfam01576 279 DLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1686 KSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1765
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1766 TMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQElEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANK 1845
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1846 IVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVN 1925
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
....*...
gi 528481573 1926 TLKNRLRR 1933
Cdd:pfam01576 598 NLEKKQKK 605
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1694 |
1.14e-17 |
|
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: 90.03 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 845 KPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL-LEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL 923
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLeLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 924 EEILHDLESRVEEEEERNQSLQN-EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1002
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEkEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1003 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1082
Cdd:pfam02463 336 EIEELE--------KELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1083 ELKIQLAKKEEELQAVLArgDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK---AEKLKRDLSEELEALKTELE 1159
Cdd:pfam02463 408 QLLLELARQLEDLLKEEK--KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdelELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1160 DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE- 1238
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQk 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1239 LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLES 1318
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1319 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKR 1398
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1399 KLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1478
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1479 AEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1558
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1559 QATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElEDERKQRALAVAAKKKLEMDLKDVEAQIEA 1638
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE-EEPEELLLEEADEKEKEENNKEEEEERNKR 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1639 ANKARDEAIKQLRKLQAQMKdyqrELEEARTSRDEIFTQSKENEKKLKSLEAEILQ 1694
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFE----EKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
838-1434 |
6.66e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.43 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 838 WRLFTKVKPLLQVTRQEEEMQAKDEEliKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLV 917
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTE--NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 918 AKKQELEEilhdLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlEKVTAEAKIKKMEEDILLLEDQN 997
Cdd:PRK03918 242 ELEKELES----LEGSKRKLEEKIRELEERIEELKKEIEELE---------------EKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 998 SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDaETTDLQDQIAEL 1077
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1078 QAQIDELKIQlaKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE-----LE 1152
Cdd:PRK03918 378 KKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1153 ALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDE---TRNHE--SQIQEMRQR-HGTALEEISEQLEQAKRVKGNLE 1226
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselIKLKElaEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1227 KNKQTLESDNKELtNEVKSLQQAKSESEHKRKKLEAQLQEVMAR-----FSEGEKVKG-------------ELADRTHKI 1288
Cdd:PRK03918 536 KLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEErlkelepfyneylELKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1289 QTELDNVSCL---LEDAEKKGIKLTKDVSSLESQLQDTQELLQEET-----RQKLNLSSRIRQLEEEKNNLLEQQEEEEE 1360
Cdd:PRK03918 615 EREEKELKKLeeeLDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528481573 1361 SRKNLEKQLATLQaqlvETKKKLEDDVGALEGLEEVKRKLQKdmevtsQKLEEKAIAFDKLEKTKNRLQQELDD 1434
Cdd:PRK03918 695 TLEKLKEELEERE----KAKKELEKLEKALERVEELREKVKK------YKALLKERALSKVGEIASEIFEELTE 758
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
902-1740 |
3.36e-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: 85.28 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 902 ETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKkmqshiQDLEEQLDEEEAARQKLQLEKVTAEA 981
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 982 KIKKMEEDILLLEDQNSKFLKEkklledrvgemtsqlaeeeekakNLGKVKNKQEMmmvdleerlkkEEKTRQELEKAKR 1061
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDA-----------------------DIETAAADQEQ-----------LPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1062 KLDAETTDLQDQIAELQAQIdelkiqlAKKEEELQAVLARGDEEVAqknnalKQLRELQAQLAELQEDLES-EKAARNKA 1140
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRR-------SKIKEQNNRDIAGIKDKLA------KIREARDRQLAVAEDDLQAlESELREQL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1141 EKLKRDLSEELEALKTELEDT---LDTTAAQQELRSKREQEVAELKKAidDETRNHESQIQEMRQRHGTALEEISEQ-LE 1216
Cdd:pfam12128 429 EAGKLEFNEEEYRLKSRLGELklrLNQATATPELLLQLENFDERIERA--REEQEAANAEVERLQSELRQARKRRDQaSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1217 QAKRVKGNLEKNKQTLEsdnkeltnEVKSLQQAKSESEHKRKKLEAQLQevmarfsegEKVKGELADRTHKIQTELDNVS 1296
Cdd:pfam12128 507 ALRQASRRLEERQSALD--------ELELQLFPQAGTLLHFLRKEAPDW---------EQSIGKVISPELLHRTDLDPEV 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1297 clleDAEKKGIKLTKDVSSLESQLQDTQELLQEEtrqklnlssriRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQL 1376
Cdd:pfam12128 570 ----WDGSVGGELNLYGVKLDLKRIDVPEWAASE-----------EELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1377 VETKKKLEDDVGALEGLEEVKRKLqkdmevTSQKLEEKaiafDKLEKTKNRLQQELDDLMVDLDHQRQIvsnLEKKQKKF 1456
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRL------FDEKQSEK----DKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAW 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1457 DQMLAEEKTiSARYAEERDRAEAEAREKDTKAlsmarALDEALEAKEE-FERLNKQLRAEMEDLISSKDDVGKNVHELEK 1535
Cdd:pfam12128 702 LEEQKEQKR-EARTEKQAYWQVVEGALDAQLA-----LLKAAIAARRSgAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1536 SKRTLEQQVEemrtqleeledelqatedaklRLEVNMQAMkAQFDRDLQardEQNEEKKRALVKQVREMEAELEDERKQR 1615
Cdd:pfam12128 776 EIRTLERKIE---------------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQL 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1616 ALAVAAKKkleMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQR-----ELEEARTSRDEIFTQSKENEKKLKSLEA 1690
Cdd:pfam12128 831 ARLIADTK---LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSE 907
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 528481573 1691 EILQLQEDLASSERARRHAEQER--DELADEISNSASGKAALLDEKRRLEAR 1740
Cdd:pfam12128 908 SVKKYVEHFKNVIADHSGSGLAEtwESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1043-1618 |
4.60e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.58 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1043 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLA----KKEEELQAVLARGDEEVAQKNNALKQLR- 1117
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEa 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1118 --------------ELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1183
Cdd:COG4913 367 llaalglplpasaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1184 KAIDDETRNHESQIQ------EMRQR------------HGTALEEISEQlEQAKRVKGNLEKNKQTLESDNKELTNEVKS 1245
Cdd:COG4913 447 DALAEALGLDEAELPfvgeliEVRPEeerwrgaiervlGGFALTLLVPP-EHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1246 LQQAKSESEHKRKKLEAQ-------LQEVMARF-------SEGE------------KVKGELADRTHKIQTELDNVSCLL 1299
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKphpfrawLEAELGRRfdyvcvdSPEElrrhpraitragQVKGNGTRHEKDDRRRIRSRYVLG 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1300 EDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeknnLLEQQEEEEESRKNLEKQLATLQAQLvet 1379
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-----RLAEYSWDEIDVASAEREIAELEAEL--- 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1380 kKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkFDQM 1459
Cdd:COG4913 678 -ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEER 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1460 LAE------EKTISARYAEERDRAEAEAREKDTKALSMARA-----------LDEALEAKEEFERLNKQLRAemEDLISS 1522
Cdd:COG4913 755 FAAalgdavERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadLDADLESLPEYLALLDRLEE--DGLPEY 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1523 KDDVGKNVHELEKSKRT-----LEQQVEEMRTQLEELEDELQATE---DAKLRLEVNMQ--AMKAQFDRDLQA------- 1585
Cdd:COG4913 833 EERFKELLNENSIEFVAdllskLRRAIREIKERIDPLNDSLKRIPfgpGRYLRLEARPRpdPEVREFRQELRAvtsgasl 912
|
650 660 670
....*....|....*....|....*....|...
gi 528481573 1586 RDEQNEEKKRALVKQVREMEAELEDERKQRALA 1618
Cdd:COG4913 913 FDEELSEARFAALKRLIERLRSEEEESDRRWRA 945
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
853-1692 |
1.06e-15 |
|
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: 83.56 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 853 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNIlAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLES 932
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 933 RVEEEEERNQSLQ----------NEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1002
Cdd:TIGR00606 277 RKKQMEKDNSELElkmekvfqgtDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1003 E-------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIA 1075
Cdd:TIGR00606 357 DrhqehirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1076 ELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAEL--------------------QEDLESEKA 1135
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskaeknsltetlkkevkslqNEKADLDRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1136 ARNKAEKLKrDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAEL---------KKAIDDETRNHESQIQEMRQRHGT 1206
Cdd:TIGR00606 517 LRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1207 ALEEIsEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE---------AQLQEVMARFSEGEKV 1277
Cdd:TIGR00606 596 LNKEL-ASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEksskqramlAGATAVYSQFITQLTD 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1278 KGE----LADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLL 1352
Cdd:TIGR00606 675 ENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEkRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1353 EQQEEEEESRKNL---EKQLATLQAQLvETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLE--EKAIAFDKLEKTKNR 1427
Cdd:TIGR00606 755 KVNRDIQRLKNDIeeqETLLGTIMPEE-ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQE 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1428 LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEA---EAREKDTKALSMARALDEALEAKEE 1504
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKDAKEQDSP 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1505 FERLNKQLRAEMEDLISSKDDVGKNVH-ELEKSKRTLEQQVEEMRTQLEELEDelqATEDAKLRLEVNMQAMKAQFdrdl 1583
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL---- 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1584 qardEQNEEKKRALVKQVREMEAELEDERKQRALAV--AAKKKLEMDLKDVEAQIeaanKARDEAIKQLRKLQaQMKDYQ 1661
Cdd:TIGR00606 987 ----EECEKHQEKINEDMRLMRQDIDTQKIQERWLQdnLTLRKRENELKEVEEEL----KQHLKEMGQMQVLQ-MKQEHQ 1057
|
890 900 910
....*....|....*....|....*....|....
gi 528481573 1662 RELEEARTSRDE---IFTQSKENEKKLKSLEAEI 1692
Cdd:TIGR00606 1058 KLEENIDLIKRNhvlALGRQKGYEKEIKHFKKEL 1091
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
852-1452 |
1.10e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 852 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLE 931
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 932 SRVEEEEERNQSLQN--EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEdillledqnSKFLKEKKLLED 1009
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA---------KKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1010 RVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKldaETTDLQDQIAELQAQIDELKIQ-- 1087
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEev 1597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1088 --LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRdlSEELEALKTELEdtldtt 1165
Cdd:PTZ00121 1598 mkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE------ 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1166 aAQQELRSKREQEvaELKKAIDDETRNHESQIQEmrqrhgtalEEISEQLEQAKrvKGNLEKNKQTLESDNKELTNEVKS 1245
Cdd:PTZ00121 1667 -AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE---------AEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKA 1732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1246 LQQAKSESEHKRKKLEAQLQE------VMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQ 1319
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1320 --------LQDTQELLQEETRQKLNLSSriRQLEEEKNNLLEQQEEEEESRKNLEKqlatlQAQLVETKKKLEDDVGALE 1391
Cdd:PTZ00121 1813 ggkegnlvINDSKEMEDSAIKEVADSKN--MQLEEADAFEKHKFNKNNENGEDGNK-----EADFNKEKDLKEDDEEEIE 1885
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1392 GLEEVKRKLQKDMEV----TSQKLEEKAIAFDKLEKTKNRLQqelddlmvDLDHQRQIVSNLEKK 1452
Cdd:PTZ00121 1886 EADEIEKIDKDDIEReipnNNMAGKNNDIIDDKLDKDEYIKR--------DAEETREEIIKISKK 1942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
855-1570 |
1.20e-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: 83.24 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 855 EEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRARLVAKK---QELEEILHDLE 931
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEgvlQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 932 srveeeeernqslQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQNSKFLKEKK-----L 1006
Cdd:pfam15921 198 -------------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkielL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1007 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKK-EEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELK 1085
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQL----SDLESTVSQLRSELREAK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1086 IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTT 1165
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1166 AAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISE---QLEQAK----RVKGNLEKNKQTLESDNKE 1238
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltaQLESTKemlrKVVEELTAKKMTLESSERT 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1239 LTNEVKSLQQAK-------SESEHKRKKLEAQLQEVMARFSEG----------EKVKGELADRTHKIQ---TELDNVSCL 1298
Cdd:pfam15921 498 VSDLTASLQEKEraieatnAEITKLRSRVDLKLQELQHLKNEGdhlrnvqtecEALKLQMAEKDKVIEilrQQIENMTQL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1299 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeeESRKNLEK-QLATLQAQLV 1377
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEAR------------VSDLELEKvKLVNAGSERL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1378 ETKKKLEDDVGALegLEEVK------RKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1451
Cdd:pfam15921 646 RAVKDIKQERDQL--LNEVKtsrnelNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1452 KQ-KKFDQMLAEEKTISARyaeerdRAEAEAREKDTKAL--SMARALDEALEAKEEFERLNKqlraEMEDLISSKDDVGK 1528
Cdd:pfam15921 721 SDgHAMKVAMGMQKQITAK------RGQIDALQSKIQFLeeAMTNANKEKHFLKEEKNKLSQ----ELSTVATEKNKMAG 790
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 528481573 1529 NVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLEV 1570
Cdd:pfam15921 791 ELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
831-1529 |
1.58e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 831 KLRHWQWWRLFTKVKPLLQVTRQ---EEEMQAKDEELIKVKERQVKVENELVEMERKhqqlLEEKNILAEQLQAETELFA 907
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 908 EAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQ-NEKKKMQSHIQDLEEQLDEEEAARQ-----KLQLEKVTAEA 981
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKKKEEAKKKADAAKKKaeekkKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 982 KIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvKNKQEMMMVDLEERLKKEEKTRQELEKAKR 1061
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1062 KLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAE 1141
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1142 KLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTAlEEISEQLEQAKRV 1221
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKV 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1222 ----KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRthkiqteldnvsc 1297
Cdd:PTZ00121 1636 eqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKK------------- 1696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1298 llEDAEKKGIKLTKdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnLLEQQEEEEESRKNLEKQLATLQAQLV 1377
Cdd:PTZ00121 1697 --EAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK--KKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1378 ETKKKLEDDVgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ-KKF 1456
Cdd:PTZ00121 1771 EEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEaDAF 1849
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481573 1457 DQMLAEEKTISaryAEERDRAEAEAREKDTKalsmaRALDEALEAKEEFERLNKQlraEMEDLISSKDDVGKN 1529
Cdd:PTZ00121 1850 EKHKFNKNNEN---GEDGNKEADFNKEKDLK-----EDDEEEIEEADEIEKIDKD---DIEREIPNNNMAGKN 1911
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1209-1928 |
1.72e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1209 EEISEQLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmARFSEGEKVKGELADRT 1285
Cdd:PTZ00121 1053 DGNHEGKAEAKAHVGQDEGLKPSYkdfDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1286 HKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNL 1365
Cdd:PTZ00121 1131 EEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1366 EKQLATLQAQLVETKKKLEddvgALEGLEEVKRKlqkdmevtsqklEEKAiafDKLEKTKNRLQ-QELDDLMVDLDHQRQ 1444
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAE----AVKKAEEAKKD------------AEEA---KKAEEERNNEEiRKFEEARMAHFARRQ 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1445 IVSNLEKKQKKFDQMLAEE--KTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISS 1522
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEkkKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1523 KDDVGKNVHELEKSKR---TLEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKaQFDRDLQARDEQNEEKKRA 1596
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEkaeAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKA 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1597 L-VKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIF 1675
Cdd:PTZ00121 1428 EeKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1676 TQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDE---LADEISNSASGKAAllDEKRRLEARIAQLEEELEEEQ 1752
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekkKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1753 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLE--RQNKDLKSKLQEL----EGSVKSKFKASIAALEAKI 1826
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLkkkeAEEKKKAEELKKAEEENKI 1661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1827 LQLEEQLEQEAKERAAAN-KIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeAEEEATRANASRRK 1905
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA---EEENKIKAEEAKKE 1738
|
730 740
....*....|....*....|....*
gi 528481573 1906 LQRELDDATEA--SEGLSREVNTLK 1928
Cdd:PTZ00121 1739 AEEDKKKAEEAkkDEEEKKKIAHLK 1763
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1294-1813 |
1.85e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.42 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1294 NVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQeetrqklNLSSRIRQLEEEKNNLLEQQEEEEEsrknLEKQLATLQ 1373
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELE-------KLEKEVKELEELKEEIEELEKELES----LEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1374 AQLVETKKKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ 1453
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1454 KKFDQMLAEEKTISARYAEERDRAEAeaREKDTKALSMARALdealeaKEEFERLNKQLRAEmedlisSKDDVGKNVHEL 1533
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAK------KEELERLKKRLTGL------TPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1534 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFDRDLQARDEQNEEKKRALvkqvREMEAELEDERK 1613
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL----EEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1614 QRALAVAAKKKLEMDLKDVEAQIEAANKAR--DEAIKQLRKLQAQMKDYQRE-LEEARTSRDEIFTQSKENEKKLKSLEA 1690
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1691 EILQLQE---DLASSERARRHAEQERDELADEISNSASGKAALLDEK---------------------RRLEARIAQLEE 1746
Cdd:PRK03918 547 ELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaekelEREEKELKKLEE 626
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1747 ELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSaaQKSENARQQLERQNKDLKSKLQELEGSVKS 1813
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
868-1696 |
4.79e-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: 81.32 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 868 KERQVKVENELVEMERKHQQLLEEKNILAEQlqaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNE 947
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEK---------QKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 948 KKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDilLLEDQNSKFLKEKKLL---EDRVGEMTSQLAEEEEK 1024
Cdd:pfam15921 144 RNQLQNTVH----------------ELEAA------KCLKED--MLEDSNTQIEQLRKMMlshEGVLQEIRSILVDFEEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1025 AKNlgKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI-DELKIQLAKKEEELQAVLARGD 1103
Cdd:pfam15921 200 SGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1104 EEVA----QKNNALKQLRELQAQLAELQEDlesekaARNKAEKLKRDLSE----------ELEALKTELEDTLDTTAAQQ 1169
Cdd:pfam15921 278 VEITglteKASSARSQANSIQSQLEIIQEQ------ARNQNSMYMRQLSDlestvsqlrsELREAKRMYEDKIEELEKQL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1170 ELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQA 1249
Cdd:pfam15921 352 VLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1250 KSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKL---TKDVSSLESQLQDTQEL 1326
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLessERTVSDLTASLQEKERA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1327 LQEETRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEV 1406
Cdd:pfam15921 512 IEATNAEITKLRSRV----DLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI---LRQQIENMTQLVGQHGRT 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1407 TSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfDQMLAEEKTISAryAEERDRAEAEAREKDT 1486
Cdd:pfam15921 585 AGAMQVEKA----QLEKEINDRRLELQEFKILKDKKDAKIRELEARVS--DLELEKVKLVNA--GSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1487 KALSMARALDEALEA-KEEFERLNKQLRAEMEdlisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1565
Cdd:pfam15921 657 QLLNEVKTSRNELNSlSEDYEVLKRNFRNKSE--------------EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1566 ---LRLEVNMQamkaqfdRDLQARDEQNEekkrALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQieaanka 1642
Cdd:pfam15921 723 ghaMKVAMGMQ-------KQITAKRGQID----ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE------- 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 528481573 1643 RDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQ 1696
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1251-1932 |
6.23e-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: 81.27 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1251 SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV----SCLLEDAEKKGIKLTKDVSSLESQLQDTQEL 1326
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1327 LQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNL-EKQLATLQAQLVETKKKLEddvgALEGLEEVKRKLQKDME 1405
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIA----SLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1406 VTSQKLEEKaiaFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKD 1485
Cdd:TIGR02169 322 ERLAKLEAE---IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1486 TKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1565
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1566 LRLEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMEAELE------------DERKQRALAVAAKKKLEMDLKDVE 1633
Cdd:TIGR02169 479 DRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNNVVVEDD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1634 AQIEaankardEAIKQLRKLQA---------QMKDYQRELEEARTS------------------------RDEIFTQSKE 1680
Cdd:TIGR02169 558 AVAK-------EAIELLKRRKAgratflplnKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfGDTLVVEDIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1681 NEKKLK------SLEAEILQLQEDLASSERARRHAE-------QERDELADEISNSASGKAALLDEKRRLEARIAQLEEE 1747
Cdd:TIGR02169 631 AARRLMgkyrmvTLEGELFEKSGAMTGGSRAPRGGIlfsrsepAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1748 LEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEA--- 1824
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEArls 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1825 --KILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANAS 1902
Cdd:TIGR02169 790 hsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750
....*....|....*....|....*....|
gi 528481573 1903 RRKLQRELDDATEASEGLSREVNTLKNRLR 1932
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1366-1933 |
6.76e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.85 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1366 EKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafdklEKtknrlQQELDDLMVDLDHQRQI 1445
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------ER-----REELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1446 VSNLEKKQKKFDQMLAEEKTISARYAEERD--RAEAEAREKDTKALSMARaldEALEAKEEferlnkQLRAEMEDLISSK 1523
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARR---EELEDRDE------ELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1524 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdRDLQARDEQNEEKKRALVKQVRE 1603
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV---------------EDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1604 MEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAikqlRKLQAQMK--DYQRELEEArtsrdEIFTQSKEN 1681
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA----EALLEAGKcpECGQPVEGS-----PHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1682 EKKLKSLEAEILQLQEDLASSErarrhaeqERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDR 1761
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1762 frkttmqVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfkASIAALEAKILqleeqleqeakerA 1841
Cdd:PRK02224 546 -------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIA-------------D 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1842 AANKIVRRTEKKlkEVFMQVEDERRhadqykEQMEKANSRMKQLKRQ-----LEEAEEEATRANASRRKLQRELDDATEA 1916
Cdd:PRK02224 604 AEDEIERLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
570
....*....|....*..
gi 528481573 1917 SEGLSREVNTLKNRLRR 1933
Cdd:PRK02224 676 RDDLQAEIGAVENELEE 692
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1128-1858 |
1.43e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1128 EDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQrhgta 1207
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----- 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1208 lEEISEQLEQAKRVkgnlEKNKQTLESDNKEltnEVKSLQQAKSESEHKRKKLEAQLQEVmaRFSEGEKvKGELADRTHK 1287
Cdd:PTZ00121 1166 -AEEARKAEDAKKA----EAARKAEEVRKAE---ELRKAEDARKAEAARKAEEERKAEEA--RKAEDAK-KAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1288 IQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEK 1367
Cdd:PTZ00121 1235 AKKDAEEAK--KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1368 QlATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQElddlmvdldhqrQIVS 1447
Cdd:PTZ00121 1310 K-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA---DEAEAAEEKAEAA------------EKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1448 NLEKKQKKFDQMLAEEKtisaRYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVG 1527
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEK----KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1528 KNVHELEKSKRTLEQQVEEMRT--QLEELEDELQATEDAKLRLEVNMQamKAQFDRDLQARDEQNEEKKRALVKQVREME 1605
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1606 AELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1685
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1686 KSLEA----EILQLQEDLASSERARRHAEQERDELADEISNS---------ASGKAALLDEKRRLEARIAQLEEELEEEQ 1752
Cdd:PTZ00121 1608 KAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1753 SNMELLNDRFRKTTMQVDTLNTELAGERSAAQ---KSENAR----QQLERQNKDLKSKLQEL--EGSVKSKFKASIAALE 1823
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENkikaEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEE 1767
|
730 740 750
....*....|....*....|....*....|....*..
gi 528481573 1824 AKILQLEEQLEQEAKERAAANKIVRR--TEKKLKEVF 1858
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRmeVDKKIKDIF 1804
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1117-1826 |
1.98e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1117 RELQAQLAELQEDLESEKAARNKAEKLKR--DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKkaiDDETRNHE 1194
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR---LELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1195 SQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE-LTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1273
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1274 GEKvkgELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlle 1353
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL--------- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1354 qqeeeeesRKNLEKQLATLQAQ------LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNR 1427
Cdd:COG4913 446 --------RDALAEALGLDEAElpfvgeLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1428 LQqelddlmVDLDHqrqivsnLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFE 1506
Cdd:COG4913 512 GR-------LVYER-------VRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1507 RLNKQLRAEmeDLISSkddvGKNVHELEKSKRTLEQQV--EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQ 1584
Cdd:COG4913 572 RHPRAITRA--GQVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEA--------LE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1585 ARDEQNEEKKRALVKQVREMEAELEDERKQRALAvaakkklemdlkDVEAQIEAANKARDEaikqLRKLQAQMKDYQREL 1664
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEIDVASAEREIA------------ELEAELERLDASSDD----LAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1665 EEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLassERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQL 1744
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1745 EEELEEEQSNMELLNDRFRKT-TMQVDTLNTELAGERSAAQKsenaRQQLERQnkDLKSKLQELEGSVKSKFKASIAALE 1823
Cdd:COG4913 779 RARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEED--GLPEYEERFKELLNENSIEFVADLL 852
|
...
gi 528481573 1824 AKI 1826
Cdd:COG4913 853 SKL 855
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
862-1537 |
2.63e-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: 78.61 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 862 EELIKVKERQVKVENELVEMERKHQqllEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHD----------LE 931
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 932 SRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIK-KMEEDILLLEDQNSKFLKEKKLLEDR 1010
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1011 VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTD----LQDQIAELQAQIDELKI 1086
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1087 ------QLAKKEE----ELQAVLARGDEEVAQKNNALKQLREL-----------QAQLAELQEDLESEKAARNKAEKLKR 1145
Cdd:pfam05483 322 atkticQLTEEKEaqmeELNKAKAAHSFVVTEFEATTCSLEELlrteqqrleknEDQLKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1146 DLSEELEALKT---ELEDTLDTTAAQQELRSK---REQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISEQLE 1216
Cdd:pfam05483 402 NKEVELEELKKilaEDEKLLDEKKQFEKIAEElkgKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1217 QAKRVKGNLEKNKQTLESDNKELTNE----VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1292
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1293 DNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1372
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKL 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1373 QAQLVETKKKLEDDVGALEGLEEVKRklqkdmeVTSQKLEEKAIAFDKLEKTKNRLQQELDdlmVDLDHQ-RQIVSNLEK 1451
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDKK-------ISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKiAEMVALMEK 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1452 KQKKFDQMLaeektisaryaEERDRAEAEAREKDTKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNV 1530
Cdd:pfam05483 712 HKHQYDKII-----------EERDSELGLYKNKEQEQSSAKAALEIELSnIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
....*..
gi 528481573 1531 HELEKSK 1537
Cdd:pfam05483 781 AILKDKK 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
847-1432 |
2.99e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.54 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 847 LLQVTRQEEEMQAKDeelikVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLvakkQELEEI 926
Cdd:PRK02224 189 LDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 927 LHDLESRVEEEEERNQSLQNEkkkmqshIQDLEeqldeeeAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1006
Cdd:PRK02224 260 IEDLRETIAETEREREELAEE-------VRDLR-------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1007 LEDRVGEMTSQLAEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1086
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDAD-------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1087 QLAKKEEELQAVLARGDEEVAQKNnalkqlrELQAQLAELQEDLESEKAARNKAEKLKR-----------------DLSE 1149
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERD-------ELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsphvETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1150 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAID--DETRNHESQIQEMRQRHGTALEEISEQLEQakrvkgnLEK 1227
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEE-------LRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1228 NKQTLEsdnkeltnevkslqqakSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTeLDNVSCLLEDAEKKGi 1307
Cdd:PRK02224 545 RAAELE-----------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1308 kltKDVSSLESQLQDTQElLQEETRQKL-NLSSRIRQLEEEknNLLEQQEEEEESRKNLEKQLATLQ---AQLVETKKKL 1383
Cdd:PRK02224 606 ---DEIERLREKREALAE-LNDERRERLaEKRERKRELEAE--FDEARIEEAREDKERAEEYLEQVEeklDELREERDDL 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 528481573 1384 EDDVGALEG----LEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQQEL 1432
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 ... |
847-1595 |
6.54e-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: 77.70 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 847 LLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQqlleeknilaEQLQAETELFAEAEEMRARLVAKKQELEEI 926
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE----------KELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 927 LHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKL 1006
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1007 LEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKI 1086
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1087 QLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA 1166
Cdd:pfam02463 518 DGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1167 AQQELRSKREQEVAELKKAIDDETRNHES---QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEV 1243
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEgilKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1244 KSLQQAKSESE----HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQ 1319
Cdd:pfam02463 678 IQELQEKAESElakeEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1320 LQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLvETKKKLEDDVGALEGLEEVKRK 1399
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA-ELLEEEQLLIEQEEKIKEEELE 836
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1400 LQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEA 1479
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEELLQELL-----LKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1480 EAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQ 1559
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-------EEEERNKRLLLAKEELGKVNLMAIEEFE 984
|
730 740 750
....*....|....*....|....*....|....*.
gi 528481573 1560 ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKR 1595
Cdd:pfam02463 985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1209-1877 |
7.67e-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: 76.98 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1209 EEISEQLEQAKRVKGNLEKNKQ---TLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegEKVKGELADRT 1285
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDkinKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKEN-------KKNIDKFLTEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1286 HKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLS---SRIRQLEEEKNNLLEQQEEEEESR 1362
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1363 KNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL--MVDLD 1440
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1441 HQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEME 1517
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1518 DLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQatedaKLRLEVNmqamkaqfdrDLQARDEQNEEKKRAL 1597
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE-----RLKETII----------KNNSEIKDLTNQDSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1598 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1677
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1678 SKENEKKLKSLEAEILQLQEDLASSErarrhAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1757
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKEN-----LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1758 -------LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkSKFKASIAALE--AKILQ 1828
Cdd:TIGR04523 608 kekkissLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII----KKIKESKTKIDdiIELMK 683
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 528481573 1829 LEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEK 1877
Cdd:TIGR04523 684 DWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELEN 732
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
810-1462 |
7.92e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 77.32 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 810 AKKQQQLSALKVLqRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELiKVKERQVKVENELVEMERKHQQLL 889
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-RAQEAVLEETQERINRARKAAPLA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 890 EEKNILAEQLQaetelfaEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAAR 969
Cdd:TIGR00618 297 AHIKAVTQIEQ-------QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 970 QKLQleKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKE 1049
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1050 EKTRQ-------ELEKAKRKLDAETTDLQDQ-----------------IAELQAQIDELKIQLAKKEEELQAV------- 1098
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKeqihlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1099 --LARGDEEVAQKNNALK----QLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELR 1172
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1173 SK-----REQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQL------EQAKRVKGNLEKNKQTLESDNKELTN 1241
Cdd:TIGR00618 608 DMlaceqHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervrEHALSIRVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1242 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDvSSLESQLQ 1321
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA-RTEAHFNN 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1322 DTQELLQEETRQKL-----NLSSRIRQLEEeknnlleqqeeeeesrknLEKQLATLQAQLvetKKKLEDDVGALEGLEEv 1396
Cdd:TIGR00618 767 NEEVTAALQTGAELshlaaEIQFFNRLREE------------------DTHLLKTLEAEI---GQEIPSDEDILNLQCE- 824
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1397 krKLQKDMEVTSQKLEEkaiafdklektKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1462
Cdd:TIGR00618 825 --TLVQEEEQFLSRLEE-----------KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
884-1633 |
1.33e-13 |
|
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: 76.55 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 884 KHQQLLEEKNILAEQLQAETELfaeAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQshiqdleeqld 963
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLC---TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 964 eeeaARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFlkekklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLE 1043
Cdd:TIGR00618 254 ----EQLKKQQLLKQLRARIEELRAQEAVLEETQERI------------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1044 ERLKKEEKTRQELEKAKrKLDAETTDLQDQIAELQAQIDELKIQ-----LAKKEEELQAVLARGDEEVAQKNNALKQLRE 1118
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHV-KQQSSIEEQRRLLQTLHSQEIHIRDAhevatSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1119 LQAQLAELQEDLESEKAARNKAEklkRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQ 1198
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1199 EMRQrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1278
Cdd:TIGR00618 474 QLQT-----KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1279 GELADRTHKIQTELDNVSCLLEDAEKKGIK---LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQ 1355
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCdnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1356 EEEEESRkNLEKQLATLQAQLVETKKKLEDdvgaleglEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1435
Cdd:TIGR00618 629 DVRLHLQ-QCSQELALKLTALHALQLTLTQ--------ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1436 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAE 1515
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1516 MEDLISskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLqardeqneEKKR 1595
Cdd:TIGR00618 780 LSHLAA----------EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKS 841
|
730 740 750
....*....|....*....|....*....|....*...
gi 528481573 1596 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVE 1633
Cdd:TIGR00618 842 ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1380-1743 |
3.57e-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: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1380 KKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqivsnlekkqkkfdqm 1459
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE----------------------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1460 laeektisaRYAEERDRAEaearekDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1539
Cdd:TIGR02169 212 ---------RYQALLKEKR------EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1540 LEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1611
Cdd:TIGR02169 277 LNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1612 RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN-------EKK 1684
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlNAA 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1685 LKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQ 1743
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1066-1725 |
9.23e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 9.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1066 ETTDLQDQIAELQAQIDELkiqlakkeEELQAVLargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNK-----A 1140
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1141 EKLKRDLSEELEALKTELEDTldttaaqqelrskrEQEVAELKKAIdDETRNHESQIQEMRQRHGTaleeisEQLEQAKR 1220
Cdd:COG4913 287 QRRLELLEAELEELRAELARL--------------EAELERLEARL-DALREELDELEAQIRGNGG------DRLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1221 vkgnleknkqtlesdnkeltnEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvkgELADRTHKIQTELDNVSCLLE 1300
Cdd:COG4913 346 ---------------------EIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1301 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLeeeknnlleqqeeeeesRKNLEKQLATLQAQ----- 1375
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-----------------RDALAEALGLDEAElpfvg 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1376 -LVETKKKLEDDVGALEGleeVKRKLQKDMEVtSQKLEEKAIAFdkLEKTKNRLQqelddlmVDLDHqrqivsnLEKKQK 1454
Cdd:COG4913 465 eLIEVRPEEERWRGAIER---VLGGFALTLLV-PPEHYAAALRW--VNRLHLRGR-------LVYER-------VRTGLP 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1455 KFDQMLAEEKTISARYAEERDRAEAEAREkdtkalSMARALD-EALEAKEEFERLNKQLRAemEDLISSKDDVG-KNVHE 1532
Cdd:COG4913 525 DPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDyVCVDSPEELRRHPRAITR--AGQVKGNGTRHeKDDRR 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1533 LEKSKRTL----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdLQARDEQNEEKKRalVKQVREMEAEL 1608
Cdd:COG4913 597 RIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDEID--VASAEREIAEL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1609 EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftQSKENEKKLKSL 1688
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALL 751
|
650 660 670
....*....|....*....|....*....|....*..
gi 528481573 1689 EAEILQLQEDlASSERARRHAEQERDELADEISNSAS 1725
Cdd:COG4913 752 EERFAAALGD-AVERELRENLEERIDALRARLNRAEE 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1208-1862 |
1.60e-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: 72.75 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1208 LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA---RFSEGEKVKGELadr 1284
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSdlsKINSEIKNDKEQ--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1285 THKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKN 1364
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1365 LEKQLATLQAqLVETKKKLEDDvgaLEGLEEVKRKLQKDMEVTSQKLEEKAiafDKLEKTKNRLQQELDDlmvdldhQRQ 1444
Cdd:TIGR04523 199 LELLLSNLKK-KIQKNKSLESQ---ISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDE-------QNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1445 IVSNLEKKQKKFDQmlAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRaEMEDLISSKD 1524
Cdd:TIGR04523 265 IKKQLSEKQKELEQ--NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS-QNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1525 DVgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREM 1604
Cdd:TIGR04523 342 EQ---ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1605 EAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKK 1684
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1685 LKSLEAEILQLqedlasserarrhaEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEeleeeqsnmELLNDRFRK 1764
Cdd:TIGR04523 498 LKKLNEEKKEL--------------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED---------ELNKDDFEL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1765 TTmqvDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAAN 1844
Cdd:TIGR04523 555 KK---ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
650
....*....|....*...
gi 528481573 1845 KIVRRTEKKLKEVFMQVE 1862
Cdd:TIGR04523 631 SIIKNIKSKKNKLKQEVK 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1365-1912 |
2.54e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1365 LEKQLATLQaQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIafDKLEKTKNRLQQELDDLMVDLDHQRQ 1444
Cdd:COG4913 247 AREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1445 IVSNLEKkqkkfdQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLI 1520
Cdd:COG4913 324 ELDELEA------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAalglPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1521 SSKDDVGKNVHELEKSKRTLEQQveemrtqLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQneekkralVK- 1599
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRE-------LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE--------LPf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1600 -----QVREMEAE-----------------LEDERKQRALAVAAKKKLEMDL-------KDVEAQIEAA----------- 1639
Cdd:COG4913 463 vgeliEVRPEEERwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRLvyervrtGLPDPERPRLdpdslagkldf 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1640 --NKARDEAIKQLRKL--------QAQMKDYQREL---------EEARTSRDEIFTQSK-----ENEKKLKSLEAEILQL 1695
Cdd:COG4913 543 kpHPFRAWLEAELGRRfdyvcvdsPEELRRHPRAItragqvkgnGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1696 QEDLASSERARRHAEQERDELAD---------EISNSASGKAALLDEKRRLEARIAQleeeleeeqsnMELLNDRFRKTT 1766
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELER-----------LDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1767 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvkskfkasiAALEAKILQLEEQLEQEAKERAAANKI 1846
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-----------DRLEAAEDLARLELRALLEERFAAALG 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1847 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKAnsrMKQLKRQLEEAEEEATRANASRRKLQRELDD 1912
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDR 823
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1017-1743 |
3.10e-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: 72.29 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1017 QLAEEEEK----AKNLGKVKNKQEMMMVDLE---ERL----------KKEEKTRQELEKAKRKLDAET---TDLQDQIAE 1076
Cdd:COG3096 300 QLAEEQYRlvemARELEELSARESDLEQDYQaasDHLnlvqtalrqqEKIERYQEDLEELTERLEEQEevvEEAAEQLAE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1077 LQAQ-------IDELKIQLAKKEEEL-----------QAVLARGDEEVAQKNNAL--KQLRELQAQL-AELQEDLESEKA 1135
Cdd:COG3096 380 AEARleaaeeeVDSLKSQLADYQQALdvqqtraiqyqQAVQALEKARALCGLPDLtpENAEDYLAAFrAKEQQATEEVLE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1136 ARNK---AEKLKRDLSEELEALK-----TELEDTLDTtaAQQELRSKREQE-----VAELKKAIDDETRNHESQIQEMRQ 1202
Cdd:COG3096 460 LEQKlsvADAARRQFEKAYELVCkiageVERSQAWQT--ARELLRRYRSQQalaqrLQQLRAQLAELEQRLRQQQNAERL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1203 rhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfsegEKVKGELA 1282
Cdd:COG3096 538 -----LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR----APAWLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1283 DRTHKIQTEldnVSCLLEDAekkgikltkdvSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR 1362
Cdd:COG3096 609 DALERLREQ---SGEALADS-----------QEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRL 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1363 KNLEKQL-ATLQAQLVEtKKKLEDD--VGALEG----------LEEVKRKLQkDMEVTSQKL---EEKAIAFDKlektKN 1426
Cdd:COG3096 675 LALAERLgGVLLSEIYD-DVTLEDApyFSALYGparhaivvpdLSAVKEQLA-GLEDCPEDLyliEGDPDSFDD----SV 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1427 RLQQELDDLMVDLDHQRQI-VSNLEK--------KQKKFDQMLAEEKTISARYAEER------DRAEAEAREKDTKALSM 1491
Cdd:COG3096 749 FDAEELEDAVVVKLSDRQWrYSRFPEvplfgraaREKRLEELRAERDELAEQYAKASfdvqklQRLHQAFSQFVGGHLAV 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1492 ARALDEALEAKE------EFERLNKQLRAEMEDLISSKDDVGKNVHELEK--------SKRTLEQQVEEMRTQLEELED- 1556
Cdd:COG3096 829 AFAPDPEAELAAlrqrrsELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllADETLADRLEELREELDAAQEa 908
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1557 --ELQATEDAKLRLEVNMQAMK---AQFDRdLQARDEQNEEKKRALVKQVREMEaeledERKQRALAVAAKKKLEM---- 1627
Cdd:COG3096 909 qaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----EVVQRRPHFSYEDAVGLlgen 982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1628 -DLKD-VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEaeilqLQEDLASSERA 1705
Cdd:COG3096 983 sDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELG-----VQADAEAEERA 1057
|
810 820 830
....*....|....*....|....*....|....*...
gi 528481573 1706 RrhaeQERDELADEISNSASGKAALLDEKRRLEARIAQ 1743
Cdd:COG3096 1058 R----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1072-1719 |
3.28e-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: 71.92 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1072 DQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLS--- 1148
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlr 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1149 ---EELEALKTELEDT-------------LDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEIS 1212
Cdd:TIGR00618 267 ariEELRAQEAVLEETqerinrarkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1213 EQLEQAKRVKGNLEKNKQTL----ESDNKELTNEVKSLQQAKSESEHKRK-------KLEAQLQEVMARFSEGEKVKGEL 1281
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSireiSCQQHTLTQHIHTLQQQKTTLTQKLQslckeldILQREQATIDTRTSAFRDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1282 ADRTHKIQTELD----------NVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1351
Cdd:TIGR00618 427 AHAKKQQELQQRyaelcaaaitCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1352 LEQQEEEEESRKNLEKQLAT--LQAQLVETKKKLEDDVGALEGLEEVKRK----LQKDMEVTSQKLEEKAIAFDKLEKTK 1425
Cdd:TIGR00618 507 CGSCIHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVYHQLTSERKqrasLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1426 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKAlsmARALDEALEAKEEF 1505
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH---ALQLTLTQERVREH 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1506 ERLNKQLRAEMEDLISSKDDVGKNVHE-LEKSKRTLEQQVEEMRTQLEELEdelqatEDAKLRLEVNMQAMKAQfdRDLQ 1584
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEqLTYWKEMLAQCQTLLRELETHIE------EYDREFNEIENASSSLG--SDLA 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1585 ARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL 1664
Cdd:TIGR00618 736 AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1665 EEARTSRDEIFTQSKENEK----KLKSLEAEILQLQEDLASSERARRHAEQERDELADE 1719
Cdd:TIGR00618 816 EDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1364-1932 |
1.51e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1364 NLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLmvdlDHQR 1443
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1444 QIVSNLEKKQKKFDQmlaEEKTISARYAEERDRAEaEAREKDTKALSMARALDEALEAKEEFERLNKqlraEMEDLISSK 1523
Cdd:PRK03918 238 EEIEELEKELESLEG---SKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSE----FYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1524 DDVGKNVHELEKSKRTLEQQV---EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqFDRDLQARDEQNEEKKRALVKQ 1600
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1601 VREMEAELEDERKqralavaAKKKLEMDLKDVEAQI---EAANKARDEAIKQLRKLQAQMKDYQRELEEARtsRDEIFtq 1677
Cdd:PRK03918 386 PEKLEKELEELEK-------AKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKCPVCGRELTEEH--RKELL-- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1678 sKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsgkaaLLDEKRRLEARIAQLEEELEEEQSN-ME 1756
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLEELEKKAEeYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1757 LLNDRFRKTTMQVDTLNTELagerSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLeqe 1836
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY--- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1837 aKERAAANKIVRRTEKKLKEVfmqvEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEAT-----RANASRRKLQRELD 1911
Cdd:PRK03918 602 -NEYLELKDAEKELEREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeeyeELREEYLELSRELA 676
|
570 580
....*....|....*....|.
gi 528481573 1912 DATEASEGLSREVNTLKNRLR 1932
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLE 697
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
978-1771 |
1.67e-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: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 978 TAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM------MVDLEERLKKEEK 1051
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIehnlskIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1052 TRQELEKAKRKLDAETTDLQDQIAElqaQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLaELQEDLE 1131
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDE---QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL-LVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1132 SEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQevaeLKKAIDDETRNHESQIQEMRQRHGTALEEI 1211
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTL----VIERQEDEAKTAAQLCADLQSKERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1212 SEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEhKRKKLEAQLQEVMARFSegekvkgeLADRTHKIQTE 1291
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELRKAERELS--------KAEKNSLTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1292 LDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQL 1369
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmlTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1370 ATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDME-VTSQKLEEKAIAFDKLekTKNRLQQELDDLMVDLDHQRQIVSN 1448
Cdd:TIGR00606 580 HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEsKEEQLSSYEDKLFDVC--GSQDEESDLERLKEEIEKSSKQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1449 LEKKQKKFDQMLAEEKTISARYAEERDR---AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSK-- 1523
Cdd:TIGR00606 658 LAGATAVYSQFITQLTDENQSCCPVCQRvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRqs 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1524 --DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQaTEDAKLRLEVNMQAMKAQFDRdLQARDEQNEekkralvKQV 1601
Cdd:TIGR00606 738 iiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG-TIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKI 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1602 REMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIKQLRKLQA---QMKDYQRELEEARTSRDEIFT 1676
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQQVNQEKQEKQheLDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEE 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1677 QSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADeiSNSASGKAALL------------------------- 1731
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS--SKETSNKKAQDkvndikekvknihgymkdienkiqd 966
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 528481573 1732 ---DEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1771
Cdd:TIGR00606 967 gkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT 1009
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1013-1741 |
1.82e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.99 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1013 EMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL--QDQIAELQAQIDELKIQLak 1090
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqQEKIERYQADLEELEERL-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1091 keEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESE----------KAARNKAEKLKRD-------LSE 1149
Cdd:PRK04863 365 --EEQNEVVEEADEQQeeneARAEAAEEEVDELKSQLADYQQALDVQqtraiqyqqaVQALERAKQLCGLpdltadnAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1150 ELEALKTELED-TLDTTAAQQELRSK---REQ--EVAELKKAIDDET-------------------RNHESQIQEMRQRH 1204
Cdd:PRK04863 443 WLEEFQAKEQEaTEELLSLEQKLSVAqaaHSQfeQAYQLVRKIAGEVsrseawdvarellrrlreqRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1205 GTALEEISEQ------LEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKvk 1278
Cdd:PRK04863 523 SELEQRLRQQqraerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA-- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1279 geLADRTHKIQTELDNVSclledaEKKGIKLTkDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNnlleqqeee 1358
Cdd:PRK04863 601 --RAPAWLAAQDALARLR------EQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE--------- 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1359 eesrknlekQLATLQAQLVETKKKLEDDVGAL---EGLEEVkrKLQkDMEVTSQKLEE--KAIAFDKLEKTKNRLQQE-- 1431
Cdd:PRK04863 663 ---------RLSQPGGSEDPRLNALAERFGGVllsEIYDDV--SLE-DAPYFSALYGParHAIVVPDLSDAAEQLAGLed 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1432 -LDDLMV---DLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEErDRAEAEAREKDTKALSMARALDEALEAKEEF-- 1505
Cdd:PRK04863 731 cPEDLYLiegDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEV-PLFGRAAREKRIEQLRAEREELAERYATLSFdv 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1506 ---ERLNKQLR----------------AEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL--------------- 1551
Cdd:PRK04863 810 qklQRLHQAFSrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnllad 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1552 -------EELEDELQATEDAKL-------------RLEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMeaeleDE 1611
Cdd:PRK04863 890 etladrvEEIREQLDEAEEAKRfvqqhgnalaqlePIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TE 963
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1612 RKQRALAVAAKKKLEMDLKDVE------AQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL 1685
Cdd:PRK04863 964 VVQRRAHFSYEDAAEMLAKNSDlneklrQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL 1043
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1686 KSleaeiLQLQEDLASSERARRHaeqeRDELADEISNSASGKAALLDEKRRLEARI 1741
Cdd:PRK04863 1044 QD-----LGVPADSGAEERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
809-1160 |
2.05e-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: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 809 FAKKQQQLSALKVLQRNCAAYLKLRHWQWWRLFTKVKPL-LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQ 887
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 888 LLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEeqldeeea 967
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-------- 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 968 arqklqlekvtaeAKIKKMEEDILLLEDQnskflkekklledrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLK 1047
Cdd:TIGR02168 845 -------------EQIEELSEDIESLAAE--------------IEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1048 KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQK-NNALKQLRELQAQLAEL 1126
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRL 977
|
330 340 350
....*....|....*....|....*....|....
gi 528481573 1127 QEDLESEKAARNKAEKLKRDLSEELEALKTELED 1160
Cdd:TIGR02168 978 ENKIKELGPVNLAAIEEYEELKERYDFLTAQKED 1011
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1043-1936 |
3.23e-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: 68.83 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1043 EERLKKEEKT---RQELEKAKRKLDAEttdlQDQIAELQAQIDELKIQLAKKEEELQAvlarGDEEVAQKNNALKQLREL 1119
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQA----ASDHLNLVQTALRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1120 ---QAQLAELQEDLESEKAARnkaeklkrdlsEELEALKTELEDTLdtTAAQQELRSKREQeVAELKKAID-DETRNheS 1195
Cdd:COG3096 350 eryQEDLEELTERLEEQEEVV-----------EEAAEQLAEAEARL--EAAEEEVDSLKSQ-LADYQQALDvQQTRA--I 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1196 QIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarfsegE 1275
Cdd:COG3096 414 QYQQAVQ----ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV-------C 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1276 KVKGELaDRthkiqteldnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEknnLLE 1353
Cdd:COG3096 483 KIAGEV-ER---------------SQAWQTARELLRRYRSQQALAQRLQQLRAQlaELEQRLRQQQNAERLLEE---FCQ 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1354 QQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVgalEGLEEVKRKLQkDMEVTSQKLEEKA----IAFDKLEKTKNRLQ 1429
Cdd:COG3096 544 RIGQQLDAAEELEELLAELEAQLEELEEQAAEAV---EQRSELRQQLE-QLRARIKELAARApawlAAQDALERLREQSG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1430 QELDDLmVDLDHQRQIVSNLEKKQKKFDQMLAEEKtisARYAEERDRAEAEAREKDTKALSMARAL----------DEAL 1499
Cdd:COG3096 620 EALADS-QEVTAAMQQLLEREREATVERDELAARK---QALESQIERLSQPGGAEDPRLLALAERLggvllseiydDVTL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1500 EAKEEFERLNKQLR---------------AEMED------LIS----SKDDVGKNVHELEK------SKRTL-------- 1540
Cdd:COG3096 696 EDAPYFSALYGPARhaivvpdlsavkeqlAGLEDcpedlyLIEgdpdSFDDSVFDAEELEDavvvklSDRQWrysrfpev 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1541 --------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDL-----QARDEQNEEKKRALVKQVREMEA 1606
Cdd:COG3096 776 plfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELER 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1607 ELED----ERKQRALAVAAKKKLEMdlkdVEAQIEAANKARDEAikqlrkLQAQMKDYQRELEEARTSRDEIFTQSK--- 1679
Cdd:COG3096 851 ELAQhraqEQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELDAAQEAQAFIQQHGKala 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1680 ENEKKLKSLEAEILQ---LQEDLASSERARRHAEQERDELADEISNSA----SGKAALLDEKRRLEARIAQLEEELEEEQ 1752
Cdd:COG3096 921 QLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENSDLNEKLRARLEQAEEAR 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1753 SNmelLNDRFRKTTMQVDTLNTELAGERSAAQkseNARQQLerqnKDLKSKLQELEGSVKSkfkasiaaleakilqleeq 1832
Cdd:COG3096 1001 RE---AREQLRQAQAQYSQYNQVLASLKSSRD---AKQQTL----QELEQELEELGVQADA------------------- 1051
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1833 leqEAKERAAANKivrrtekklkevfmqvederrhaDQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDD 1912
Cdd:COG3096 1052 ---EAEERARIRR-----------------------DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQ 1105
|
970 980 990
....*....|....*....|....*....|....
gi 528481573 1913 ATEASEG----------LSREvNTLKNRLRRGGP 1936
Cdd:COG3096 1106 EREQVVQakagwcavlrLARD-NDVERRLHRREL 1138
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1040-1824 |
3.78e-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: 68.71 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1040 VDLEERLKKEEKTRQELEKAKR-KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARgdeevaqknnalkqlre 1118
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQ----------------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1119 lqaQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhesqIQ 1198
Cdd:pfam12128 331 ---HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAK----IR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1199 EMRQRHGTALEEISEQLEQAKRvkgnleknkQTLESDNKELTNEVKSLQQAKSEsehkrkkleAQLQEVMARFSEGEKVK 1278
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELR---------EQLEAGKLEFNEEEYRLKSRLGE---------LKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1279 GELAD-RTHKIQTELdnvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlleqqee 1357
Cdd:pfam12128 466 LENFDeRIERAREEQ-------EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ---------- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1358 eeesrknLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLektknRLQQelddlmv 1437
Cdd:pfam12128 529 -------LFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKL-----DLKR------- 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1438 dLDHQRQIVSNlekkqkkfDQMLAEEKTISARYAEERDRAEAEarekdTKALSMARALDEALEAKEEFERlnkqlraemE 1517
Cdd:pfam12128 590 -IDVPEWAASE--------EELRERLDKAEEALQSAREKQAAA-----EEQLVQANGELEKASREETFAR---------T 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1518 DLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEledELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRAL 1597
Cdd:pfam12128 647 ALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE---RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1598 VKQVREMEAELEDERKQRALAVAAKkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIfTQ 1677
Cdd:pfam12128 724 EGALDAQLALLKAAIAARRSGAKAE------LKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV-LR 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1678 SKENEKKLKSLEAEILQLQedlasSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1757
Cdd:pfam12128 797 YFDWYQETWLQRRPRLATQ-----LSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSK 871
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1758 LNdrfrktTMQVDTLNTELAGERSaaqksenarqQLERQNKDLKSKLQELEGSVKSK---FKASIAALEA 1824
Cdd:pfam12128 872 LA------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 |
3.92e-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: 59.37 E-value: 3.92e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 528481573 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, ... |
1002-1220 |
4.91e-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: 66.71 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1002 KEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1081
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1082 DELKIQLAKKEEELQAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDT 1161
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLD---AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1162 LDTTAAQQELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRHGTALEEISEQLEQAKR 1220
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1041-1282 |
8.74e-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: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1041 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvlargdeevaqknnALKQLRELQ 1120
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--------------LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1121 AQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNhESQIQEM 1200
Cdd:COG4942 97 AELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1201 RQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG--EKVK 1278
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgfAALK 252
|
....
gi 528481573 1279 GELA 1282
Cdd:COG4942 253 GKLP 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1071-1292 |
9.38e-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: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1071 QDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1150
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1151 LEALKTELEDTLDTTAAQ--QELRSKREQEVAELKKAID-DETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEK 1227
Cdd:COG4942 92 IAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1228 NKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTEL 1292
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
856-1273 |
1.26e-10 |
|
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: 66.67 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 856 EMQAKDEELikvKERQVKVENELVEMERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLVAKKQELEEILHDLESRVE 935
Cdd:pfam05483 385 ELQKKSSEL---EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE-KIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 936 EEEERNQSLQNEKKKMqshiqdleeqldeeeaarqKLQLEKvtaeAKIKKMEedillLEDQNSKFLKEKKLLEDRVGEMT 1015
Cdd:pfam05483 461 AIKTSEEHYLKEVEDL-------------------KTELEK----EKLKNIE-----LTAHCDKLLLENKELTQEASDMT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1016 SQLAEEEEKAKNlgkVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL 1095
Cdd:pfam05483 513 LELKKHQEDIIN---CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1096 QAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1175
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1176 EQ--------------EVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKN----KQTLESDNK 1237
Cdd:pfam05483 670 EEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEqssaKAALEIELS 749
|
410 420 430
....*....|....*....|....*....|....*.
gi 528481573 1238 ELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1273
Cdd:pfam05483 750 NIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1044-1715 |
1.27e-10 |
|
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: 66.67 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1044 ERLKK-EEKTRQELEKAKRKLDAETTDLQDQ---IAELQAQIDELKIQLakkEEELQAvlargDEEVAQKNNALKQ---- 1115
Cdd:pfam05483 88 EKIKKwKVSIEAELKQKENKLQENRKIIEAQrkaIQELQFENEKVSLKL---EEEIQE-----NKDLIKENNATRHlcnl 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1116 LRELQAQLAELQEDLESEkaaRNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKREQE---VAELKKAIDDETR 1191
Cdd:pfam05483 160 LKETCARSAEKTKKYEYE---REETRQVYMDLNNNIEKMILAFEElRVQAENARLEMHFKLKEDhekIQHLEEEYKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1192 NHESQI---------QEMRQRHGT-ALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLE 1261
Cdd:pfam05483 237 DKEKQVsllliqiteKENKMKDLTfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1262 AQLQ---EVMARFSEGEKVKGELADRTHK----IQTELDNVSCLLED---AEKKGIKLTKD-VSSLESQLQDTQELLQEE 1330
Cdd:pfam05483 317 EDLQiatKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEEllrTEQQRLEKNEDqLKIITMELQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1331 TRQKLNLSSRIrqleEEKNNLLEQQEEEEESRKNLEKQLATLQAQ------LVETKKK----LEDDVGALEGLEEVKRKL 1400
Cdd:pfam05483 397 TKFKNNKEVEL----EELKKILAEDEKLLDEKKQFEKIAEELKGKeqelifLLQAREKeihdLEIQLTAIKTSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1401 QKDMEVTSQKLEEKAIAF----DKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKfdqMLAEEKTISARYAEERDR 1476
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELtahcDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---MLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1477 AEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELED 1556
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1557 ELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQI 1636
Cdd:pfam05483 630 QLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALM 709
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1637 EAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRdeiftqskenEKKLKSLEAEILQLQEDLASSERARRHAEQERDE 1715
Cdd:pfam05483 710 EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL----------EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
903-1634 |
1.29e-10 |
|
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: 66.67 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 903 TELFAEAEEMR-------ARLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQshiqdleeqldeeeaarqkLQLE 975
Cdd:pfam05483 81 SKLYKEAEKIKkwkvsieAELKQKENKLQENRKIIEAQRKAI----QELQFENEKVS-------------------LKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 976 KVTAEAKikkmeeDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNL-GKVKNKQEMMMVDLEERLKKEEKTRQ 1054
Cdd:pfam05483 138 EEIQENK------DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVyMDLNNNIEKMILAFEELRVQAENARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1055 E----LEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQAQlaELQEDL 1130
Cdd:pfam05483 212 EmhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKD-LTFLLEESRDKANQLEEKTKLQDE--NLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1131 ESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAiddetRNHESQIQEMRQRHGTALEE 1210
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1211 ISEQLEQakrvkgNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEaQLQEVMARFSEGEKVKGELADRTHKIQT 1290
Cdd:pfam05483 364 LLRTEQQ------RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1291 ELDNVSCLLEDAEKK----GIKLTKDVSSLESQLQDTQELLQEETRQKLnlssRIRQLEEEKNNLLEQQEEEEESRKNLE 1366
Cdd:pfam05483 437 KEQELIFLLQAREKEihdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKL----KNIELTAHCDKLLLENKELTQEASDMT 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1367 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTS----QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQ 1442
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVReefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1443 RQIVSNLEK----KQKKFDQMLAEEKTIsaryaeeRDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1518
Cdd:pfam05483 593 ENKCNNLKKqienKNKNIEELHQENKAL-------KKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIED 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1519 LISSKDDVgknVHELEKSKRTLEQQVeemrtqleELEDELQATEDAKLRLEVN-MQAMKAQFDRDLQARDEQ-----NEE 1592
Cdd:pfam05483 666 KKISEEKL---LEEVEKAKAIADEAV--------KLQKEIDKRCQHKIAEMVAlMEKHKHQYDKIIEERDSElglykNKE 734
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 528481573 1593 KKRALVKQVREME-----AELEDERKQRALAVAAKKKLEMDLKDVEA 1634
Cdd:pfam05483 735 QEQSSAKAALEIElsnikAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
922-1276 |
1.34e-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: 66.58 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 922 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1001
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1002 KEKKLLEDRVgemtsqlaeeeekaKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1081
Cdd:TIGR04523 419 QEKELLEKEI--------------ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1082 DELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLESEKaarNKAEKLKRDLSEELEALKTELedt 1161
Cdd:TIGR04523 485 EQKQKELKSKEKELKKL----NEEKKELEEKVKDLTKKISSLKEKIEKLESEK---KEKESKISDLEDELNKDDFEL--- 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1162 ldTTAAQQELRSKREQEVAELKKAIDDETRNHEsQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTN 1241
Cdd:TIGR04523 555 --KKENLEKEIDEKNKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
330 340 350
....*....|....*....|....*....|....*
gi 528481573 1242 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEK 1276
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
847-1435 |
1.60e-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: 66.79 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 847 LLQVTRQEE--EMQAKDEELIKVKERQVK-----VENELVEMERKHQQLLEEKNILAEQ----LQAETELFAEAEEMRAR 915
Cdd:pfam12128 272 TLIASRQEErqETSAELNQLLRTLDDQWKekrdeLNGELSAADAAVAKDRSELEALEDQhgafLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 916 LVAKKQELEEILHDLESRVEEEEERNQSLqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDI-LLLE 994
Cdd:pfam12128 352 WQSELENLEERLKALTGKHQDVTAKYNRR--RSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELrEQLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 995 DQNSKFLKEKKLLEDRVGEMTSQLAE---EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1071
Cdd:pfam12128 430 AGKLEFNEEEYRLKSRLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1072 D---QIAELQAQIDELKIQLAKK---------------EEELQAVLARG------------DEEVAQKNNA------LKQ 1115
Cdd:pfam12128 510 QasrRLEERQSALDELELQLFPQagtllhflrkeapdwEQSIGKVISPEllhrtdldpevwDGSVGGELNLygvkldLKR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1116 L---------RELQAQLAELQEDLESEKA-----------ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKR 1175
Cdd:pfam12128 590 IdvpewaaseEELRERLDKAEEALQSAREkqaaaeeqlvqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1176 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKgnlEKNKQTLESDnkeLTNEVKSLQQAKSESEH 1255
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK---QAYWQVVEGA---LDAQLALLKAAIAARRS 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1256 KRKKLEAQLQEVMARFSEGEKVKGelaDRTHKIQTELDNVSCLLEDAEKKGikltKDVSSLESQLQDTqeLLQEETRQKL 1335
Cdd:pfam12128 744 GAKAELKALETWYKRDLASLGVDP---DVIAKLKREIRTLERKIERIAVRR----QEVLRYFDWYQET--WLQRRPRLAT 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1336 NLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVK-----RKLQKDMEVTSQK 1410
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERLAQ 894
|
650 660
....*....|....*....|....*
gi 528481573 1411 LEEkaiAFDKLEKTKNRLQQELDDL 1435
Cdd:pfam12128 895 LED---LKLKRDYLSESVKKYVEHF 916
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
772-1294 |
1.76e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 772 FFRTGVLahleEERDL--KITDIIIYFQSVCRgylARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWW 838
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 839 RLFTKVKpLLQ--VTRQEEEMQAKDEELIKVKERQVKVENELVEMerkHQQLLEEKNILAEQLQAETElfaEAEEMRARL 916
Cdd:COG4913 285 FAQRRLE-LLEaeLEELRAELARLEAELERLEARLDALREELDEL---EAQIRGNGGDRLEQLEREIE---RLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 917 VAKKQELEEILHDLESRVEEEEernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 996
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 997 NS----KFLKEKKLLEDRVGEMTS---------QLAEEEEK-------------------AKNLGKV-----KNKQEMMM 1039
Cdd:COG4913 435 KSnipaRLLALRDALAEALGLDEAelpfvgeliEVRPEEERwrgaiervlggfaltllvpPEHYAAAlrwvnRLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1040 VDLEERLKKEEKTRQELEKAK--RKLDAETTDLQDQI-AELQAQIDELKIQlakKEEELQ--------AVLARGDEEVAQ 1108
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLeAELGRRFDYVCVD---SPEELRrhpraitrAGQVKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1109 KN-------------NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELE---DTLDTTAAQQELR 1172
Cdd:COG4913 592 KDdrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1173 SKrEQEVAELKKAiDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAksE 1252
Cdd:COG4913 672 EL-EAELERLDAS-SDDLAALEEQLEELEAE----LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL--A 743
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 528481573 1253 SEHKRKKLEAQLQEVMARFSEGEKVKgELADRTHKIQTELDN 1294
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRE-NLEERIDALRARLNR 784
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1494-1728 |
2.44e-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: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1494 ALDEALEAKEEFERLNKQL---RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1570
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIaelEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1571 NMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQL 1650
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1651 RKLQAQMKDYQRELEEARTSRDEIFTQSkenEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1728
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1537-1743 |
2.55e-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: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1537 KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnMQAMKAQFDR--DLQARDEQNEEKKRALVKQVREMEAELEDERKQ 1614
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1615 RALAvaAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQ-AQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL 1693
Cdd:COG4913 299 ELRA--ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 528481573 1694 QLQEDLAS-SERARRHAE---QERDELADEISNSASGKAALLDEKRRLEARIAQ 1743
Cdd:COG4913 377 ASAEEFAAlRAEAAALLEaleEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1022-1422 |
2.97e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1022 EEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQA--VL 1099
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1100 ARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEV 1179
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1180 AELKKAIDDETRNHESQIQEMRQRHgtALEEISEQLEQAKR-------------------------------VKGNLEKN 1228
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLllliaaallallglggsllsliltiagvlflVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1229 KQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIK 1308
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1309 LTKDVSSLESQLQDTQELLQ--EETRQKLNLSSRIRQLEE--EKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE 1384
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 528481573 1385 DDVGALEGLEEVKRKLQKDMEVtSQKLEEKAIAFDKLE 1422
Cdd:COG4717 450 ELREELAELEAELEQLEEDGEL-AELLQELEELKAELR 486
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1243-1713 |
5.21e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1243 VKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ- 1321
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1322 -DTQELLQEETRQKLNLSSRIRQLEEEknnlleqqeeeEESRKNLEKQLATLQAQLVETKKKLEddvgalEGLEEVKRKL 1400
Cdd:COG4717 128 lPLYQELEALEAELAELPERLEELEER-----------LEELRELEEELEELEAELAELQEELE------ELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1401 QKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH--QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAE 1478
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1479 AEAREKDTKALSMA----------RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMR 1548
Cdd:COG4717 271 LILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1549 TQLEELEDELQ--ATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVREMEAELEDERK--QRALAVAAKKK 1624
Cdd:COG4717 351 ELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGelEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1625 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY--QRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLASS 1702
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEEL-------KAELRELAEEWAALKLALELL 502
|
490
....*....|.
gi 528481573 1703 ERARRHAEQER 1713
Cdd:COG4717 503 EEAREEYREER 513
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
969-1740 |
5.48e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 969 RQKLQLEKVTAEAKIKKMEEDILLLEDQnskfLKEKKLLedrVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKk 1048
Cdd:PRK04863 336 HLNLVQTALRQQEKIERYQADLEELEER----LEEQNEV---VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALD- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1049 EEKTR--------QELEKAKRKLDA---ETTDLQDQIAELQAQIDEL---------KIQLAKK-----EEELQAVLARGD 1103
Cdd:PRK04863 408 VQQTRaiqyqqavQALERAKQLCGLpdlTADNAEDWLEEFQAKEQEAteellsleqKLSVAQAahsqfEQAYQLVRKIAG 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1104 E---EVAQKN--NALKQLRE----------LQAQLAELQEDLESEKAAR------NKAEKLKRDLSEELEALKTELEDTL 1162
Cdd:PRK04863 488 EvsrSEAWDVarELLRRLREqrhlaeqlqqLRMRLSELEQRLRQQQRAErllaefCKRLGKNLDDEDELEQLQEELEARL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1163 DTTAAQQElrskreqEVAELKKAIDDETRNHESQIQEMRQRhGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNE 1242
Cdd:PRK04863 568 ESLSESVS-------EARERRMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLER 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1243 VKSLQQAKSESEHKRKKLEAQLQEVMAR-FSEGEKVKGeLADRTHKIQ-TEL-DNVSclLEDA----------------- 1302
Cdd:PRK04863 640 ERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNA-LAERFGGVLlSEIyDDVS--LEDApyfsalygparhaivvp 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1303 EKKGIK---------------LTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNlleqqeeeeeSRKNLEK 1367
Cdd:PRK04863 717 DLSDAAeqlagledcpedlylIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLF----------GRAAREK 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1368 QLATLQAQ---LVETKKKLEDDVgalegleevkRKLQKDMEVTSQKL-EEKAIAFD-----KLEKTKNRLQQ---ELDDL 1435
Cdd:PRK04863 787 RIEQLRAEreeLAERYATLSFDV----------QKLQRLHQAFSRFIgSHLAVAFEadpeaELRQLNRRRVElerALADH 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1436 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKTIsaryAEER--DRAEaEAREKDTKALSMARALDEALEAKEEFERLNKQLR 1513
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALNRLLPRLNLL----ADETlaDRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ 931
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1514 AEMEDLisskDDVGKNVHELEKSKRTLEQQVEEMrTQLEELEDELqATEDAklrleVNMQAMKAQFDRDLQARDEQNEEK 1593
Cdd:PRK04863 932 SDPEQF----EQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHF-SYEDA-----AEMLAKNSDLNEKLRQRLEQAEQE 1000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1594 KRALVKQVREMEAELEDerkqralavaaKKKLEMDLKdveAQIEAANKARDEAIKQLRKLQAQmkdYQRELEE-ARTSRD 1672
Cdd:PRK04863 1001 RTRAREQLRQAQAQLAQ-----------YNQVLASLK---SSYDAKRQMLQELKQELQDLGVP---ADSGAEErARARRD 1063
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528481573 1673 EIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL------DEKRRLEAR 1740
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLrlvkdnGVERRLHRR 1137
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1616-1850 |
6.24e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1616 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQL 1695
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1696 QEDLasserarrhaEQERDELADEIS----NSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLnDRFRKTTMQVDT 1771
Cdd:COG4942 96 RAEL----------EAQKEELAELLRalyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1772 LNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1850
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
984-1492 |
6.38e-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: 64.46 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 984 KKMEEDILLLEDQ----NSKFLKEKKLLEDRVGEMTSQLAEEE--EKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELE 1057
Cdd:pfam10174 137 KTLEEMELRIETQkqtlGARDESIKKLLEMLQSKGLPKKSGEEdwERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELH 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1058 KAKRKLD--AETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQlaelqedlesEKA 1135
Cdd:pfam10174 217 RRNQLQPdpAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSH----------SKF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1136 ARNKAEKLKRDLSE---ELEALKTELE-------------DTLDTTAAQQELRSKREQ-EVAELKKAIDDETR---NHES 1195
Cdd:pfam10174 287 MKNKIDQLKQELSKkesELLALQTKLEtltnqnsdckqhiEVLKESLTAKEQRAAILQtEVDALRLRLEEKESflnKKTK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1196 QIQEMRQRHGTALEEIS------------------------EQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKS 1251
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRdlkdmldvkerkinvlqkkienlqEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALS 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1252 ESE-------HKRKKLEAQLQEVMARFSEGEKV--------KGELADRTHKIQTELDNVSCLLEDAEKKGIKL------- 1309
Cdd:pfam10174 447 EKEriierlkEQREREDRERLEELESLKKENKDlkekvsalQPELTEKESSLIDLKEHASSLASSGLKKDSKLksleiav 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1310 ---TKDVSSLESQLQDTQElLQEETRQKLNLSSRIRQLEEEknnLLEQQEEEEESRKNLEKQLATLQAqlVETKKKLEDD 1386
Cdd:pfam10174 527 eqkKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE---VARYKEESGKAQAEVERLLGILRE--VENEKNDKDK 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1387 -VGALEGLEEVKRKLQ--KDMEVTSQKLEEKAIAFDKLEK--------TKNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1455
Cdd:pfam10174 601 kIAELESLTLRQMKEQnkKVANIKHGQQEMKKKGAQLLEEarrrednlADNSQQLQLEELMGALEKTRQELDATKARLSS 680
|
570 580 590
....*....|....*....|....*....|....*..
gi 528481573 1456 FDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1492
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1361-1624 |
9.63e-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: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1361 SRKNLEKQLATLQAQLVETKKKLEDdvgalegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1440
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1441 HQRQivsNLEKKQKKFDQMLAEektisaryaeerdrAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLI 1520
Cdd:COG4942 94 ELRA---ELEAQKEELAELLRA--------------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1521 SSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqfdrdLQARDEQNEEKKRALVKQ 1600
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 528481573 1601 VREMEAELEDERKQRALAVAAKKK 1624
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1287-1931 |
1.07e-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: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1287 KIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1366
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1367 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIV 1446
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1447 SNLEKKQKKFDQMLAEektisaryaeerdraeAEAREKDTKALSmaralDEALEAKEEFERLNKQLRAEMEDLISSKDDV 1526
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQ----------------ISELKKQNNQLK-----DNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1527 GKNVHELEKSkrtlEQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA 1606
Cdd:TIGR04523 263 NKIKKQLSEK----QKELEQNNKKIKELEKQLN---QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1607 ELEDERKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLK 1686
Cdd:TIGR04523 336 IISQLNEQIS-------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1687 SLEAEILQLQEDLASSERARRHAEQERDELADEISNsasgkaaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTT 1766
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-------LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1767 MQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKsKFKASIAALEAKILQleeqleqeaKERAAANKI 1846
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISD---------LEDELNKDD 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1847 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNT 1926
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
....*
gi 528481573 1927 LKNRL 1931
Cdd:TIGR04523 632 IIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1488-1729 |
1.87e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1488 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR 1567
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1568 LEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAI 1647
Cdd:COG4942 88 LEKEIAELRAE----LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1648 KQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGK 1727
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 528481573 1728 AA 1729
Cdd:COG4942 244 PA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1477-1702 |
1.87e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1477 AEAEAREKDTKALSMARA-LDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELE 1555
Cdd:COG4942 17 AQADAAAEAEAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1556 DELQATEDAKLRLEVNMQAMK--------------AQFDRDLQARDEQNeekkRALVKQVREMEAELEDERKQRALAVAA 1621
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLA----PARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1622 KKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqskenEKKLKSLEAEILQLQEDLAS 1701
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPA 245
|
.
gi 528481573 1702 S 1702
Cdd:COG4942 246 A 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
848-1222 |
2.42e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 848 LQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQEL---- 923
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 924 EEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKE 1003
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1004 KK------------LLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQ 1071
Cdd:COG4717 271 LIltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1072 DQIAELQAQIDELKIQLAKKEEE--LQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKlkrdlSE 1149
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----AL 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481573 1150 ELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHEsqIQEMRQRHGTALEEISEQLEQAKRVK 1222
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALK 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
897-1285 |
2.46e-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: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 897 EQLQAETELFAEAEEMRA-------RLVAKKQELEEILHDLESRVEEEEERNQSLQNEK--KKMQSHIQDLEEQLDEEEA 967
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 968 ARQKLQLEKVTAEAKIKKmeEDILLLEDQNSKFLKEKKL----LEDRVGEMtsQLAEEEEKAKNLGKVKNKQEMMMvdle 1043
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKREL--ERIRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1044 ERLKKEEKTRQELEKAkRKLDAETTDLQDQIAELQAQIDELKiqlAKKEEELQAVLARGDEEVAQKNNALKQLR-ELQAQ 1122
Cdd:pfam17380 386 ERQQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIR---AEQEEARQREVRRLEEERAREMERVRLEEqERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1123 LAELQEDLESEKAARNKAEKLKRDLSEelealkteledtldttaAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQ 1202
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKR-----------------AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1203 RHGTALEEiseqleqAKRVKGNLEKNKQtlesdnKELtNEVKSLQQAKSESEHKRKKLEA--QLQEVMARFSEGEKVKGE 1280
Cdd:pfam17380 525 RQKAIYEE-------ERRREAEEERRKQ------QEM-EERRRIQEQMRKATEERSRLEAmeREREMMRQIVESEKARAE 590
|
....*
gi 528481573 1281 LADRT 1285
Cdd:pfam17380 591 YEATT 595
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1076-1909 |
2.90e-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: 62.37 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1076 ELQAQIDEL--KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1153
Cdd:TIGR00606 170 ALKQKFDEIfsATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1154 LKT---ELEDTL-------DTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKG 1223
Cdd:TIGR00606 250 LKNrlkEIEHNLskimkldNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1224 NLEKNKQTLESDNKELTNEVKSLQ-QAKSESEHKRKKlEAQLQEVMARFSEGEKVKGELADRthkiqtELDNVSCL-LED 1301
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLATRLELDGFERGPFSER------QIKNFHTLvIER 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1302 AEKKGIKLTKDVSSLESQLQDTQELLqEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrknLEKQlatlQAQLVETKK 1381
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQA-DEIRDEKKGLGRTIELKKEI----------------LEKK----QEELKFVIK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1382 KLEDDVGALEGLEEVKRKLQKDMEVTSqKLEEKAIAFDKLEKTKNRLQQELDdlmvdldhqrqivsnLEKKQKKFDQMLA 1461
Cdd:TIGR00606 462 ELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQNEKAD---------------LDRKLRKLDQEME 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1462 EEKtisaRYAEERDRAEAEAREKDTKalsmaraldealeakeeFERLNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLE 1541
Cdd:TIGR00606 526 QLN----HHTTTRTQMEMLTKDKMDK-----------------DEQIRKIKSRHSDELTSLLGYF-PNKKQLEDWLHSKS 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1542 QQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFDRDLQARDEQneekkralvkqvremEAELEDerkqRALAVAA 1621
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ---------------LSSYED----KLFDVCG 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1622 KKKLEMDLKDVEAQIEAANKardeaikQLRKLQAQMKDYQRELEEARTSR-------DEIFTQSKENEKKLKSLEAEILQ 1694
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRL 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1695 LQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMElLNDRFRKTTMQVDTLNT 1774
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAK 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1775 ELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVK----SKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRT 1850
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1851 EKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRE 1909
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1070-1814 |
2.90e-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: 62.43 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1070 LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLREL-QAQLAELQE-DLESEKAARNKAEKLK--R 1145
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEEIQenK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1146 DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqemrqrhgTALEEISEQLEQAK-----R 1220
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlemhfK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1221 VKGNLEKNKQTLESDNKELTN---EVKSLQQAKSESEHKRKKLEAQLQEVMARFSE-GEKVK------GELADRTHKIQT 1290
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDkekQVSLLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKlqdenlKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1291 ELDNVSCLLEDAEKKGIKLTKDV---SSLESQLQDTQELLQEET-RQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE 1366
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLqiaTKTICQLTEEKEAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1367 KQLATLQAQLVETKKKLEDdVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMvdldhqrqiv 1446
Cdd:pfam05483 377 DQLKIITMELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLL---------- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1447 SNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALD----EALEAKEEFERLNKQLRAEMEDLISS 1522
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENKELTQEASDMTLELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1523 KddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDEL-QATEDAKLRLEVNMQAMKAQFDRDLQARDEQN--EEKKRALVK 1599
Cdd:pfam05483 526 K----KQEERMLKQIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilENKCNNLKK 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1600 QVREMEAELEDERKQRAlavAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFtqsk 1679
Cdd:pfam05483 602 QIENKNKNIEELHQENK---ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL---- 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1680 ENEKKLKSLEAEILQLQEdlasserarrhaeqerdELADEISNSASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLN 1759
Cdd:pfam05483 675 EEVEKAKAIADEAVKLQK-----------------EIDKRCQHKIAEMVALMEKHKHQYDKIIEER------DSELGLYK 731
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1760 DRFRKTTMQVDTLNTELAGERsAAQKSENARQQLERQNKD-LKSKLQELEGSVKSK 1814
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIK-AELLSLKKQLEIEKEEKEkLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
942-1168 |
3.65e-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: 60.93 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 942 QSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEE 1021
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1022 EEKaknLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLAR 1101
Cdd:COG4942 103 KEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1102 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ 1168
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1042-1518 |
4.52e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1042 LEERLKKEektRQELEKAKRKLDaetTDLQDQIAELQAQIDELKIQLAKKEEELQAvLARGDEEVAQKNNALKQLRELQA 1121
Cdd:COG4717 47 LLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1122 QLAELQEDLEsekaARNKAEKLKRDLSEELEALKtELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR 1201
Cdd:COG4717 120 KLEKLLQLLP----LYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1202 QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAksesehKRKKLEAQLQEVMARFSEGEKVKGEL 1281
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE------ERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1282 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEES 1361
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1362 RKNLEKQLATLQAQLvetkkkleddvgALEGLEEVKRKLQKDMEVTS-QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLD 1440
Cdd:COG4717 349 LQELLREAEELEEEL------------QLEELEQEIAALLAEAGVEDeEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1441 HQRQIVSNLEKKQKKfdQMLAEEKTISARYAEERDRAEAEAREKDTKaLSMARALDEALEAKEEFERLNKQLRAEMED 1518
Cdd:COG4717 417 ELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAE-LEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1402-1797 |
8.63e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1402 KDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQmLAEEKTISARYAEERDRAEA-E 1480
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1481 AREKDTKAL--SMARALDEALEAKEEFERLNKQL----RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEEL 1554
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1555 EDELQATEDAK-----------------------------------LRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVK 1599
Cdd:COG4717 233 ENELEAAALEErlkearlllliaaallallglggsllsliltiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1600 QVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRkLQAQMKDYQRELEEARTSRDEIFTQSK 1679
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1680 ENEKKLKSLEAEILQLQEDLASSERARRH--AEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1757
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 528481573 1758 --LNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQN 1797
Cdd:COG4717 472 aeLLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
887-1268 |
9.73e-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: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 887 QLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEE 966
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 967 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERL 1046
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1047 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAvlargdeevaqknnALKQLRELQAQLAel 1126
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEA--------------LLEELRSLQERLN-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1127 qedlesekAARNKAEKLKRDLSE---------------ELEALKTELEdTLDTTAAQQELRSKREQEVAELKKAIDDETR 1191
Cdd:pfam07888 248 --------ASERKVEGLGEELSSmaaqrdrtqaelhqaRLQAAQLTLQ-LADASLALREGRARWAQERETLQQSAEADKD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1192 NHESQIQEMRQRHGTALEEISEQleQAKRVKGNLEK--NKQTLESDNKELTNEVKSLQQAKSESEHkrkkLEAQLQEVM 1268
Cdd:pfam07888 319 RIEKLSAELQRLEERLQEERMER--EKLEVELGREKdcNRVQLSESRRELQELKASLRVAQKEKEQ----LQAEKQELL 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1071-1296 |
1.32e-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: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1071 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLKRDLSEE 1150
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1151 LEALK---------------TELEDTLDTTAAQQELRSKREQEVAELKKAIdDETRNHESQIQEMRQRHGTALEEISEQL 1215
Cdd:COG3883 92 ARALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1216 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1295
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
.
gi 528481573 1296 S 1296
Cdd:COG3883 251 A 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
969-1275 |
1.34e-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: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 969 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDR--VGEMTSQLAEEEEKAKNLgkvknKQEMMMVD-LEER 1045
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidVASAEREIAELEAELERL-----DASSDDLAaLEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1046 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1125
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1126 LQEDLESEKA-ARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQE-----VAELKKAIDDETRNHESQIQ- 1198
Cdd:COG4913 774 RIDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFVADLLs 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1199 EMRQrhgtALEEISEQLEQAKRVKGNLEKNKQT---LESDNKELTnEVKSLQQ--------AKSESEHKRKKLEAQLQEV 1267
Cdd:COG4913 854 KLRR----AIREIKERIDPLNDSLKRIPFGPGRylrLEARPRPDP-EVREFRQelravtsgASLFDEELSEARFAALKRL 928
|
....*...
gi 528481573 1268 MARFSEGE 1275
Cdd:COG4913 929 IERLRSEE 936
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1050-1272 |
1.37e-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: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1050 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQ--LAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1127
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1128 EDLES--EKAARNKAEKLKRDLSEELEALKTELEDTLDT-TAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRH 1204
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQ-IAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1205 GTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFS 1272
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR----RLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
884-1265 |
1.55e-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: 59.75 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 884 KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEIlhdlESRVEEEEERNQSLQNEKKKMqshiqdleeqld 963
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA----EKARQAEMDRQAAIYAEQERM------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 964 eeeAARQKLQLEKVTAEAKIKKMEEdillledqnskflkekklledrvgemtsqlAEEEEKAKNLGKVKNKQEMMMvdle 1043
Cdd:pfam17380 343 ---AMERERELERIRQEERKRELER------------------------------IRQEEIAMEISRMRELERLQM---- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1044 ERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDELK--------IQLAKKEEELQAVLARGDEEVAQKNNALKQ 1115
Cdd:pfam17380 386 ERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVER 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1116 LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEElealktELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHES 1195
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1196 QIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQtlesdNKELTNEVKslqqaksESEHKRKKLEAQLQ 1265
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----EREMMRQIV-------ESEKARAEYEATTP 596
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1541-1753 |
1.80e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1541 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVA 1620
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1621 AKKKLEMDLKDVEAQIEAANKArdEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLA 1700
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528481573 1701 SSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQS 1753
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1463-1933 |
2.33e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1463 EKTISARYAEERDRAEAEArekdtkALSMARALDEALEAKEEFERLNkqlraemeDLISSKDDVGKNVHELEKSKRTLEQ 1542
Cdd:PRK02224 169 ERASDARLGVERVLSDQRG------SLDQLKAQIEEKEEKDLHERLN--------GLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1543 QVEEMRTQLEELEDELQATEDAKLRLEvnmqamkaqfdrDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1622
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIE------------DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1623 KKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlqedLASS 1702
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE-------LEEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1703 ERARRHAEQERDELADEIsnsasgkaalldekRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELageRSA 1782
Cdd:PRK02224 376 REAVEDRREEIEELEEEI--------------EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL---RTA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1783 AQKSENARQQLERQNkdLKSKLQELEGS----VKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVrRTEKKLKEVF 1858
Cdd:PRK02224 439 RERVEEAEALLEAGK--CPECGQPVEGSphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLE 515
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1859 MQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1933
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1224-1823 |
2.91e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1224 NLEKNKQTLESDNKELTNEVKSLQQAK---SESEHKRKKLEAQLQEVMarfsegekvkgelaDRTHKIQTELDNVSCLLE 1300
Cdd:PRK01156 184 NIDYLEEKLKSSNLELENIKKQIADDEkshSITLKEIERLSIEYNNAM--------------DDYNNLKSALNELSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1301 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIrqleeeknnlleqqeeeeESRKNLEKQLATLQAQLVETK 1380
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPV------------------YKNRNYINDYFKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1381 KKLEDDVGALEGLEEVKRKLQKdmevtsqkLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQML 1460
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV--------LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1461 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEAleaKEEFERLNKQLRAemedLISSKDDVGKNVHEL------- 1533
Cdd:PRK01156 384 KNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI---SSKVSSLNQRIRA----LRENLDELSRNMEMLngqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1534 --------EKSKRTLEQQVEE---MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKkRALVKQVR 1602
Cdd:PRK01156 457 vcgttlgeEKSNHIINHYNEKksrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-RADLEDIK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1603 EMEAELEDERKQRALAVAAKKklEMDLKDVEAQ---------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1667
Cdd:PRK01156 536 IKINELKDKHDKYEEIKNRYK--SLKLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1668 RTSRDEIFtqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELAdeisnsasGKAALLDEKRRLEARIAQleee 1747
Cdd:PRK01156 614 KSYIDKSI---REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSIIPDLKEITSRIND---- 678
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1748 leeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEgsvksKFKASIAALE 1823
Cdd:PRK01156 679 ----------IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK-----KIKKAIGDLK 739
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
849-1269 |
2.97e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 849 QVTRQEEEMQAKDEELIKVKERQVKVENELVEME---RKHQQLLEEKNILAEQLQAETELFAEAEEMRaRLVAKKQELEE 925
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELReelEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 926 ILHDLESRVEEEEERNQSLQNEKKK----MQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFL 1001
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1002 KEKKLLEDR-----VGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1076
Cdd:COG4717 241 LEERLKEARlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1077 LQAQIDELKIQLAKKEEELQAVLARgdeevaqknnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKT 1156
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDR-----------IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1157 ELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1236
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
410 420 430
....*....|....*....|....*....|...
gi 528481573 1237 keltnevkSLQQAKSESEHKRKKLEAQLQEVMA 1269
Cdd:COG4717 470 --------ELAELLQELEELKAELRELAEEWAA 494
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
812-1412 |
3.70e-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: 58.90 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 812 KQQQLSALKVLQRNCAAYLKLRHWqwwRLFTKVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERK---HQQL 888
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 889 LEEKNILAEQLQAETELFAEAEEMRAR------------LVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQ 956
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 957 DLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKE------KKLLEDRVGEMTSQLAEEEEKAKNLGK 1030
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLKEEIEKSSKQRAMLAG 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1031 VKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKN 1110
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1111 NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRS---KREQEVAELKKAID 1187
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDverKIAQQAAKLQGSDL 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1188 DETRnheSQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEV 1267
Cdd:TIGR00606 821 DRTV---QQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1268 MARFSE--------------GEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQE--LLQEET 1331
Cdd:TIGR00606 898 QSLIREikdakeqdspletfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdyLKQKET 977
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1332 rqklNLSSRIRQLEEEKNNLLEQQEEEEESRKNLE---KQLATLQAQLveTKKKLEDDVGALEGLEEVKRKLQKDMEVTS 1408
Cdd:TIGR00606 978 ----ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNL--TLRKRENELKEVEEELKQHLKEMGQMQVLQ 1051
|
....
gi 528481573 1409 QKLE 1412
Cdd:TIGR00606 1052 MKQE 1055
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1020-1196 |
3.79e-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: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1020 EEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVL 1099
Cdd:COG3883 17 QIQAKQKELSELQAELE----AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1100 A-----------------------------RGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1150
Cdd:COG3883 93 RalyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 528481573 1151 LEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQ 1196
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1574-1741 |
3.85e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.09 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1574 AMKAQFDR--DLQARD---EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIK 1648
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1649 QLRKLQA--QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSAsg 1726
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL-- 158
|
170
....*....|....*
gi 528481573 1727 kAALLDEKRRLEARI 1741
Cdd:COG1579 159 -EELEAEREELAAKI 172
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
862-1817 |
4.05e-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: 58.91 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 862 EELIKVKERQVKVENELVEMERKHQQLLEEKniLAEQLQAETELFAEAEEMRARLVAK-KQELEEILHDLESRVEEEEER 940
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMETATVELH--LSNIENKKNELLDIIVEIKKHIHGEiNKDLNKILEDFKNKEKELSNK 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 941 NQSLQNEKKKM---QSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQ 1017
Cdd:TIGR01612 771 INDYAKEKDELnkyKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1018 LAEEEEKAKNlgKVKNKQEMMmVDLEERLKKEEKTRQeLEKAKRKLDaettDLQDQIAELQAQIDE--LKIQLAKKEEEL 1095
Cdd:TIGR01612 851 FINFENNCKE--KIDSEHEQF-AELTNKIKAEISDDK-LNDYEKKFN----DSKSLINEINKSIEEeyQNINTLKKVDEY 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1096 QAVLARGDEEVAQKNNALKQLRE-LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTlDTTAAQQEL--- 1171
Cdd:TIGR01612 923 IKICENTKESIEKFHNKQNILKEiLNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLN-DYEAKNNELiky 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1172 ------------RSKREQEVAELKKAIDD---ETRNHESQIQEMRQRHGTALEEISEQLEqaKRVKGNLEK-NKQTLESD 1235
Cdd:TIGR01612 1002 fndlkanlgknkENMLYHQFDEKEKATNDieqKIEDANKNIPNIEIAIHTSIYNIIDEIE--KEIGKNIELlNKEILEEA 1079
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1236 NKELTNEVKSLQQAK----------------SESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNvsclL 1299
Cdd:TIGR01612 1080 EINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQIND----L 1155
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1300 EDAEKKGIKlTKDVSSLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNNLLEQQEEEEESRKNLEKqlaTLQ 1373
Cdd:TIGR01612 1156 EDVADKAIS-NDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGK---LFL 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1374 AQLVETKKKLEDDVGALEG----LEEVKRKlqkdmevtSQKLEEKAIAFDKLEKTKNRLQQELDD----LMVDLDHQRQI 1445
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEAyiedLDEIKEK--------SPEIENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI 1300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1446 vSNLEKKQKKFDQMLAEEKTISARYAE-ERDRAEAEAREKDT--------------KALSMARALDEALEAKEEFERLNK 1510
Cdd:TIGR01612 1301 -SDIREKSLKIIEDFSEESDINDIKKElQKNLLDAQKHNSDInlylneianiynilKLNKIKKIIDEVKEYTKEIEENNK 1379
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1511 QLRAEM---EDLISS-KDDVgknvhELEKSKRTLEQQVEEmrTQLEELEDELQATEDAKLRLEVNMqamkaqfDRDLQAR 1586
Cdd:TIGR01612 1380 NIKDELdksEKLIKKiKDDI-----NLEECKSKIESTLDD--KDIDECIKKIKELKNHILSEESNI-------DTYFKNA 1445
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1587 DEQNEEKKrALVKQVremeaELEDERKQRALAVA---AKKKLEMDLKDVEAQIEAANKARDEA---IKQLRKLQAQMKDY 1660
Cdd:TIGR01612 1446 DENNENVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQY 1519
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1661 QRELEE------ARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK 1734
Cdd:TIGR01612 1520 KKDVTEllnkysALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQ 1599
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1735 RRLEA------RIAQLEEELEEEQSNMELLNDRFrkTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELE 1808
Cdd:TIGR01612 1600 LSLENfenkflKISDIKKKINDCLKETESIEKKI--SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD 1677
|
....*....
gi 528481573 1809 gSVKSKFKA 1817
Cdd:TIGR01612 1678 -ELDSEIEK 1685
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1268 |
4.71e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 843 KVKPLLQVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRarlvaKKQE 922
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----KAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 923 leeilhdlesrveeeeernqslqnEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLK 1002
Cdd:PTZ00121 1631 ------------------------EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1003 EKKLLEdrvgemtsQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAElqaQID 1082
Cdd:PTZ00121 1687 EKKAAE--------ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD---EEE 1755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1083 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA---RNKAEKLKRDLSEELEAlkTELE 1159
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiieGGKEGNLVINDSKEMED--SAIK 1833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1160 DTLDTTAAQQElRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1239
Cdd:PTZ00121 1834 EVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDL----KEDDEEEIEEADEIEKIDKDDIEREIPNNNMA 1908
|
410 420
....*....|....*....|....*....
gi 528481573 1240 TNEVKSLQQAKSESEHKRKKLEAQLQEVM 1268
Cdd:PTZ00121 1909 GKNNDIIDDKLDKDEYIKRDAEETREEII 1937
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1549-1933 |
5.17e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1549 TQLEELEDELQATEDAKLRLevnmqamkaqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRAL--AVAAKKKLE 1626
Cdd:COG4717 71 KELKELEEELKEAEEKEEEY------------AELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1627 MDLKDVEAQIEAAnkarDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ-SKENEKKLKSLEAEILQLQEDLASSERA 1705
Cdd:COG4717 139 AELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1706 RRHAEQERDELADEISNSASGKAALLDEKRRLEARI------------AQLEEELEEEQSNMELLNDRFRKTTMQVDTLN 1773
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1774 TELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKfKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK 1853
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1854 --LKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEASEGLSREVNTLKN 1929
Cdd:COG4717 374 alLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELRE 453
|
....
gi 528481573 1930 RLRR 1933
Cdd:COG4717 454 ELAE 457
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1062-1215 |
5.52e-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: 55.70 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1062 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAV---LARGDEEVAQKNNALKQLRELQA-------------QLAE 1125
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteLEDLEKEIKRLELEIEEVEARIKkyeeqlgnvrnnkEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1126 LQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTldttaaqQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHG 1205
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
170
....*....|
gi 528481573 1206 TALEEISEQL 1215
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1069-1665 |
6.41e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1069 DLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLS 1148
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1149 EELEALK--TELEDTLDTTAAQQELRSKRE-QEVAELKKAIDDETR---NHESQIQEMRQRHGTA--LEEISEQLEQAKR 1220
Cdd:PRK01156 267 MELEKNNyyKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKKQilsNIDAEINKYHAIIKKLsvLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1221 VKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSclle 1300
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS---- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1301 daekkgikltKDVSSLESQLQDTQELLQEETRQKLNLSSRIR------QLEEEKNNLLEQQEEEEESRknlekqlatlqa 1374
Cdd:PRK01156 423 ----------SKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSNHIINHYNEKKSR------------ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1375 qLVETKKKLEDDVGAlegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKnrlQQELDDLMVDLdhqrqivSNLEKKQK 1454
Cdd:PRK01156 481 -LEEKIREIEIEVKD---IDEKIVDLKKRKEYLESEEINKSINEYNKIESA---RADLEDIKIKI-------NELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1455 KFDQMLAEEKTISARYAEER----------------DRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1518
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSKrtswlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1519 LISSKDDVGKNVHELEKSKRTLEQQVEEMRTQ---LEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEqneekKR 1595
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKIDNYKKQiaeIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR-----LE 701
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1596 ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIkqLRK-----LQAQMKDYQRELE 1665
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAM--IRKsasqaMTSLTRKYLFEFN 774
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1461-1724 |
6.76e-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: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1461 AEEKTISARYAEERDRaeaeaREKDTKALS-MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRT 1539
Cdd:pfam05667 226 WNSQGLASRLTPEEYR-----KRKRTKLLKrIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1540 L----EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDrDLQARDEQ---NEEKKRALVKQVREMEAELEDER 1612
Cdd:pfam05667 301 ThtekLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLE-DLESSIQElekEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1613 KQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-EEARTSRDEIFTQSKENEKKL---KSL 1688
Cdd:pfam05667 380 EELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLiEEYRALKEAKSNKEDESQRKLeeiKEL 459
|
250 260 270
....*....|....*....|....*....|....*.
gi 528481573 1689 EAEILQLQEDLASSERARRHAEQERDELADEISNSA 1724
Cdd:pfam05667 460 REKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSA 495
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1316-1868 |
8.13e-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: 57.44 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1316 LESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDdvgalegLEE 1395
Cdd:pfam05557 32 LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLAD-------ARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1396 VKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERD 1475
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1476 RAEaearekdtkalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQvEEMRTQLEELE 1555
Cdd:pfam05557 185 DSE------------IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-EKYREEAATLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1556 DELQATEdAKLRLEVNMQAMKAQFDR---DLQARDEQNEEKKRALVKQVREMEAELEDERKQRalavaakKKLEMDLKDV 1632
Cdd:pfam05557 252 LEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR-------RELEQELAQY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1633 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEART---SRDEIFTQSKENEKKLKSLE--AEILQLQEDLASSERARR 1707
Cdd:pfam05557 324 LKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQAHNEEMEAQL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1708 HAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELL--NDRFR--KTTMQVDTLNTELAGERSAA 1783
Cdd:pfam05557 404 SVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLEleRQRLReqKNELEMELERRCLQGDYDPK 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1784 -----QKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK---LK 1855
Cdd:pfam05557 484 ktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKnqrLK 563
|
570
....*....|...
gi 528481573 1856 EVFMQVEDERRHA 1868
Cdd:pfam05557 564 EVFQAKIQEFRDV 576
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1255-1928 |
1.12e-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: 57.16 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1255 HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSslesqlQDTQELLQEETRQK 1334
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1335 LNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEE--------VKRKLQKDMEV 1406
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAkynrrrskIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1407 TSQKLE--------EKAIAFDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQMLAEEKTISARyaEERDRA 1477
Cdd:pfam12128 395 IKDKLAkireardrQLAVAEDDLQALESELREQLEAGKLEFnEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1478 EAEAREKDTKAL-SMARALDEALEAKEEFERLNKQLRAEmedlisskddvgknvhelekskrtlEQQVEEMRTQLEELED 1556
Cdd:pfam12128 473 IERAREEQEAANaEVERLQSELRQARKRRDQASEALRQA-------------------------SRRLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1557 ELQA---TEDAKLRLEVNM--QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEA-ELEDERKQRALAVAAKKKLEMDLK 1630
Cdd:pfam12128 528 QLFPqagTLLHFLRKEAPDweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1631 DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSrdeiFTQSKENEKKLKS-LEAEILQLQEdlaSSERARRHA 1709
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1710 EQERDELADEISNSASGKAALLDEKRR--LEARIAQLEEELEEEQSnmellndrfrkTTMQVDTLNTELAGERSAAQKSE 1787
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVVEGA-----------LDAQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1788 NArqqLERQNK-DLKSKlqELEGSVKSKFKASIAALEAKIlqleeqleqeakERAAankiVRRTEKKLKEVFMQvEDERR 1866
Cdd:pfam12128 750 KA---LETWYKrDLASL--GVDPDVIAKLKREIRTLERKI------------ERIA----VRRQEVLRYFDWYQ-ETWLQ 807
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1867 HADQYKEQMEKANSRMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLS---REVNTLK 1928
Cdd:pfam12128 808 RRPRLATQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRcemSKLATLK 876
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1324-1567 |
1.26e-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: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1324 QELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQK 1402
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1403 DMEVTSQKLEEKAIAFDKLEktknrlQQELDDLMVDLDHQRQIVSNLEkkqkKFDQMLAEEKTISARYAEERDRAEAEAR 1482
Cdd:COG4942 98 ELEAQKEELAELLRALYRLG------RQPPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1483 EKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1562
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 528481573 1563 DAKLR 1567
Cdd:COG4942 248 FAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
969-1183 |
1.27e-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: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 969 RQKLQlekvTAEAKIK--KMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEErL 1046
Cdd:COG3206 188 RKELE----EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-S 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1047 KKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAkkeEELQAVLARGDEEVAQknnALKQLRELQAQL 1123
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREASLQAQL 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1124 AELQEDLESEKAARNKAEKLKRDlseeLEALKTELEDTLdttAAQQELRSKREQEVAELK 1183
Cdd:COG3206 337 AQLEARLAELPELEAELRRLERE----VEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
890-1112 |
1.40e-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: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 890 EEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDE--EEA 967
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElrAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 968 ARQKLQLEKVTAEA-KIKKMEEDILLLEDQN-SKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEER 1045
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1046 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKiqlaKKEEELQAVLARGDEEVAQKNNA 1112
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1581-1792 |
1.50e-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: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1581 RDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1660
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1661 QRELEEA-RTSRDEIFTQSKENEKKLKSLE----------AEILQLQEDLASSERARRHAEQERDELADEISNSASGKAA 1729
Cdd:COG4942 110 LRALYRLgRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481573 1730 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQ 1792
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1139-1856 |
1.76e-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: 56.65 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1139 KAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR-QRHGTAL--EEISEQL 1215
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNaTRHLCNLlkETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1216 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEvmarfsEGEKVKGELADRTHKIQTELDNV 1295
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE------DHEKIQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1296 SCLLEDAEKKgikltkdvsslESQLQDTQELLqEETRQKLNlssrirQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQ 1375
Cdd:pfam05483 243 SLLLIQITEK-----------ENKMKDLTFLL-EESRDKAN------QLEEKTKLQDENLKELIEKKDHLTKELEDIKMS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1376 L---VETKKKLEDDVG-ALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQ----ELDDLMVDLDHQRQIVS 1447
Cdd:pfam05483 305 LqrsMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1448 NLEKKQKKFDQMlaeektisaryAEERDRAEAEAREKDTKALSMARALDEaleaKEEFERLNKQLRAEMEDLISSKDDVG 1527
Cdd:pfam05483 385 ELQKKSSELEEM-----------TKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1528 KNVHELE-------KSKRTLEQQVEEMRTQLE-ELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQ--------NE 1591
Cdd:pfam05483 450 KEIHDLEiqltaikTSEEHYLKEVEDLKTELEkEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQediinckkQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1592 EKKRALVKQVREMEAELEDE--------RKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE 1663
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDElesvreefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1664 LEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASserARRHAEQERDELADEISNSASGKAALLDEKRRLEARIaq 1743
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA-- 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1744 leeeleeeqsnmellnDRFRKTTMQVDTLNTELAGERSAAQKSENAR--QQLERQNKDL---KSKLQElEGSVKSKFKAS 1818
Cdd:pfam05483 685 ----------------DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydKIIEERDSELglyKNKEQE-QSSAKAALEIE 747
|
730 740 750
....*....|....*....|....*....|....*...
gi 528481573 1819 IAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1856
Cdd:pfam05483 748 LSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1043-1253 |
1.85e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1043 EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRE-LQA 1121
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREeLGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1122 QLAELQED----------LESE----------------KAARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQELRSKR 1175
Cdd:COG3883 91 RARALYRSggsvsyldvlLGSEsfsdfldrlsalskiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1176 EQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1253
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1282-1518 |
1.88e-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: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1282 ADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeees 1361
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1362 rKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLqkdMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDH 1441
Cdd:COG4942 86 -AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA---LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1442 QRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1518
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
849-1414 |
2.00e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.27 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 849 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELE 924
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 925 EILHDLESRVEEEEernQSLQNEKKKMQSHiqdleeqldeeeaaRQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1004
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKN--------------EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1005 KLLedrvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERlkkeektrqelEKAKRKLDAETTDLQDQIAELQAQIDEL 1084
Cdd:pfam05483 412 KIL----AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR-----------EKEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1085 KIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldt 1164
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE----- 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1165 tAAQQELRSKREqevaELKKAIDDETRNHESQIQEMRQRHgTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVK 1244
Cdd:pfam05483 552 -SVREEFIQKGD----EVKCKLDKSEENARSIEYEVLKKE-KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1245 SLQQAKSESEHKRKKLEAQLQEVMARFsegekvkGELADRTHK-IQTELDNVSCLLEDAEK------KGIKLTKDVsSLE 1317
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKF-------EEIIDNYQKeIEDKKISEEKLLEEVEKakaiadEAVKLQKEI-DKR 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1318 SQlQDTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDvgaleglEEVK 1397
Cdd:pfam05483 698 CQ-HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIE-------KEEK 769
|
570
....*....|....*..
gi 528481573 1398 RKLQKDMEVTSQKLEEK 1414
Cdd:pfam05483 770 EKLKMEAKENTAILKDK 786
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
981-1403 |
2.18e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 981 AKIKKMEEDILLLEDQNSKF---LKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMM---------MVDLEERLKK 1048
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1049 EEKTRQELEKAKRKLDAettdLQDQIAELQAQIDELKIQL-AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1127
Cdd:COG4717 151 LEERLEELRELEEELEE----LEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1128 EDLESEKAARNKAEKLKRDLSEE-----------LEALKTELEDTLDTTAA------------QQELRSKREQEVAELKK 1184
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1185 AIDDETRN--HESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELtnEVKSLQQAKSESEHKRK-KLE 1261
Cdd:COG4717 307 LQALPALEelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGvEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1262 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLNLSSRI 1341
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481573 1342 RQLEEEKNNLleqqeeeeesrkNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1403
Cdd:COG4717 463 EQLEEDGELA------------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1507-1933 |
2.22e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1507 RLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnmqamkAQFDRDLQAR 1586
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1587 DEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV----EAQIEAANKARDEAIKQLRKLQAQMKDYQR 1662
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1663 ELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALL-----DEKRRL 1737
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLflllaREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1738 EARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKskLQELEGSVKSKFKA 1817
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1818 SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVfmqvedERRHADQYKEQMEKansRMKQLKRQLEEAEEEAT 1897
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL------EELLEALDEEELEE---ELEELEEELEELEEELE 449
|
410 420 430
....*....|....*....|....*....|....*...
gi 528481573 1898 RANASRRKLQRELDDATEASE--GLSREVNTLKNRLRR 1933
Cdd:COG4717 450 ELREELAELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
945-1698 |
3.28e-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: 55.83 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 945 QNEKKKMQSHIQDLEEQLDEEEAARQKLQLEkvtAEAKIKKMEEDILLLEDQ-NSKFLKEKKLLEDRVGEMTSQLaEEEE 1023
Cdd:TIGR01612 532 QNIKAKLYKEIEAGLKESYELAKNWKKLIHE---IKKELEEENEDSIHLEKEiKDLFDKYLEIDDEIIYINKLKL-ELKE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1024 KAKNLGKvKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQI-AELQAQIDEL-KIQLAKKEEELQAVLAR 1101
Cdd:TIGR01612 608 KIKNISD-KNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIySTIKSELSKIyEDDIDALYNELSSIVKE 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1102 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELEDTLDTTAaqQELRSKR 1175
Cdd:TIGR01612 687 NAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVElhlsniENKKNELLDIIVEIKKHIHGEINKDLNKIL--EDFKNKE 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1176 EQEVAELK--KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRvkgNLEKNKQTL------ESDNKELTNEVKSLQ 1247
Cdd:TIGR01612 765 KELSNKINdyAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQ---NYDKSKEYIktisikEDEIFKIINEMKFMK 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1248 QAKSESEHKRKKLEAQLQEVM----ARFSE-GEKVKGELADR-------------------THKIQTELDNVSCLLEDAE 1303
Cdd:TIGR01612 842 DDFLNKVDKFINFENNCKEKIdsehEQFAElTNKIKAEISDDklndyekkfndskslineiNKSIEEEYQNINTLKKVDE 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1304 KkgIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEeeKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKl 1383
Cdd:TIGR01612 922 Y--IKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIE--KSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNN- 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1384 eddvGALEGLEEVKRKLQKDMEVTSQKleekaiAFDKLEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEE 1463
Cdd:TIGR01612 997 ----ELIKYFNDLKANLGKNKENMLYH------QFDEKEKATNDIEQKIEDA-------NKNIPNIEIAIHTSIYNIIDE 1059
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1464 ktISARYAEERDRAEAEAREKDTKALSMARALDEALE-------AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKS 1536
Cdd:TIGR01612 1060 --IEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKhynfddfGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1537 KRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFDRDLQARDEQNEekkraLVKQVREMEAELEDERK 1613
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEE 1211
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1614 QRALAVA---------------AKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMkDYQRELEEARTSRDEI---F 1675
Cdd:TIGR01612 1212 VKGINLSygknlgklflekideEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEMETFNISHDDDkdhH 1290
|
810 820
....*....|....*....|...
gi 528481573 1676 TQSKENEKKLKSLEAEILQLQED 1698
Cdd:TIGR01612 1291 IISKKHDENISDIREKSLKIIED 1313
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1523-1743 |
3.67e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1523 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQFDrDLQARDEQNEEKKRALVKQVR 1602
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAK-LLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1603 EMEAELEDERKQRALAVAAKKKLEMD--LKDVEAQIEAANKARDEAIK-------QLRKLQAQMKDYQREL-EEARTSRD 1672
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528481573 1673 EIFTQSKENEKKLKSLEAEILQLQEDLAS-SERARRHAEQERD-ELADEISNSasgkaaLLdeKRRLEARIAQ 1743
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1094-1266 |
3.84e-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: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1094 ELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtlDTTAAQQELRS 1173
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1174 KREQEvaelkkAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSES 1253
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|...
gi 528481573 1254 EHKRKKLEAQLQE 1266
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1373-1591 |
4.03e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1373 QAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK 1452
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1453 QKKFDQMLAEEKTI--SARYAEERDRAEAEAREKDtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDdvgknv 1530
Cdd:COG3883 95 LYRSGGSVSYLDVLlgSESFSDFLDRLSALSKIAD----ADADLLEELKADKAELEAKKAELEAKLAELEALKA------ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528481573 1531 hELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNE 1591
Cdd:COG3883 165 -ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1185-1427 |
4.68e-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: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1185 AIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQL 1264
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1265 QEVMARFsegEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1344
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1345 EEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKT 1424
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 528481573 1425 KNR 1427
Cdd:COG4942 250 ALK 252
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1380 |
5.22e-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: 55.05 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 854 EEEMQAKDEELIKVKERQVKVENELVEMER-KHQQLLEEKNILAEQLQAETELFAeaeemrarlVAKKQELEEILHDLES 932
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQnKNHINNELESKEEQLSSYEDKLFD---------VCGSQDEESDLERLKE 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 933 RVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVG 1012
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRD 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1013 EMTS----QLAEEEEKAKNLGKVKNKQEMMMVD-------LEERLKKEEKTRQELEKAK---------RKLDAETTDLQD 1072
Cdd:TIGR00606 727 EMLGlapgRQSIIDLKEKEIPELRNKLQKVNRDiqrlkndIEEQETLLGTIMPEEESAKvcltdvtimERFQMELKDVER 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1073 QIAELQAQID---------ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQedleSEKAARNKAEKL 1143
Cdd:TIGR00606 807 KIAQQAAKLQgsdldrtvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK----SEKLQIGTNLQR 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1144 KRDLSEELEALKTELEDTLdttaaqQELRSKREQEVAELKKAIDDETRNHE--SQIQEMRQRHGTALEEISEQLEQAKRV 1221
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLI------REIKDAKEQDSPLETFLEKDQQEKEEliSSKETSNKKAQDKVNDIKEKVKNIHGY 956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1222 KGNLEKNKQTLESDN-KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSegekvkgeladrTHKIQTELDNVSCLLE 1300
Cdd:TIGR00606 957 MKDIENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID------------TQKIQERWLQDNLTLR 1024
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1301 DAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETK 1380
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKL--EENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1450-1933 |
5.53e-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: 55.07 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1450 EKKQKKFDQMLAEEKTISARYAEERDRAEA----EAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDD 1525
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1526 VGKNVHELEKSKRTLEQQVEEM--------RTQLEELEDELQATEDAklrlevnmQAMKAQFDRDLQARDEQNEEKKRAL 1597
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1598 VKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQ 1677
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1678 SKEN-------EKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1750
Cdd:TIGR02169 415 LQRLseeladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1751 EQSNMELLNDRFRKTTMQVDTLNTEL------------------------AGERSAAQKSEN------ARQQLERQN--- 1797
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgeryataievaAGNRLNNVVVEDdavakeAIELLKRRKagr 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1798 ------KDLKSKLQELE--------------------------------------------------------------- 1808
Cdd:TIGR02169 575 atflplNKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtlegelfeksga 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1809 ---GSVKSKFKASIAA-LEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQ 1884
Cdd:TIGR02169 655 mtgGSRAPRGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1885 LKRQLEEAEEE-------ATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1933
Cdd:TIGR02169 735 LKERLEELEEDlssleqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1039-1916 |
5.68e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1039 MVDLEERLKKEEKT---RQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlakkEEELQAVLARgdeeVAQKNNAL-- 1113
Cdd:PRK04863 275 MRHANERRVHLEEAlelRRELYTSRRQLAAEQYRLVEMARELAELNEAESDL----EQDYQAASDH----LNLVQTALrq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1114 -KQLRELQAQLAELQEDLESEKAARNKAeklkRDLSEELEALKTELEDTLDTTAAQqelrskreqeVAELKKAID-DETR 1191
Cdd:PRK04863 347 qEKIERYQADLEELEERLEEQNEVVEEA----DEQQEENEARAEAAEEEVDELKSQ----------LADYQQALDvQQTR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1192 NheSQIQEMRQrhgtALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVmarf 1271
Cdd:PRK04863 413 A--IQYQQAVQ----ALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV---- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1272 segekvkgeladrtHKIQTELDNvscllEDAEKKGIKLTKDVSSLESQLQDTQELLQE--ETRQKLNLSSRIRQLEEEKN 1349
Cdd:PRK04863 483 --------------RKIAGEVSR-----SEAWDVARELLRRLREQRHLAEQLQQLRMRlsELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1350 NLLEQQEeeeesrkNLEKQLATLQAQLVEtkkkleddvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK---- 1425
Cdd:PRK04863 544 KRLGKNL-------DDEDELEQLQEELEA----------RLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawl 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1426 ------NRLQ----------QELDDLMVD-LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKA 1488
Cdd:PRK04863 607 aaqdalARLReqsgeefedsQDVTEYMQQlLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1489 LSMARAlDEALEAKEEFERLNKQLR---------------AEMEDL----------ISSKDDVGKNVHELEK------SK 1537
Cdd:PRK04863 687 LSEIYD-DVSLEDAPYFSALYGPARhaivvpdlsdaaeqlAGLEDCpedlyliegdPDSFDDSVFSVEELEKavvvkiAD 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1538 RTL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFDRDLQ-----ARDEQNEEKKR 1595
Cdd:PRK04863 766 RQWrysrfpevplfgraarEKRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELR 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1596 ALVKQVREMEAELED----ERKQRALAVAAKKKL--------EMDLKDVEAQIEAANKARDEaIKQLRKLQAQMKDYQRE 1663
Cdd:PRK04863 841 QLNRRRVELERALADhesqEQQQRSQLEQAKEGLsalnrllpRLNLLADETLADRVEEIREQ-LDEAEEAKRFVQQHGNA 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1664 LEeartsrdeiftQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAAllDEKRRLEARIAq 1743
Cdd:PRK04863 920 LA-----------QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAKNSD- 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1744 leeeleeeqsnmelLNDRFRkttmqvdtlntelagersaaQKSENARQQLERQNKDLKSKLQELegsvkSKFKASIAALE 1823
Cdd:PRK04863 986 --------------LNEKLR--------------------QRLEQAEQERTRAREQLRQAQAQL-----AQYNQVLASLK 1026
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1824 AkilqleeqleqeakERAAANKIVRRTEKKLKEVFMQVEDE-----RRHADQYKEQMEKANSRMKQLKRQLEEAEEEATR 1898
Cdd:PRK04863 1027 S--------------SYDAKRQMLQELKQELQDLGVPADSGaeeraRARRDELHARLSANRSRRNQLEKQLTFCEAEMDN 1092
|
970
....*....|....*...
gi 528481573 1899 ANASRRKLQRELDDATEA 1916
Cdd:PRK04863 1093 LTKKLRKLERDYHEMREQ 1110
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
931-1142 |
5.92e-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: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 931 ESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIlllEDQNSKFLKEKKLLEDR 1010
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1011 VGEM-----TSQLAEEEEKAKNLGKVKNKQEMMMVDLE---ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQID 1082
Cdd:COG3883 92 ARALyrsggSVSYLDVLLGSESFSDFLDRLSALSKIADadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1083 ELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1142
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1314-1738 |
6.61e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1314 SSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEkQLATLQAQLVETKKKLEDDVGALEG 1392
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1393 LEEVKRKLQKDMEVTSQ---------KLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkfDQMLAEE 1463
Cdd:COG4717 124 LLQLLPLYQELEALEAElaelperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1464 KTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLR-----AEMEDLISSKDDVGKNVHE------ 1532
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaAALLALLGLGGSLLSLILTiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1533 ------------LEKSKRTLEQQVEEMR--TQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDL-----QARDEQNEEK 1593
Cdd:COG4717 281 lvlgllallfllLAREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1594 KRALVKQVREMEAEL--------EDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRK--LQAQMKDYQRE 1663
Cdd:COG4717 361 EELQLEELEQEIAALlaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1664 LEEARTSRDEIftqskenEKKLKSLEAEILQLQED--LASSERARRHAEQERDELADEISNSASGKAALLDEKRRLE 1738
Cdd:COG4717 441 LEELEEELEEL-------REELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1023-1155 |
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 528481573 1023 EKAK-NLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLakkEEELQAVLAR 1101
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1102 GDEEVAQknnALKQLRELQAQLA------ELQEDLESEKAARNKAEKLKRDLSEELEALK 1155
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYasvkahELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1342-1931 |
7.56e-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: 54.74 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1342 RQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAiafDKL 1421
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV---HEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1422 EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDR-AEAEAREKDTKALSMARALD---- 1496
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmSTMHFRSLGSAISKILRELDteis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1497 -------------EAL--EAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTleqQVEEMRTQLEELEDELQAT 1561
Cdd:pfam15921 235 ylkgrifpvedqlEALksESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARS---QANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1562 EDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELE----------------DERKQRALAVAAKKKL 1625
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTearterdqfsqesgnlDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1626 EMDLKDVEAQ------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAE-- 1691
Cdd:pfam15921 392 ELSLEKEQNKrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQle 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1692 -----ILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNmellNDRFRKTT 1766
Cdd:pfam15921 472 stkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE----GDHLRNVQ 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1767 MQVDTLNTELAGERSAA----QKSENARQ-----------------QLERQNKDLKSKLQELEgSVKSKFKASIAALEAK 1825
Cdd:pfam15921 548 TECEALKLQMAEKDKVIeilrQQIENMTQlvgqhgrtagamqvekaQLEKEINDRRLELQEFK-ILKDKKDAKIRELEAR 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1826 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQME--KANSRMK---------QLKRQLEEAEE 1894
Cdd:pfam15921 627 VSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKseemetttnKLKMQLKSAQS 706
|
650 660 670
....*....|....*....|....*....|....*..
gi 528481573 1895 EATRANASRRKLQRELDDATEASEGLSREVNTLKNRL 1931
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI 743
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1367-1933 |
9.64e-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: 54.07 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1367 KQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEekaiafDKLEKTKNRLQQELDDLMVDLDHQRQIV 1446
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1447 SNLEKKQKKFDQMLAEEKtisARYAEERD--RAEAEAREKDTKALsmaraLDEALEAKEEFERLnKQLRAEmedliSSKD 1524
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKAL-----TGKHQDVTAKYNRR-RSKIKE-----QNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1525 DVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlEVNMQamkaqfdrdlQARDEQNEEKKRALVKQVREM 1604
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL-EFNEE----------EYRLKSRLGELKLRLNQATAT 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1605 EAELEDERKQRALAVAAKKKLEMDLKDVE-AQIE--AANKARDEAIKQLRKLQAQMKDYQRELEEARTsrdEIFTQSKEN 1681
Cdd:pfam12128 460 PELLLQLENFDERIERAREEQEAANAEVErLQSElrQARKRRDQASEALRQASRRLEERQSALDELEL---QLFPQAGTL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1682 EKKLKSLEAEILQLQEDLASSE---RARRHAEQERDELADEISNSASGkaalLDEKR-----------RLEARIAQLEEE 1747
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPEllhRTDLDPEVWDGSVGGELNLYGVK----LDLKRidvpewaaseeELRERLDKAEEA 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1748 LEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKiL 1827
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ-L 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1828 QLEEQLEQEAKERAAANKIVRRTEK--KLKEVfmqVEDERRHADQYKEQMEKANSrmkQLKRQLEEAEEEATRANASRrk 1905
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKqaYWQVV---EGALDAQLALLKAAIAARRS---GAKAELKALETWYKRDLASL-- 763
|
570 580
....*....|....*....|....*...
gi 528481573 1906 lqrelDDATEASEGLSREVNTLKNRLRR 1933
Cdd:pfam12128 764 -----GVDPDVIAKLKREIRTLERKIER 786
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1510-1726 |
1.13e-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: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1510 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRdlQARDEQ 1589
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1590 NEEKKR-------------ALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQ 1656
Cdd:COG3883 97 RSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1657 MKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1726
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
969-1125 |
1.14e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 969 RQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknLGKVKNKQEMmmvdleERLKK 1048
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEY------EALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1049 EEKTrqeLEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1125
Cdd:COG1579 97 EIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1633-1856 |
1.18e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1633 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLasserarrhaEQE 1712
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1713 RDELADEI------SNSASGKAALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAqks 1786
Cdd:COG3883 85 REELGERAralyrsGGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1787 ENARQQLERQNKDLKSKLQELEgSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKE 1856
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
797-1259 |
1.58e-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: 53.43 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 797 QSVCRGYLARkafAKKQQQLSALKVLQRNCAAY-----LKLRHWQWWRLFTKVKPLLQVTRQEEEMQAKDEELIKVKErq 871
Cdd:TIGR00618 419 FRDLQGQLAH---AKKQQELQQRYAELCAAAITctaqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL-- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 872 vKVENELVEMER---KHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEK 948
Cdd:TIGR00618 494 -ARLLELQEEPCplcGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 949 KKMQSHIQDLEEQLDEEEAARQKLQ-LEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKN 1027
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQ 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1028 LGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQD---QIAELQAQIDELKIQLAKKEEELQAVLARGDE 1104
Cdd:TIGR00618 653 LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEmlaQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1105 EVAQKNNALKQ-LRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELK 1183
Cdd:TIGR00618 733 DLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1184 KAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEsdnkELTNEVKSLQQAKSESEHKRKK 1259
Cdd:TIGR00618 813 PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----QLTQEQAKIIQLSDKLNGINQI 884
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1246-1911 |
1.63e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.19 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1246 LQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADrthKIQTELDNVSclLEDAEKKGIKLTKDVSSLESQLQDTQE 1325
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE---EIQENKDLIK--ENNATRHLCNLLKETCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1326 LLQEETRQ-KLNLSSRIrqleeEKNNLLEQQEEEEESRKNLEKQLatlqaqlvetkkKLEDDVGALEGLEEVKRKLQKDm 1404
Cdd:pfam05483 176 YEREETRQvYMDLNNNI-----EKMILAFEELRVQAENARLEMHF------------KLKEDHEKIQHLEEEYKKEIND- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1405 evtsqklEEKAIAFDKLEKTKNrlQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEARek 1484
Cdd:pfam05483 238 -------KEKQVSLLLIQITEK--ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1485 dtKALSMARALDEALE-AKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAted 1563
Cdd:pfam05483 307 --RSMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI--- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1564 aklrlevnmqamkaqFDRDLQARDEQNEEkkraLVKQVREMEAELEDERKqralAVAAKKKLEMDLKDVEAQIEAANKAR 1643
Cdd:pfam05483 382 ---------------ITMELQKKSSELEE----MTKFKNNKEVELEELKK----ILAEDEKLLDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1644 DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNS 1723
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1724 ASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1803
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1804 LQELEGSVKSKFKasiaaleaKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMK 1883
Cdd:pfam05483 596 CNNLKKQIENKNK--------NIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
650 660
....*....|....*....|....*...
gi 528481573 1884 QLKRQLEEAEEEATRANASRRKLQRELD 1911
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
854-1343 |
1.70e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 854 EEEMQAKDEELIKVKErqvkvenELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVA---KKQELEEILHDL 930
Cdd:PRK01156 189 EEKLKSSNLELENIKK-------QIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSledMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 931 ESRVEEEEERN---QSLQNEKKKMQS--------HIQDLEEQLDEEEAARQKLQ---LEKVTAEAKIKKMEEdillLEDQ 996
Cdd:PRK01156 262 ESDLSMELEKNnyyKELEERHMKIINdpvyknrnYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 997 NSKFLKEKKLLEDRVGEMT----------SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAE 1066
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1067 TTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARG----------------------------DEEVAQKNNALKQLRE 1118
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhiinhynekksrlEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1119 LQAQLAELQEDLESEKAARNKAEKLKrdlseeLEALKTELEDTLDTTAAQQELRSKREQEVAELKKA-IDDETRNHESQI 1197
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1198 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN-----------KELTNEVKSLQQAKSESEHKRKKLEA---- 1262
Cdd:PRK01156 572 NALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFpddksyidksiREIENEANNLNNKYNEIQENKILIEKlrgk 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1263 --QLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDA-------EKKGIKLTKDVSSLESQLQDTQELLQ--EET 1331
Cdd:PRK01156 652 idNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlESTIEILRTRINELSDRINDINETLEsmKKI 731
|
570
....*....|..
gi 528481573 1332 RQKLNLSSRIRQ 1343
Cdd:PRK01156 732 KKAIGDLKRLRE 743
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
982-1190 |
1.70e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.01 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 982 KIKKMEEDILL-LEDQNSKFLKE-------------KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK--------QEMMM 1039
Cdd:PRK05771 2 APVRMKKVLIVtLKSYKDEVLEAlhelgvvhiedlkEELSNERLRKLRSLLTKLSEALDKLRSYLPKlnplreekKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1040 VDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELK------------------------IQLAKKEEEL 1095
Cdd:PRK05771 82 KSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfkyvsvfvgtVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1096 QAVLARGDEEVAQKNN---------------ALKQLRELQAQLAELQEDLESEKAARNKAEKLKR------DLSEELEAL 1154
Cdd:PRK05771 162 LESDVENVEYISTDKGyvyvvvvvlkelsdeVEEELKKLGFERLELEEEGTPSELIREIKEELEEiekereSLLEELKEL 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 528481573 1155 KTELEDTLdtTAAQQELRSKREQEVAELKKAIDDET 1190
Cdd:PRK05771 242 AKKYLEEL--LALYEYLEIELERAEALSKFLKTDKT 275
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1419-1632 |
1.74e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1419 DKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAR 1482
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1483 EKDTKALSMARALDEALEAKEEFERLNKQLR---------AEMEDLISSKDDVGKnvhelekskrtLEQQVEEMRTQLEE 1553
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITK-----------IKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1554 LEDELQatEDAKLRLEVNMQAMKAqfdRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1632
Cdd:PHA02562 318 LDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1242-1621 |
1.92e-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: 52.38 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1242 EVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQ 1321
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1322 DtQELLQEETRQKL-NLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKL 1400
Cdd:pfam19220 101 E-AEAAKEELRIELrDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1401 QKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmlAEEKTISARYAEERDRAEAE 1480
Cdd:pfam19220 180 QALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQ-----------------AERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1481 ARekdtkalSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA 1560
Cdd:pfam19220 243 RA-------SLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1561 TEDAKLRLEVNMQAM-KAQFDRD------------LQARDEQ----NEEKKRALVKQVREMEAELEDERKQRALAVAA 1621
Cdd:pfam19220 316 MQRARAELEERAEMLtKALAAKDaaleraeeriasLSDRIAEltkrFEVERAALEQANRRLKEELQRERAERALAQGA 393
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1403-1622 |
1.94e-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: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1403 DMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE-EKTISARYAEERDRAEAEA 1481
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEaEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1482 REKDT----KALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1557
Cdd:COG3883 97 RSGGSvsylDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1558 LQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAK 1622
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
853-1076 |
2.27e-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: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 853 QEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLVAKKQELEEILH 928
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 929 DLESRVEEEEERNQSLQneKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAE--AKIKKMEEDILLLEDQNSKFLKEKKL 1006
Cdd:COG4942 98 ELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArrEQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1007 LEdrvgemtSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1076
Cdd:COG4942 176 LE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1095-1324 |
3.05e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1095 LQAVLARGDEEVAQKNNALKQLRE----LQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEdtldttAAQQE 1170
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA------EAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1171 LRSKREQevaeLKKaiddetRNHESQIQEMRQRHGTAL---EEISEQLEQAKRVKGNLEKNKQTLE---SDNKELTNEVK 1244
Cdd:COG3883 81 IEERREE----LGE------RARALYRSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADADLLEelkADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1245 SLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQ 1324
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
1041-1154 |
3.73e-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: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1041 DLEERLK--KEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEEL----------------------- 1095
Cdd:pfam14362 107 EIDRELLeiQQEEADAAKAQLAAAYRARLAELEAQIAALDAEIDAAEARLDALQAEArceldgtpgtgtgvpgdgpvakt 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528481573 1096 -QAVLARGDEEVAQ-KNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1154
Cdd:pfam14362 187 kQAQLDAAQAELAAlQAQNDARLAALRAELARLTAERAAARARSQAAIDGDDGLLARLEAL 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1686-1930 |
3.94e-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: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1686 KSLEAEILQLQEDLASSERARRHAEQERDeladeisnsasgKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1765
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDARE------------QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1766 tmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQLEeqleqeaKERAAANK 1845
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLE-------RELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1846 IVRRTEKKLKEVFMQVEDErrhADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDateasegLSREVN 1925
Cdd:COG4913 360 RRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 528481573 1926 TLKNR 1930
Cdd:COG4913 430 SLERR 434
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1042-1610 |
4.07e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1042 LEERLKKEEKTRQELEKAKRKLDAETT-------DLQDQIAELQAQIDELKIQLAKKE--EELQAVLARGDEEVAQKNNA 1112
Cdd:PRK10246 299 IQEQSAALAHTRQQIEEVNTRLQSTMAlrarirhHAAKQSAELQAQQQSLNTWLAEHDrfRQWNNELAGWRAQFSQQTSD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1113 LKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE---LEDTLDTTAAQQELRSKREQEVAELKKAIDDE 1189
Cdd:PRK10246 379 REQLRQWQQQLTHAEQKLNALPAI---TLTLTADEVAAALAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1190 TRNHESQIQEMRQRHGTALEEISEQ---LEQAKRVKgNLEKNKQTLESDNK-----ELTNEVKSLQQAKSESEHKRKkLE 1261
Cdd:PRK10246 456 QTQRNAALNEMRQRYKEKTQQLADVktiCEQEARIK-DLEAQRAQLQAGQPcplcgSTSHPAVEAYQALEPGVNQSR-LD 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1262 AQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELL-----QEETRQKLN 1336
Cdd:PRK10246 534 ALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldaQEEHERQLR 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1337 LSSRIRQLEEEKNNLleqqeeeeesrknlEKQLATLQAQLVETKKKLEDDVGAL------EGLEEvkrKLQKDMEVTSQK 1410
Cdd:PRK10246 614 LLSQRHELQGQIAAH--------------NQQIIQYQQQIEQRQQQLLTALAGYaltlpqEDEEA---SWLATRQQEAQS 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1411 LEEKAIAFDKLEKTKNRLQQELDDL--MVDLDHQRQIVSnLEKKQKKFDQML---AEEKTISARYAEERDRAeAEAREKD 1485
Cdd:PRK10246 677 WQQRQNELTALQNRIQQLTPLLETLpqSDDLPHSEETVA-LDNWRQVHEQCLslhSQLQTLQQQDVLEAQRL-QKAQAQF 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1486 TKALSMARALDealeaKEEFerlnkqLRAEMEDlisskddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA----- 1560
Cdd:PRK10246 755 DTALQASVFDD-----QQAF------LAALLDE---------ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQhqqhr 814
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1561 ------TEDAKlRLEVNMQAMKAQFdRDLQAR----------DEQNEEKKRALVKQVREMEAELED 1610
Cdd:PRK10246 815 pdgldlTVTVE-QIQQELAQLAQQL-RENTTRqgeirqqlkqDADNRQQQQALMQQIAQATQQVED 878
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1432-1810 |
4.38e-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: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1432 LDDLMVDLDHQRQIvsNLEKKQKKFDQMlaeektisaryAEERDRAEaeaREKDTKALSMARALDEALEAKEEFERLNKQ 1511
Cdd:pfam17380 271 LNQLLHIVQHQKAV--SERQQQEKFEKM-----------EQERLRQE---KEEKAREVERRRKLEEAEKARQAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1512 LRAEMEDLisskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRlevnmqamkaQFDRDLQARDEQNE 1591
Cdd:pfam17380 335 IYAEQERM------------AMERERELERIRQEERKRELERIRQEEIAMEISRMR----------ELERLQMERQQKNE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1592 ekkralvkQVREmeaELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1671
Cdd:pfam17380 393 --------RVRQ---ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1672 DEIFTQsKENEKKLKSLEAEILQLQEDLASSERaRRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEE 1751
Cdd:pfam17380 462 VERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1752 QSNMELLNDRFRKTTMQVDTLNTElagERSAAQKSENARQQLeRQNKDLKSKLQELEGS 1810
Cdd:pfam17380 540 EERRKQQEMEERRRIQEQMRKATE---ERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1532-1708 |
4.77e-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: 49.92 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1532 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDlqaRDEQNEEKKralVKQVREMEAELEDE 1611
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRN---NKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1612 RKQRAlavaakkKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAqmkdyqrELEEARTSRDEIFTQSKENEKKLKSLEAE 1691
Cdd:COG1579 102 KRRIS-------DLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|....*....
gi 528481573 1692 ILQL--QEDLASSERARRH 1708
Cdd:COG1579 168 LAAKipPELLALYERIRKR 186
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1074-1313 |
4.91e-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: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1074 IAELQAQIDELKIQLAKKEEELQAvlaRGDEEVAQKNNA-LKQlrELQAQLAEL---QEDLES-EKAARNKAEKLKRD-L 1147
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNA---LADKERAEADRQrLEQ--EKQQQLAAIsgsQSQLEStDQNALETNGQAQRDaI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1148 SEELEALKTELE------DTLDTTAAQQELRSK--REQEVAELKKAID---DETRNHES-QIQEMRQRHGTALEEISEQL 1215
Cdd:NF012221 1612 LEESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQeqlDDAKKISGkQLADAKQRHVDNQQKVKDAV 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1216 EQAKRVKGNLEKNKQTLESDnkeltnevksLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNV 1295
Cdd:NF012221 1692 AKSEAGVAQGEQNQANAEQD----------IDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENK 1761
|
250
....*....|....*...
gi 528481573 1296 SCLLEdAEKKGIKLTKDV 1313
Cdd:NF012221 1762 ANQAQ-ADAKGAKQDESD 1778
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1038-1419 |
5.01e-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: 51.43 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1038 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLR 1117
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1118 ELQAQLAELQEDLESekaarnkaeklkrdLSEELEALKTELEDTLDTtaAQQELRSKREQEvaELKKAIDDETRNHESQI 1197
Cdd:pfam07888 126 AHEARIRELEEDIKT--------------LTQRVLERETELERMKER--AKKAGAQRKEEE--AERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1198 QEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTL------ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1271
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1272 SEGE-----------KVKGELADRTHKIQTELDNVS----CLLEDAEKKGIKLTKdvssLESQLQDTQELLQEETRQKLN 1336
Cdd:pfam07888 268 DRTQaelhqarlqaaQLTLQLADASLALREGRARWAqereTLQQSAEADKDRIEK----LSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1337 LSSrirQLEEEKnnlLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKdmeVTSQKLEEKAI 1416
Cdd:pfam07888 344 LEV---ELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET---VADAKWSEAAL 414
|
...
gi 528481573 1417 AFD 1419
Cdd:pfam07888 415 TST 417
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1696-1934 |
5.02e-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: 50.92 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1696 QEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTE 1775
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1776 LAGERSAAQKSENARQQLERQNKdLKSKLQeleGSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLK 1855
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1856 EVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRANASRRKLQRELDDATEASEGLSREVNTLKNRLRRG 1934
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
975-1484 |
6.80e-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: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 975 EKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQ 1054
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK----------YLEALNKKLNEKES 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1055 ELEKAKRKLDAettdLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQE------ 1128
Cdd:pfam05557 98 QLADAREVISC----LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqrik 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1129 -----------------DLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETR 1191
Cdd:pfam05557 174 elefeiqsqeqdseivkNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1192 NH--ESQIQE---MRQRHGTAL---EEISEQLEQakrvkgnLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1263
Cdd:pfam05557 254 KEklEQELQSwvkLAQDTGLNLrspEDLSRRIEQ-------LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1264 LQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLED------AEKKGIKLTKDVSSLESQLQDTQ-----------EL 1326
Cdd:pfam05557 327 IEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESydkeltMSNYSPQLLERIEEAEDMTQKMQahneemeaqlsVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1327 LQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESR-KNLEKQLATLQAQLvetkKKLEDDVGALEgLEEVKRKLQKDME 1405
Cdd:pfam05557 407 EEELGGYKQQAQTLERELQALRQQESLADPSYSKEEvDSLRRKLETLELER----QRLREQKNELE-MELERRCLQGDYD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1406 VTSQK---LEEKAIAfdkleKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERdRAEAEAR 1482
Cdd:pfam05557 482 PKKTKvlhLSMNPAA-----EAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL-RKELESA 555
|
..
gi 528481573 1483 EK 1484
Cdd:pfam05557 556 EL 557
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
887-1345 |
7.53e-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: 50.89 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 887 QLLEEKNILaEQLQAETELfAEAEEMRARLvakkqELEEILHDLESRVEEEEERNQSLQNEKKKMQshiQDLEEQLDEEE 966
Cdd:pfam05557 3 ELIESKARL-SQLQNEKKQ-MELEHKRARI-----ELEKKASALKRQLDRESDRNQELQKRIRLLE---KREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 967 AARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMmmvdLEERL 1046
Cdd:pfam05557 73 EQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL----LKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1047 KKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEE-----ELQAVLARGDEEVAQKNNALKQLRELQA 1121
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSElaripELEKELERLREHNKHLNENIENKLLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1122 QLAELQEDLESEKAARNKAEKLKRDLS---EELEALKTELEDTLDTTAAQQELRSK------REQEVAELKKAIDDETRN 1192
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLELEKEkleQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqREIVLKEENSSLTSSARQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1193 HESQIQEMRQRHGTALEEISE---QLEQAKRVKGNLEKN-----------KQTLESDNKELTNEVKSLQQAK--SESEHK 1256
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDlnkKLKRHKALVRRLQRRvllltkerdgyRAILESYDKELTMSNYSPQLLEriEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1257 RKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKltKDVSSLESQLQDTQELLQEETRQKLN 1336
Cdd:pfam05557 389 TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNE 466
|
....*....
gi 528481573 1337 LSSRIRQLE 1345
Cdd:pfam05557 467 LEMELERRC 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1485-1729 |
8.01e-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: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1485 DTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL------ 1558
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1559 -QATEDAKLRLEV------------NMQAMKAQFDRDLQARDEQNEEKKralvkQVREMEAELEDERKQralAVAAKKKL 1625
Cdd:COG3883 95 lYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKA-----ELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1626 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1705
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260
....*....|....*....|....
gi 528481573 1706 RRHAEQERDELADEISNSASGKAA 1729
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1021-1155 |
9.84e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.63 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1021 EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL--KIQLAKKEEELQav 1098
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLerELSEARSEERRE-- 460
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528481573 1099 lARGDEEVAQKNNALKQLR----ELQAQLAELQEDLESEKAARNKaeklkrDLSEELEALK 1155
Cdd:COG2433 461 -IRKDREISRLDREIERLEreleEERERIEELKRKLERLKELWKL------EHSGELVPVK 514
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1533-1737 |
1.06e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1533 LEKSK-RTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDE 1611
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1612 RKQRALAVAAKKKLEMDLKDVEAQIEAANK----------------ARDEAIKQLRKLQAQMKDYQRELEEARTSRDE-- 1673
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1674 -IFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRL 1737
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
900-1138 |
1.14e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 900 QAETELFAEAEEMRArLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarQKLQLEKVTA 979
Cdd:COG3883 13 FADPQIQAKQKELSE-LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 980 EAKIKKMEE-------------------DILLLEDQNSKFLKEKKLLeDRVGEMTSQLAEEEEKAKNlgKVKNKQEmmmv 1040
Cdd:COG3883 78 EAEIEERREelgeraralyrsggsvsylDVLLGSESFSDFLDRLSAL-SKIADADADLLEELKADKA--ELEAKKA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1041 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQ 1120
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|....*...
gi 528481573 1121 AQLAELQEDLESEKAARN 1138
Cdd:COG3883 231 AAAAAAAAAAAAAASAAG 248
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
867-1163 |
1.15e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 867 VKERQVKVEnelvEMERKHQQLLEEKNILAEQLQAETELfAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQN 946
Cdd:PRK02224 470 IEEDRERVE----ELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 947 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDIllledqnskflkekklleDRVGEMTSQLAEEEEKAK 1026
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI------------------ESLERIRTLLAAIADAED 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1027 NLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDlqDQIAELQAQIDELKIQLAKKEEELQAVLARGDE-- 1104
Cdd:PRK02224 607 EIERLREKRE----ALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDlq 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1105 -EVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLK---RDLSEEL-----EALKTELEDTLD 1163
Cdd:PRK02224 681 aEIGAVENELEELEELRERREALENRVEALEALYDEAEELEsmyGDLRAELrqrnvETLERMLNETFD 748
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1050-1326 |
1.28e-05 |
|
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: 49.69 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1050 EKTRQELEKAkRKLDAETTD----LQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAE 1125
Cdd:pfam04108 17 TDARSLLEEL-VVLLAKIAFlrrgLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1126 LQE-----------DLESEKAARNKAEKLKRDLSEELEALKTELED-TLDTTAAQQELRSKreQEVAELKKAIDDETRNH 1193
Cdd:pfam04108 96 PPGeekqktlldfiDEDSVEILRDALKELIDELQAAQESLDSDLKRfDDDLRDLQKELESL--SSPSESISLIPTLLKEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1194 ESQIQEMRQRhgtaLEEIS---EQLEQAKRV-KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMA 1269
Cdd:pfam04108 174 ESLEEEMASL----LESLTnhyDQCVTAVKLtEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNS 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1270 RFSEGEKVKGELADrthkIQTELDN-VSCLLEDAEkkgiKLTKDVSSLESQLQDTQEL 1326
Cdd:pfam04108 250 LIDELLSALQLIAE----IQSRLPEyLAALKEFEE----RWEEEKETIEDYLSELEDL 299
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1063-1278 |
1.28e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1063 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLargDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEK 1142
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY---DELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1143 LKRDLSEELEALKTEL----EDTLDTTAAQQ-----ELRSKREQEVAELKKAIDDEtrnhESQIQEMRQRhgtaLEEISE 1213
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQisegpDRITKIKDKLKELQHSLEKL----DTAIDELEEI----MDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1214 QLEQAKRVKGNLEKNKQTL---ESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1278
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLitlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
660-684 |
1.29e-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: 1.29e-05
10 20
....*....|....*....|....*
gi 528481573 660 YKESLTKLMATLRNTNPNFVRCIIP 684
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1042-1217 |
1.38e-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: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1042 LEERLKKEEKTRQELEK-----AKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLArgdeevaqknnalKQL 1116
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLG-------------QNV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1117 RELQAQLAELQEDLesEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQ-----QELRSKREQEVAELKKAIDDETR 1191
Cdd:pfam01442 69 EELRQRLEPYTEEL--RKRLNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*.
gi 528481573 1192 NHESQIQEMRQRHGTALEEISEQLEQ 1217
Cdd:pfam01442 147 EVQAQLSQRLQELREKLEPQAEDLRE 172
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1037-1268 |
1.42e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1037 MMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQL 1116
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1117 RELQAQLAELQEDLESEKAARNKAEKLKRD---LSEELEALKTELEDTLDTTAAQQEL--RSKR-EQEVAELKKAID--D 1188
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEknE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1189 ETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKE---LTNEVKSLQQAKSESEHKRKKLEAQLQ 1265
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEadeLHKEIVEAQEKADELHEEIIELQKELR 240
|
...
gi 528481573 1266 EVM 1268
Cdd:COG1340 241 ELR 243
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1000-1346 |
1.52e-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: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1000 FLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQA 1079
Cdd:COG5185 171 ELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1080 QIDELKIQLAKKEEELQAVLARGDEEVA----QKNNALKQLRELQAQLAELQEDLESEKA------------ARNKAEKL 1143
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGENAESSKrlneNANNLIKQFENTKEKIAEYTKSIDIKKAtesleeqlaaaeAEQELEES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1144 KRDLSEELEALKTELEDTLDT-TAAQQELRSKREQEVAELKKAIDDET-RNHESQIQEMRQRHGTALEEiseQLEQAKRV 1221
Cdd:COG5185 331 KRETETGIQNLTAEIEQGQESlTENLEAIKEEIENIVGEVELSKSSEElDSFKDTIESTKESLDEIPQN---QRGYAQEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1222 KGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKiqteldnvSCLLED 1301
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEIN--------RSVRSK 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 528481573 1302 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1346
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 ... |
1056-1212 |
1.58e-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: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1056 LEKAKRKLDAETTDLQDQIAELQAQIDelkiQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKA 1135
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1136 ARNKAEKLKRDLsEELEALKTELEDTLDTTAAQQE-LRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALEEIS 1212
Cdd:pfam00529 132 LAPIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1588-1740 |
1.73e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.90 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1588 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE--------AANKARD----EAIKQLRKLQA 1655
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREdlarEALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1656 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQERDELADEISNSASGKAALLDEK- 1734
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK----KDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174
|
....*.
gi 528481573 1735 RRLEAR 1740
Cdd:COG1842 175 EEMEAR 180
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1125-1385 |
1.90e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1125 ELQEDLESEK--AARNKAEKLK-RDLSEELEALKTELEDTLDTTAAQQ----ELRSKREQEVAELKKAIDD---ETRNHE 1194
Cdd:PHA02562 154 KLVEDLLDISvlSEMDKLNKDKiRELNQQIQTLDMKIDHIQQQIKTYNknieEQRKKNGENIARKQNKYDElveEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1195 SQIqemrqrhgtalEEISEQLEqakrvkgNLEKNKQTLESDNKELTNEvkslqQAKSESEHKRKKLEAQLQE-------V 1267
Cdd:PHA02562 234 AEI-----------EELTDELL-------NLVMDIEDPSAALNKLNTA-----AAKIKSKIEQFQKVIKMYEkggvcptC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1268 MARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGI---KLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1344
Cdd:PHA02562 291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDefnEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 528481573 1345 EEEknnlleqqeeeeesRKNLEKQLATLQAQLVETKKKLED 1385
Cdd:PHA02562 371 QAE--------------FVDNAEELAKLQDELDKIVKTKSE 397
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
904-1540 |
1.94e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 904 ELFAEAEEMRaRLVAKKQELEEILHDLESRVEEEeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKI 983
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 984 KKMEEDILLLED---QNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGkvknkqemmmvDLEERLKKEEKTRQeleKAK 1060
Cdd:PRK01156 228 NNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYK-----------ELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1061 RKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ--AVLARGDEEVAQKNnalKQLRELQAQLAELQEDLESEKAARN 1138
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKK---SRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1139 KAEKLK---RDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRhgtaLEEISEQL 1215
Cdd:PRK01156 371 SIESLKkkiEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNM 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1216 ------------------EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEA-QLQEVMARFSEGEK 1276
Cdd:PRK01156 447 emlngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1277 VKGELADRTHKIQTeldnvsclLEDAEKKGIKLTKDVSSLEsqlqdtQELLQEETRQKLNLSSRIRQLEEEknnlleqqe 1356
Cdd:PRK01156 527 ARADLEDIKIKINE--------LKDKHDKYEEIKNRYKSLK------LEDLDSKRTSWLNALAVISLIDIE--------- 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1357 eeeesrknlekqlaTLQAQLVETKKKLEDdvgALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNrlqqELDDLM 1436
Cdd:PRK01156 584 --------------TNRSRSNEIKKQLND---LESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN----EIQENK 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1437 VDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEaearekdtkalSMARALDEALEAKEEFERLNKQLRAEM 1516
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLK-----------KSRKALDDAKANRARLESTIEILRTRI 711
|
650 660
....*....|....*....|....
gi 528481573 1517 EDLISSKDDVGKNVHELEKSKRTL 1540
Cdd:PRK01156 712 NELSDRINDINETLESMKKIKKAI 735
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
922-1562 |
2.13e-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: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 922 ELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEqldeeeaarQKLQLEKVTAEA-------KIKKMEEDILLLE 994
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA---------QINDLEDVADKAisnddpeEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 995 DQNSKFLKEKKLLEDRVGEM-TSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ 1073
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIeKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEI 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1074 IAELQAQIDelkiqlAKKEEELQAVLARGDEE---VAQKNNalkqlrelqaqlaelqedlESEKAARNKAEKLKRDLSEE 1150
Cdd:TIGR01612 1263 ENEMGIEMD------IKAEMETFNISHDDDKDhhiISKKHD-------------------ENISDIREKSLKIIEDFSEE 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1151 --LEALKTELEDTLDTTAAQQELRSKREQEVAELK--------KAIDDETRNHESQIQEMRQRHGTALEEiSEQLEQAKR 1220
Cdd:TIGR01612 1318 sdINDIKKELQKNLLDAQKHNSDINLYLNEIANIYnilklnkiKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLIKKIK 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1221 VKGNLEKNKQTLES--DNKELTNEVKSLQQAKSEsehkrkkleaqlqevmarfsegekvkgeladrthkIQTELDNVSCL 1298
Cdd:TIGR01612 1397 DDINLEECKSKIEStlDDKDIDECIKKIKELKNH-----------------------------------ILSEESNIDTY 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1299 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN-LSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQlatlqaqlv 1377
Cdd:TIGR01612 1442 FKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNdHDFNINELKEHIDKSKGCKDEADKNAKAIEKN--------- 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1378 etkkkleddvgaleglEEVKRKLQKDMEVTSQKLEEKAIAfDKLEKTKNRLQQELDDLMvdlDHQRQIVSNLEKKQKKFD 1457
Cdd:TIGR01612 1513 ----------------KELFEQYKKDVTELLNKYSALAIK-NKFAKTKKDSEIIIKEIK---DAHKKFILEAEKSEQKIK 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1458 QMLAEEKTISARYAEERDRAEA------EAREKDTKALSMARALDEALEAKEEFERLNKQLRA----EMEDLISSKDDVG 1527
Cdd:TIGR01612 1573 EIKKEKFRIEDDAAKNDKSNKAaidiqlSLENFENKFLKISDIKKKINDCLKETESIEKKISSfsidSQDTELKENGDNL 1652
|
650 660 670
....*....|....*....|....*....|....*
gi 528481573 1528 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1562
Cdd:TIGR01612 1653 NSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1473-1915 |
2.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1473 ERDRAEAEAREKDTKALsmARALDEALEAKEEFERLNKQLRAEMEDLisskdDVGKNVHELEKSKRTLEQQVEEMRTQLE 1552
Cdd:COG4717 77 EEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1553 ELEDELQATEDaklrLEVNMQAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDV 1632
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1633 EAQIEA-ANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEK--------------KLKSLEAEILQLQE 1697
Cdd:COG4717 226 EEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1698 DLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELA 1777
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1778 GERSAAQKSEnARQQLERQNKDLKSKLQELEGSVKSKFKA-SIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKe 1856
Cdd:COG4717 386 ELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELE- 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1857 vfmQVEDERRHADQYKEQmekansrmKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1915
Cdd:COG4717 464 ---QLEEDGELAELLQEL--------EELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1390-1887 |
2.87e-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: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1390 LEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK-KQKKFD--QMLAEEKTI 1466
Cdd:pfam07111 75 LRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEgSQRELEeiQRLHQEQLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1467 SARYAEERDRA----EAEAREKDTKALSMARA--LDEALEAKEEFERLNKQLRAEMEDLISS------------------ 1522
Cdd:pfam07111 155 SLTQAHEEALSsltsKAEGLEKSLNSLETKRAgeAKQLAEAQKEAELLRKQLSKTQEELEAQvtlveslrkyvgeqvppe 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1523 ---------KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEK 1593
Cdd:pfam07111 235 vhsqtweleRQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREK 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1594 KRALVKQVREMEAELEDERKQRALAVAAKKK-----------LEMDLKDVEAQIEA--------------ANKAR----- 1643
Cdd:pfam07111 315 VFALMVQLKAQDLEHRDSVKQLRGQVAELQEqvtsqsqeqaiLQRALQDKAAEVEVermsakglqmelsrAQEARrrqqq 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1644 --DEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKL----------KSLEAEILQLQEDLASSERARRHAEQ 1711
Cdd:pfam07111 395 qtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQESCPPPPPAPP 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1712 ERDELADEISNSASGKAALlDEKRRLEARIAQLEEELEEEQSNMELLndRFRKTTMQVDT---------------LNTEL 1776
Cdd:pfam07111 475 VDADLSLELEQLREERNRL-DAELQLSAHLIQQEVGRAREQGEAERQ--QLSEVAQQLEQelqraqeslasvgqqLEVAR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1777 AGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqlEEQLEQEAKERAAANKIVRRT--EKKL 1854
Cdd:pfam07111 552 QGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRL---NEARREQAKAVVSLRQIQHRAtqEKER 628
|
570 580 590
....*....|....*....|....*....|...
gi 528481573 1855 KEVFMQVEDERRhadqyKEQMEKANSRMKQLKR 1887
Cdd:pfam07111 629 NQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1474-1739 |
2.94e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1474 RDRAEAEAREKDTKALSMARALDEA---LEAKEEFERLNKQLRAEMEdlISSKDDVGKnvhELEKSKRTLEQQVEEMRTQ 1550
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEAldkLRSYLPKLNPLREEKKKVS--VKSLEELIK---DVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1551 LEELEDELQATEDAKLRLEVnmqaMKAqFDRDLQARDEQ----------NEEKKRALVKQVREMEAELEDERKQRALAVA 1620
Cdd:PRK05771 109 ISELENEIKELEQEIERLEP----WGN-FDLDLSLLLGFkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1621 AKKKlemdlkdveaqieaanKARDEAIKQLRKLqaqmkDYQR-ELEEARTSRDEIftqsKENEKKLKSLEAEILQLQEDL 1699
Cdd:PRK05771 184 VVLK----------------ELSDEVEEELKKL-----GFERlELEEEGTPSELI----REIKEELEEIEKERESLLEEL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 528481573 1700 ASSerarrhaeqeRDELADEISNSasgKAALLDEKRRLEA 1739
Cdd:PRK05771 239 KEL----------AKKYLEELLAL---YEYLEIELERAEA 265
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1643-1808 |
3.05e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1643 RDEAIKQLRKLQAQMKDyQRELEEARTSrdeiftqskenekklkSLEAEILQLQEDLASSERARRHAEQERDELADEISn 1722
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGAGA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1723 SASGKAALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS 1802
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKIADLGR 179
|
170
....*....|....
gi 528481573 1803 KL--------QELE 1808
Cdd:PRK09039 180 RLnvalaqrvQELN 193
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
865-1886 |
3.06e-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: 49.28 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 865 IKVKERQVKVENELVEMERKHQQLLEEKNILAEQLqAETELFAEAEEMRAR---LVAKKQELEEILHD--------LESR 933
Cdd:TIGR01612 605 LKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDEL-AKISPYQVPEHLKNKdkiYSTIKSELSKIYEDdidalyneLSSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 934 VEEEEERNQSLQNEKKKMQSHIQDLEeqldeeeaarqklqlekvtaeAKIKKMEEDILLLEDQNSKFLKEKklLEDRVGE 1013
Cdd:TIGR01612 684 VKENAIDNTEDKAKLDDLKSKIDKEY---------------------DKIQNMETATVELHLSNIENKKNE--LLDIIVE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1014 MTSQLAEE--EEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAelqaqIDELKIQLAK- 1090
Cdd:TIGR01612 741 IKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKYKSKISEIKNHYNDQIN-----IDNIKDEDAKq 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1091 ---KEEELQAVLARGDEEVAQKNNALKQLRElqAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDtldttaa 1167
Cdd:TIGR01612 812 nydKSKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD------- 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1168 qqELRSKREQEVAELKKAIDDETRNHESQIQEMrqrhgTALEEISEQLEQAKRVKGNLEK--NKQTL--ESDNKEL---- 1239
Cdd:TIGR01612 883 --DKLNDYEKKFNDSKSLINEINKSIEEEYQNI-----NTLKKVDEYIKICENTKESIEKfhNKQNIlkEILNKNIdtik 955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1240 -TNEVK---------SLQQAKSESEHKRKKL-----EAQLQEVMARFSEGEKVKGElaDRTHKIQTELDNVSCLLEDAEK 1304
Cdd:TIGR01612 956 eSNLIEksykdkfdnTLIDKINELDKAFKDAslndyEAKNNELIKYFNDLKANLGK--NKENMLYHQFDEKEKATNDIEQ 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1305 KGIKLTKDVSS---------------LESQLQDTQELLQEETRQKLNLS----SRIRQ----------LEEEKNNLLEQQ 1355
Cdd:TIGR01612 1034 KIEDANKNIPNieiaihtsiyniideIEKEIGKNIELLNKEILEEAEINitnfNEIKEklkhynfddfGKEENIKYADEI 1113
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1356 EEEEESRKNLEKQLATLQAQLVETKKKLEDDVgaleglEEVKRKLQKDMEVTsqkleEKAIAFDKLEKTKNRLQqeldDL 1435
Cdd:TIGR01612 1114 NKIKDDIKNLDQKIDHHIKALEEIKKKSENYI------DEIKAQINDLEDVA-----DKAISNDDPEEIEKKIE----NI 1178
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1436 MVDLDHQRQIVSNLEK------KQKKFDQMLAEEKTISARYAE-------ERDRAEAEAREKDTKAL-SMARALDEALEA 1501
Cdd:TIGR01612 1179 VTKIDKKKNIYDEIKKllneiaEIEKDKTSLEEVKGINLSYGKnlgklflEKIDEEKKKSEHMIKAMeAYIEDLDEIKEK 1258
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1502 KEEFER---LNKQLRAEMEDLISSKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNM-QAMKA 1577
Cdd:TIGR01612 1259 SPEIENemgIEMDIKAEMETFNISHDDD-KDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLlDAQKH 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1578 QFDRDLQARDEQN------EEKKRALVKQVREMEAELEDERKQ------RALAVAAKKKLEMDLKDVEAQIEAA--NKAR 1643
Cdd:TIGR01612 1338 NSDINLYLNEIANiynilkLNKIKKIIDEVKEYTKEIEENNKNikdeldKSEKLIKKIKDDINLEECKSKIESTldDKDI 1417
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1644 DEAIKQLRKLQAQMkdyqreLEEaRTSRDEIFTQSKENEKKL----KSLE------AEILQLQEDLASSERARRHAE-QE 1712
Cdd:TIGR01612 1418 DECIKKIKELKNHI------LSE-ESNIDTYFKNADENNENVlllfKNIEmadnksQHILKIKKDNATNDHDFNINElKE 1490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1713 RDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN--DRFRKTTMQVD----------TLNTELAGER 1780
Cdd:TIGR01612 1491 HIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNkfAKTKKDSEIIIkeikdahkkfILEAEKSEQK 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1781 SAAQKSENARQQLERQNKDLKSK----LQELEGSVKSKFkASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKK--- 1853
Cdd:TIGR01612 1571 IKEIKKEKFRIEDDAAKNDKSNKaaidIQLSLENFENKF-LKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKeng 1649
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 528481573 1854 -----LKEVFMQVEDERRHADQYKEQMEKANSRMKQLK 1886
Cdd:TIGR01612 1650 dnlnsLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
854-1222 |
3.18e-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: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 854 EEEMQAKDEELIKVKERQV----KVENELVEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRAR--------LVAKKQ 921
Cdd:pfam09731 51 LGEDPPLAPKPKTFRPLQPsvvsAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE--KEATKDAAEakaqlpksEQEKEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 922 ELEEILHDLESRVEEEEERNQSLQNEKKK-MQSHIQDLEEQLDEEEAARQK-LQLEKVTAEAKIKKMEEDILLLEDQNSK 999
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQaVKAHTDSLKEASDTAEISREKaTDSALQKAEALAEKLKEVINLAKQSEEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1000 FLKEKKLLEDRVGEMTS----QLAEEEEKAKNLGKVKNKqemmMVDLEErlKKEEKTRQELEK--------AKRKLDAET 1067
Cdd:pfam09731 209 AAPPLLDAAPETPPKLPehldNVEEKVEKAQSLAKLVDQ----YKELVA--SERIVFQQELVSifpdiipvLKEDNLLSN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1068 TDLQDQIAELQAQIDELKIQLA--KKEEELQAVLARGDEEVAQKNNALKQLRELQAQLA--ELQEDLESEKAARNKAEKL 1143
Cdd:pfam09731 283 DDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRESY 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1144 KRDLSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNHESQIQEMRQRHG---TALEEISEQLEQAKR 1220
Cdd:pfam09731 363 EEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANLKgleKATSSHSEVEDENRK 441
|
..
gi 528481573 1221 VK 1222
Cdd:pfam09731 442 AQ 443
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
977-1181 |
3.42e-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: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 977 VTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvKNKQEMMMVDLEERLKKEEKTRQEL 1056
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL---QAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1057 EKAKRK--------------LDAETTD-----------LQDQIAELQAQIDELKIQLAKKEEELQAVLArgdEEVAQKNN 1111
Cdd:COG3883 89 GERARAlyrsggsvsyldvlLGSESFSdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLA---ELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1112 ALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1181
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
848-1079 |
3.65e-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: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 848 LQVTRQE------EEMQAKDEELIKVKERQVKVENELVEMERkhqqlleeknILAEQLQAETELFAEAEEMRARlvakkq 921
Cdd:pfam17380 383 LQMERQQknervrQELEAARKVKILEEERQRKIQQQKVEMEQ----------IRAEQEEARQREVRRLEEERAR------ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 922 ELEEI-LHDLESRVEEEEERNQSLQNEKKKMQshIQDLEEQLDEEEAARQKLqLEKVTAEAKIKKMEEDillledqnskf 1000
Cdd:pfam17380 447 EMERVrLEEQERQQQVERLRQQEEERKRKKLE--LEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEE----------- 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1001 lKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEM---MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAEL 1077
Cdd:pfam17380 513 -RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeerRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
..
gi 528481573 1078 QA 1079
Cdd:pfam17380 592 EA 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1395-1646 |
3.91e-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: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1395 EVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEktisaryaeER 1474
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---------EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1475 DRAEAEAREKDTKALsMARALDEAleakeefERLNKQLRAEMedLISSKDdvgknVHELEKSKRTLEQQVEEMRTQLEEL 1554
Cdd:COG4942 91 EIAELRAELEAQKEE-LAELLRAL-------YRLGRQPPLAL--LLSPED-----FLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1555 E---DELQATEdaklrlevnmQAMKAQFDRDLQARDEQNEEKKR--ALVKQVREMEAELEDERKQRALAVAAKKKLEMDL 1629
Cdd:COG4942 156 RadlAELAALR----------AELEAERAELEALLAELEEERAAleALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*..
gi 528481573 1630 KDVEAQIEAANKARDEA 1646
Cdd:COG4942 226 EALIARLEAEAAAAAER 242
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
852-1272 |
4.19e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 852 RQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQL------LEEKNILAEQLQAETE-LFAEAEEMRARLVAKKQELE 924
Cdd:PRK01156 329 KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYnsylksIESLKKKIEEYSKNIErMSAFISEILKIQEIDPDAIK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 925 EILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDillledqnskFLKEK 1004
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINH----------YNEKK 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1005 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVD-LEERLKKEEKTRQELEKAKRKLdAETTDLQDQIAELQAQIDE 1083
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKS 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1084 LKIQL--AKKEEELQAVLARGDEEV----AQKNNALKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALKTE 1157
Cdd:PRK01156 558 LKLEDldSKRTSWLNALAVISLIDIetnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSY---IDKSIREIENEANNLNNK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1158 LEDTLDTTAAQQELRSKRE---QEVAElKKAIDDETRNHESQIQEMRQRhgtaLEEISEQLEQAKRVKGNLEKNKQTLES 1234
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDnykKQIAE-IDSIIPDLKEITSRINDIEDN----LKKSRKALDDAKANRARLESTIEILRT 709
|
410 420 430
....*....|....*....|....*....|....*...
gi 528481573 1235 DNKELTNEVKSLQQaKSESEHKRKKLEAQLQEVMARFS 1272
Cdd:PRK01156 710 RINELSDRINDINE-TLESMKKIKKAIGDLKRLREAFD 746
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1187-1417 |
4.29e-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: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1187 DDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQE 1266
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1267 VmarFSEGEKVK-----------GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEetrqkl 1335
Cdd:COG3883 95 L---YRSGGSVSyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1336 nLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKA 1415
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
..
gi 528481573 1416 IA 1417
Cdd:COG3883 245 SA 246
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
983-1210 |
4.78e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 983 IKKMEEDILLLE-------DQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMvDLEERLKKEEKTRQE 1055
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILE-EQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1056 LEKA-KRKLDAETTDLQDQIAELQAQIDELKIQLA--KKEEELQAVLargdeevaQKNNAL--KQLRELQAQLAELQEDL 1130
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIevAETEERVFKL--------EKERSLldASLRELESKFIVAQEDV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1131 esekaarNKAEKLKRD-LSEELEalktELEDTLDTTAAQ-----------QELRSKREQEVAELKKAiddETRNHESQIQ 1198
Cdd:PLN02939 288 -------SKLSPLQYDcWWEKVE----NLQDLLDRATNQvekaalvldqnQDLRDKVDKLEASLKEA---NVSKFSSYKV 353
|
250
....*....|..
gi 528481573 1199 EMRQRHGTALEE 1210
Cdd:PLN02939 354 ELLQQKLKLLEE 365
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1299-1504 |
6.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1299 LEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVE 1378
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------------DKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1379 TKKKLEDDVGAL----------------EGLEEVKRK---LQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDL 1439
Cdd:COG3883 84 RREELGERARALyrsggsvsyldvllgsESFSDFLDRlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1440 DHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEE 1504
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
982-1296 |
6.30e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 982 KIKKMEEDILLLEDQNSK--FLKEKKLL----------EDRVGEMTSQLAE----EEEKAKNLGKVKNKQEMMMVD---- 1041
Cdd:PRK04778 80 SLPDIEEQLFEAEELNDKfrFRKAKHEIneieslldliEEDIEQILEELQEllesEEKNREEVEQLKDLYRELRKSllan 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1042 ----------LEERLKKEEKTRQELEKAK------------RKLDAETTDLQDQIA-----------ELQAQIDELKIQL 1088
Cdd:PRK04778 160 rfsfgpaldeLEKQLENLEEEFSQFVELTesgdyveareilDQLEEELAALEQIMEeipellkelqtELPDQLQELKAGY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1089 AKKEEE--------LQAVLARGDEEVAQKNNALKQLR--ELQAQLAELQED-------LESEKAARNKAEKLKRDLSEEL 1151
Cdd:PRK04778 240 RELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDldEAEEKNEEIQERidqlydiLEREVKARKYVEKNSDTLPDFL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1152 EALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---IDDETRNHE---SQIQEMrqrhgtaLEEISEQL 1215
Cdd:PRK04778 320 EHAKEQNKELKEEIDrvkqsytlNESELESVRqlEKQLESLEKQydeITERIAEQEiaySELQEE-------LEEILKQL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1216 EQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKL----------------EAQLQEVMARFSEG----E 1275
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSnlpglpedylemffevSDEIEALAEELEEKpinmE 472
|
410 420
....*....|....*....|.
gi 528481573 1276 KVKGELadrtHKIQTELDNVS 1296
Cdd:PRK04778 473 AVNRLL----EEATEDVETLE 489
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1080-1248 |
7.14e-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: 46.93 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1080 QIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELqaqLAELQEDLESEKAARNKAEKLKrdlSEELEALKTELE 1159
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDR---KDALEEELRQLKQLEDELEDCD---PTELDRAKEKLK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1160 DTLDTTAAQQELRSKREQEVAELKKAIDDETrnhesqiqemrqrhgtalEEISEQLEQAKRVKGNLEKNKQTLESDNKEL 1239
Cdd:smart00787 215 KLLQEIMIKVKKLEELEEELQELESKIEDLT------------------NKKSELNTEIAEAEKKLEQCRGFTFKEIEKL 276
|
....*....
gi 528481573 1240 TNEVKSLQQ 1248
Cdd:smart00787 277 KEQLKLLQS 285
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1442-1933 |
8.16e-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: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1442 QRQIVSNLEKKQKkFDQMLAEEKTISAryaEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIS 1521
Cdd:TIGR00618 165 KKELLMNLFPLDQ-YTQLALMEFAKKK---SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1522 SKDDVgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrDLQARDEQNEEKKRALVKQV 1601
Cdd:TIGR00618 241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA---AHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1602 REMEAELEDERKQRALAVAAKKKLEmdlkdveaqieaankardEAIKQLRKLQAQMKDYQRELEEArTSRDEIFTQSKEN 1681
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIE------------------EQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1682 EKKLKSLEA--EILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLN 1759
Cdd:TIGR00618 378 TQHIHTLQQqkTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1760 DRFRKTTMQvdtlntELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSvKSKFKASIAALEAKILQLEEQLEQEAKE 1839
Cdd:TIGR00618 458 KIHLQESAQ------SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1840 RAAANKiVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQleeaeeeATRANASRRKLQRELDDATEASEG 1919
Cdd:TIGR00618 531 QRGEQT-YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNLQNITVRLQDLTEK 602
|
490
....*....|....
gi 528481573 1920 LSREVNTLKNRLRR 1933
Cdd:TIGR00618 603 LSEAEDMLACEQHA 616
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1108-1411 |
8.29e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1108 QKNNALKQLRELQA-QLAELQEDLESEKAarNKAEKLKRDLSEELEALKTELEdtldttAAQQELRSKREQEVAELKKAI 1186
Cdd:PRK05771 17 YKDEVLEALHELGVvHIEDLKEELSNERL--RKLRSLLTKLSEALDKLRSYLP------KLNPLREEKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1187 DDetrnhesqiqemrqrhgtaLEEISEQLEqaKRVKGnleknkqtLESDNKELTNEVKSLQQAKSESEhkrkKLEAqLQE 1266
Cdd:PRK05771 89 KD-------------------VEEELEKIE--KEIKE--------LEEEISELENEIKELEQEIERLE----PWGN-FDL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1267 VMARFSEGEKVKGELAdRTHKIQTE----LDNVSCLLEDAEKKG------IKLTKDVSSLESQLQDTqELLQEETRQKLN 1336
Cdd:PRK05771 135 DLSLLLGFKYVSVFVG-TVPEDKLEelklESDVENVEYISTDKGyvyvvvVVLKELSDEVEEELKKL-GFERLELEEEGT 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1337 LSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEGL--EEVKRKLQKDMEVTSQKL 1411
Cdd:PRK05771 213 PSELIREIKEEL--------------EEIEKERESLLEELKELAKKYLEELLALYEYleIELERAEALSKFLKTDKT 275
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1113-1457 |
8.32e-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: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1113 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTaaQQELRSKREQEVAELKKAIDDETRN 1192
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1193 HESQIQEMRQRHGtalEEISEQLEQAKRVKgNLEKNKQtlesdnKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARfs 1272
Cdd:pfam17380 379 ELERLQMERQQKN---ERVRQELEAARKVK-ILEEERQ------RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1273 EGEKVKGELADRTHKIQTELDnvscllEDAEKKGIKLTKDvsslesqlqdtqellQEETRQKLnlssrirqLEEEKnnll 1352
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQ------QEEERKRKKLELE---------------KEKRDRKR--------AEEQR---- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1353 eqqeeeeesRKNLEKQLATLQAQLVETKKK-------LEDDVGALegLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTK 1425
Cdd:pfam17380 494 ---------RKILEKELEERKQAMIEEERKrkllekeMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKAT 562
|
330 340 350
....*....|....*....|....*....|..
gi 528481573 1426 NRlQQELDDLMVDLDHQRQIVSNlEKKQKKFD 1457
Cdd:pfam17380 563 EE-RSRLEAMEREREMMRQIVES-EKARAEYE 592
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1143-1273 |
8.50e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1143 LKRDLSEELEALKTELEDTLDttAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRqrhgtalEEISEQLEQAKRVK 1222
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR-------NELQKLEKRLLQKE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 528481573 1223 GNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE 1273
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1039-1135 |
8.98e-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: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1039 MVDLEERLKKEEKTRQELEKAKRKLDAET-TDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNnalkQLR 1117
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG----KIP 488
|
90
....*....|....*...
gi 528481573 1118 ELQAQLAELQEDLESEKA 1135
Cdd:COG0542 489 ELEKELAELEEELAELAP 506
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1075-1329 |
9.18e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1075 AELQAQIDELKiqlakKEEELQAvlargDEEVAQKNnaLKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1154
Cdd:PRK11281 39 ADVQAQLDALN-----KQKLLEA-----EDKLVQQD--LEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1155 KTELEDTLDTTAAQQELRSkREQEVAELkkaiddetrnhESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLEs 1234
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQ-LESRLAQT-----------LDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1235 dnkELTNEVKSLQQAKSESEHKRK-KLEAQLQEVMARFSEGekvkgeladrthkiQTELDNVSCLLEDAEKKGIKLTKDV 1313
Cdd:PRK11281 174 ---QIRNLLKGGKVGGKALRPSQRvLLQAEQALLNAQNDLQ--------------RKSLEGNTQLQDLLQKQRDYLTARI 236
|
250
....*....|....*.
gi 528481573 1314 SSLESQLQDTQELLQE 1329
Cdd:PRK11281 237 QRLEHQLQLLQEAINS 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1488-1729 |
9.44e-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: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1488 ALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtleQQVEEMRTQLEELEDELQATEDAKLR 1567
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----EEYNELQAELEALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1568 LEVNMQAMKAQFDRdlQARDEQNEEKKRALVKQVreMEAELEDERKQRALAV-----AAKKKLEmDLKDVEAQIEAANKA 1642
Cdd:COG3883 77 AEAEIEERREELGE--RARALYRSGGSVSYLDVL--LGSESFSDFLDRLSALskiadADADLLE-ELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1643 RDEAIKQLRKLQAQMKDYQRELEeartsrdeifTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISN 1722
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELE----------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
....*..
gi 528481573 1723 SASGKAA 1729
Cdd:COG3883 222 AAAAAAA 228
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1472-1699 |
9.84e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1472 EERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQL 1551
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1552 EELEDELQATEDAKLRLEvNMQAMKAQFDRDLQARDeQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEmDLKD 1631
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRA-ELKE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1632 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDL 1699
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1588-1711 |
1.06e-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: 45.44 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1588 EQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIE------------AANKARDEAIKQLRKLQA 1655
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKkleekaqaaltkGNEELAREALAEKKSLEK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1656 QMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEilqlQEDLASSERARRHAEQ 1711
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK----KNLLKARLKAAKAQEA 149
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1070-1717 |
1.18e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1070 LQDQIAELQAQIDELKIQLAKKEEELQAVLargdeevaqknNALKQLRElqaqlAELQEDLESEKAARNKAEKLK---RD 1146
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSM-----------NSIKTFWS-----PELKKERALRKEEAARISVLKeqyRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1147 LSEELEALKTELEDTLDTTAAQQELRSKREQEV------AELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQakr 1220
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFttspvdGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1221 VKGNLEKNKQTLESDNKELTN-----EVKSLQQAKSESEHKRKK----LEAQLQEVMARFSEGEKVKGELADRTHK---I 1288
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKllemlQSKGLPKKSGEEDWERTRriaeAEMQLGHLEVLLDQKEKENIHLREELHRrnqL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1289 QTELDNVSCLLEDAEKKGIKltkdVSSLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKN-----NLLEQQEEEE 1359
Cdd:pfam10174 222 QPDPAKTKALQTVIEMKDTK----ISSLERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKShskfmKNKIDQLKQE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1360 ESRKN-----LEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDD 1434
Cdd:pfam10174 298 LSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKST 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1435 LMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMArALDEALEAKEE-FERLN 1509
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1510 KQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ------ATEDAKLR-LEVNMQAMKAQFDR- 1581
Cdd:pfam10174 457 EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSKl 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1582 DLQARDEQNEE----KKRALVKQVREMEAELEDERKQRALAVA-------AKKKLEMDLKDVEAQIEAANKARDEAIKQL 1650
Cdd:pfam10174 537 ENQLKKAHNAEeavrTNPEINDRIRLLEQEVARYKEESGKAQAeverllgILREVENEKNDKDKKIAELESLTLRQMKEQ 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1651 RKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKlkslEAEILQLQEDLASSERARRHAEQERDELA 1717
Cdd:pfam10174 617 NKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD----NSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
981-1261 |
1.34e-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: 47.07 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 981 AKIKKMEEDILLLEDqnskFLKEKKLLEDRVGEMTSQLAEEEEKAkNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKak 1060
Cdd:pfam18971 567 AKGLSLQEANKLIKD----FLSSNKELAGKALNFNKAVAEAKSTG-NYDEVKKAQK----DLEKSLRKREHLEKEVEK-- 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1061 rKLDAETTDLQDQIAELQA--QIDELkIQLAKKEEElqavlaRGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARN 1138
Cdd:pfam18971 636 -KLESKSGNKNKMEAKAQAnsQKDEI-FALINKEAN------RDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFD 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1139 KAEKLK-RDLS---EELEALKTELED----------TLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIqeMRQRH 1204
Cdd:pfam18971 708 EFKNGKnKDFSkaeETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVI--INQKV 785
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1205 GTALEEISEQLEQAKRVkGNLEKNKQTLeSDNKELTNEVKSLQQAKSESEHKRKKLE 1261
Cdd:pfam18971 786 TDKVDNLNQAVSVAKAM-GDFSRVEQVL-ADLKNFSKEQLAQQAQKNEDFNTGKNSE 840
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1630-1826 |
1.44e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1630 KDVEAQIEAANKARDeaikqlrkLQAQMKDYQRELEEARTSRDEIFTQSKENE---KKLKSLEAEILQLQEDLASSERAr 1706
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETEqlkQQLAQAPAKLRQAQAELEALKDD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1707 rhaeqerdelADEISNSASGKAALldekRRLEARIAQLEEELEEEQSNMELLNDrfrkttmQVDTLNTelAGERSAAQKS 1786
Cdd:PRK11281 110 ----------NDEETRETLSTLSL----RQLESRLAQTLDQLQNAQNDLAEYNS-------QLVSLQT--QPERAQAALY 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 528481573 1787 ENAR--QQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKI 1826
Cdd:PRK11281 167 ANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQN 208
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1468-1787 |
1.46e-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: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1468 ARYAEERDRaEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEM 1547
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1548 RTQLEELEDELQATEDAKLRLEVNMQAMKaqfdrdlqardeqneEKKRALVKQVREMEAElederkqralavaaKKKLEM 1627
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAE--------------RKQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1628 DLKDVEAQIEAANKardeAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERArr 1707
Cdd:pfam07888 179 KLQQTEEELRSLSK----EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERK-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1708 hAEQERDELADEISNSASGKAALldEKRRLEAR----------------IAQLEEELEEEQSNMELLNDRFRKTTMQVDT 1771
Cdd:pfam07888 253 -VEGLGEELSSMAAQRDRTQAEL--HQARLQAAqltlqladaslalregRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330
....*....|....*.
gi 528481573 1772 LNTELAGERSAAQKSE 1787
Cdd:pfam07888 330 LEERLQEERMEREKLE 345
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
999-1435 |
1.46e-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: 46.77 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 999 KFLKEKKLLEDRVGEMTSQ-LAEEEEKAKNLGkvknkqemMMVDLEERLKKEEKTRQELEkakrklDAETTDLQDQIAEL 1077
Cdd:pfam06160 7 KIYKEIDELEERKNELMNLpVQEELSKVKKLN--------LTGETQEKFEEWRKKWDDIV------TKSLPDIEELLFEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1078 QAQIDELKIQLAKKE-EELQAVLARGDEEVAQKNNALKQLrelqaqlaelqedLESEKAARNKAEKLK---RDLSEELEA 1153
Cdd:pfam06160 73 EELNDKYRFKKAKKAlDEIEELLDDIEEDIKQILEELDEL-------------LESEEKNREEVEELKdkyRELRKTLLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1154 LKTELEDTLDTTAAQ-QELRSKREQEVaELKKAID-DETRNHESQIQEMrqrhgtaLEEISEQLEqakRVKGNLEKNKQT 1231
Cdd:pfam06160 140 NRFSYGPAIDELEKQlAEIEEEFSQFE-ELTESGDyLEAREVLEKLEEE-------TDALEELME---DIPPLYEELKTE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1232 LESDNKELTNEVKSLQQAKSESEH-----KRKKLEAQLQEVMARFSEGE--KVKGELADrthkIQTELDNVSCLLE---D 1301
Cdd:pfam06160 209 LPDQLEELKEGYREMEEEGYALEHlnvdkEIQQLEEQLEENLALLENLEldEAEEALEE----IEERIDQLYDLLEkevD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1302 AEKKGIKLTKDVSSLESQLQDTQELLQEETRQkLNLSSRIRQLEEEKNnlleqqeeeeesrKNLEKQLATLQAQLVETKK 1381
Cdd:pfam06160 285 AKKYVEKNLPEIEDYLEHAEEQNKELKEELER-VQQSYTLNENELERV-------------RGLEKQLEELEKRYDEIVE 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 528481573 1382 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDL 1435
Cdd:pfam06160 351 RLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEF 404
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1409-1933 |
1.61e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1409 QKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM---LAEEKTISARYAEERDRAEAEAREKD 1485
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1486 TKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR-----------------TLEQQVEEMR 1548
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1549 TQLEELEDELQATEDAKLRLEVnMQAMKAQFDRDLQARDEQN---------EEKKRALVKQVREMEAELEDERKQR---- 1615
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNnqilelegyEMDYNSYLKSIESLKKKIEEYSKNIerms 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1616 ALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQS----------------- 1678
Cdd:PRK01156 391 AFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhi 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1679 -KENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMEL 1757
Cdd:PRK01156 471 iNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1758 LNDRFRKTTMQ-VDTLNTELAgeRSAAQKS----ENARQQLERQNK---DLKSKLQELEGS---VKSKFKASIAALEAKI 1826
Cdd:PRK01156 551 IKNRYKSLKLEdLDSKRTSWL--NALAVISlidiETNRSRSNEIKKqlnDLESRLQEIEIGfpdDKSYIDKSIREIENEA 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1827 LQLEEQLEQEAKERAAANKIvRRTEKKLKEVFMQVEDERRHADQYKEQMEKANSRMKQLKRQLEeaeeeatRANASRRKL 1906
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKL-RGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-------DAKANRARL 700
|
570 580
....*....|....*....|....*..
gi 528481573 1907 QRELDDATEASEGLSREVNTLKNRLRR 1933
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLES 727
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1632-1886 |
1.78e-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: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1632 VEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFT--QSKENEKKLKSLEAEILQLQEDLASSERARRHA 1709
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1710 EQERDELADEISNSASGKAAlldekRRLEARIAQleeeleeeqsnmellndrfrkttmqvdtLNTELAGERSAAQKSENA 1789
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVI-----QQLRAQLAE----------------------------LEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1790 RQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKIlqleeqleqeakerAAANKIVRRTEKKLKEvFMQVEDE----R 1865
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQARE--------------ASLQAQLAQLEARLAE-LPELEAElrrlE 357
|
250 260
....*....|....*....|.
gi 528481573 1866 RHADQYKEQMEKANSRMKQLK 1886
Cdd:COG3206 358 REVEVARELYESLLQRLEEAR 378
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
917-1099 |
2.03e-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: 44.92 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 917 VAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQ 996
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 997 NSKFLKEKklledrvgEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAE 1076
Cdd:COG1579 82 LGNVRNNK--------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|...
gi 528481573 1077 LQAQIDELKIQLAKKEEELQAVL 1099
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPEL 176
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1402-1646 |
2.11e-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: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1402 KDMEVTSQKLEEKAIAfdklEKTKNRLQQELDDLmvdLDHqrqiVSNLEKKQKKFDQmLAEEKTISAryaeERDRAEAEA 1481
Cdd:NF012221 1552 KQDDAAQNALADKERA----EADRQRLEQEKQQQ---LAA----ISGSQSQLESTDQ-NALETNGQA----QRDAILEES 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1482 REKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLIssKDDVGKnvhELEKSKRTLEQQVEEMRTQLE----ELEDE 1557
Cdd:NF012221 1616 RAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQE---QLDDAKKISGKQLADAKQRHVdnqqKVKDA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1558 LQATEDAKLRLEVNMQAMKAQFDrdlQARDEQNEEKKRALVKQVREMEAElederkQRALAVAAKKKLEMDlKDVEAQIE 1637
Cdd:NF012221 1691 VAKSEAGVAQGEQNQANAEQDID---DAKADAEKRKDDALAKQNEAQQAE------SDANAAANDAQSRGE-QDASAAEN 1760
|
....*....
gi 528481573 1638 AANKARDEA 1646
Cdd:NF012221 1761 KANQAQADA 1769
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1580-1703 |
2.18e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1580 DRDLQARDEQNEEKKRALVKQVREMEAELEDE---RKQRALAVAAKKKLEMDLKDVEAQIEAANK------ARDEAIKQL 1650
Cdd:COG1566 78 PTDLQAALAQAEAQLAAAEAQLARLEAELGAEaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgavsqqELDEARAAL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 528481573 1651 RKLQAQMKDYQRELEEARTSRDEIfTQSKENEKKLKSLEAEILQLQEDLASSE 1703
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLREE-EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1490-1843 |
2.29e-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: 45.83 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1490 SMARALDEALEAKEEFERLNKQLRAEMEDLISSKddvgKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLe 1569
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELPQAK----SRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1570 vnmQAMKAQFDRDLQARDEQNEEKK---RALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEA 1646
Cdd:pfam19220 89 ---VARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1647 IKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASS----ERARRHAEQERDELADEISN 1722
Cdd:pfam19220 166 RERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEqaerERAEAQLEEAVEAHRAERAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1723 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQ------ 1796
Cdd:pfam19220 246 LRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraelee 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1797 -----NKDLKSKLQELEGSVKS-------------KFKASIAALEAKILQLEEQLEQEAKERAAA 1843
Cdd:pfam19220 326 raemlTKALAAKDAALERAEERiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1063-1217 |
2.30e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1063 LDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEK 1142
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDL----QDSVANLRASLSAAEAERSRLQALLAELA---GAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1143 LKRDLSEELEALKTELEDTLDTTAA-QQELRSKREQeVAELKKAIDD-ETRNHESQ--IQEMRQRHGTALEEISEQLEQ 1217
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELlNQQIAALRRQ-LAALEAALDAsEKRDRESQakIADLGRRLNVALAQRVQELNR 194
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1361-1569 |
2.39e-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: 45.98 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1361 SRKNLEKQLATLQAQ------LVETKKKLEDDVgalEGLEEVKRK--LQK-DMEVTSQKLEEKaiafdkLEKTKNRLQQE 1431
Cdd:pfam15066 340 SNLYLEKKVKELQMKitkqqvFVDIINKLKENV---EELIEDKYNviLEKnDINKTLQNLQEI------LANTQKHLQES 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1432 lddlmvdldhqrqivsnleKKQKKFDQMlaEEKTISARYAEERDRAEAEAREKDtKALSMARALDEALEAKE-EFERLnK 1510
Cdd:pfam15066 411 -------------------RKEKETLQL--ELKKIKVNYVHLQERYITEMQQKN-KSVSQCLEMDKTLSKKEeEVERL-Q 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1511 QLRAEMEDLISSKDDVgknvheLEKSKRTLEQQVEEMRTQLEELEDE-LQATEDAKLRLE 1569
Cdd:pfam15066 468 QLKGELEKATTSALDL------LKREKETREQEFLSLQEEFQKHEKEnLEERQKLKSRLE 521
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1622-1803 |
2.62e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1622 KKKLEMDLKDVEAqieAANKARDEAIKQL---------RKLQAQ-MKDYQRELEE----ARTSRDEIFTQSKE-----NE 1682
Cdd:PRK10929 25 EKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEprsvpPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1683 KKLKSLEAEILQLQEDLAssERARRhAEQERDElADEISNSASGKAALLDEKRRL----EARI-AQLEEELEEEQSNMEL 1757
Cdd:PRK10929 102 MSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLAQAQLTA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 528481573 1758 LNDRFRKTTMQVDTLntELagersaAQKSENARQQLERQNKDLKSK 1803
Cdd:PRK10929 178 LQAESAALKALVDEL--EL------AQLSANNRQELARLRSELAKK 215
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
849-1328 |
2.65e-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: 45.89 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 849 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETEL---FAEAEEMRARLVAKKQELEE 925
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 926 IlHDLESRVeeeeernQSLQNEKKKMQSHIQDLEEQLDEEEAARQKL-QLEKVTAEAKIKKMEEDILLLEDQNSKFLKEK 1004
Cdd:pfam05557 199 I-PELEKEL-------ERLREHNKHLNENIENKLLLKEEVEDLKRKLeREEKYREEAATLELEKEKLEQELQSWVKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1005 KLLEDRVGE-MTSQLAEEEEKAKNLGKVKNkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDE 1083
Cdd:pfam05557 271 TGLNLRSPEdLSRRIEQLQQREIVLKEENS-------SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRR 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1084 L--KIQLAKKEEE-LQAVLARGDEEVAQKN---NALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTE 1157
Cdd:pfam05557 344 LqrRVLLLTKERDgYRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1158 LedTLDTTAAQQELRSKREQEVAELKKAIDDetrnhesqIQEMRQRhgtaLEEISEQLEqakrvkgnLEKNKQTLESDNK 1237
Cdd:pfam05557 424 L--QALRQQESLADPSYSKEEVDSLRRKLET--------LELERQR----LREQKNELE--------MELERRCLQGDYD 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1238 ELTNEVKSLQQ-AKSESEHKRKKLEAQLQEVMARfsegekvkgeLADRTHKIQTELDNVSCL----LEDAEKKGIKLTKD 1312
Cdd:pfam05557 482 PKKTKVLHLSMnPAAEAYQQRKNQLEKLQAEIER----------LKRLLKKLEDDLEQVLRLpettSTMNFKEVLDLRKE 551
|
490
....*....|....*.
gi 528481573 1313 VSSLESQLQDTQELLQ 1328
Cdd:pfam05557 552 LESAELKNQRLKEVFQ 567
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1054-1282 |
2.80e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1054 QELEKAKRKLD------AETTDLQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQKNNALkQLRELQAQLAELQ 1127
Cdd:PRK11281 63 QDLEQTLALLDkidrqkEETEQLKQQLAQAPAKLRQAQ-------AELEALKDDNDEETRETLSTL-SLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1128 EDLESekaarnkaekLKRDLSE---ELEALKTELEDtldttaAQQEL--RSKREQEVAELKKAIDDETRNHESQIQEMRQ 1202
Cdd:PRK11281 135 DQLQN----------AQNDLAEynsQLVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1203 RHGTALEEISEQLEQakrvkgNLEKNKQTLESDNKELtnEVKSLQQAKSESE---------HKRKKL------EAQLQEV 1267
Cdd:PRK11281 199 AEQALLNAQNDLQRK------SLEGNTQLQDLLQKQR--DYLTARIQRLEHQlqllqeainSKRLTLsektvqEAQSQDE 270
|
250
....*....|....*
gi 528481573 1268 MARFSEGEKVKGELA 1282
Cdd:PRK11281 271 AARIQANPLVAQELE 285
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1062-1743 |
2.80e-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: 45.97 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1062 KLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNnalkQLRELQAQLAELQEDLESEKAARNKAE 1141
Cdd:pfam10174 175 KSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHL----REELHRRN----QLQPDPAKTKALQTVIEMKDTKISSLE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1142 KLKRDLSEELEALKTELEdtLDTTAAQQELRSkreqevAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEqakrv 1221
Cdd:pfam10174 247 RNIRDLEDEVQMLKTNGL--LHTEDREEEIKQ------MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLE----- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1222 kgnleknkqTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVkgeLADRTHKIQteldnvsclled 1301
Cdd:pfam10174 314 ---------TLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESF---LNKKTKQLQ------------ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1302 aekkgiKLTKDVSSLESQLQDTQELLQEETRqKLNLssrirqleeeknnlleqqeeeeesrknLEKQLATLQAQLVETKK 1381
Cdd:pfam10174 370 ------DLTEEKSTLAGEIRDLKDMLDVKER-KINV---------------------------LQKKIENLQEQLRDKDK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1382 KLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDlmvDLDHQRQIVSNLEKKQKKFDQMLA 1461
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELT 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1462 EEKTISARYAEERDRAEAEAREKDTKALSMARALDealEAKEEFERLNKQLraemedlisskddvgKNVHELEKSKRTLE 1541
Cdd:pfam10174 493 EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE---QKKEECSKLENQL---------------KKAHNAEEAVRTNP 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1542 QQVEemRTQLEELEDELQATEDAKLRLEVnmqamkaqfDRDLQA-RDEQNEekKRALVKQVREMEAELEDERKQRALAVA 1620
Cdd:pfam10174 555 EIND--RIRLLEQEVARYKEESGKAQAEV---------ERLLGIlREVENE--KNDKDKKIAELESLTLRQMKEQNKKVA 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1621 AKKKLEMDLK------DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEIL- 1693
Cdd:pfam10174 622 NIKHGQQEMKkkgaqlLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRk 701
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 528481573 1694 QLQEDLASSERARRHAEQERDELADEISNSASGK-------AALLDEKRRLEARIAQ 1743
Cdd:pfam10174 702 QLEEILEMKQEALLAAISEKDANIALLELSSSKKkktqeevMALKREKDRLVHQLKQ 758
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1553-1825 |
3.30e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1553 ELEDELQATEDAKLRLEvnmqAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAElederkqrALAVAAKKKLEMDLKDV 1632
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAAEARAAKDKDAVAA--------ALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1633 EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskENEKKlKSLEAEIlqlqedlassERAR-RHAEQ 1711
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAA------------ADPKK-AAVAAAI----------ARAKaKKAAQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1712 ErDELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKttmqvdtlnTELAGERSAAQKSENARQ 1791
Cdd:PRK05035 565 Q-AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA---------VAAAIARAKAKKAEQQAN 634
|
250 260 270
....*....|....*....|....*....|....
gi 528481573 1792 QLERQNKDLKsklqelegsvKSKFKASIAALEAK 1825
Cdd:PRK05035 635 AEPEEPVDPR----------KAAVAAAIARAKAR 658
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1460-1616 |
3.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1460 LAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED----LISSKDDVGKNVHELEK 1535
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1536 SKRTLEQQVEEMRTQLEELE------DELQATEDAKLRLEVNMQAMKAQfdrdLQARDEQNEEKKRALVKQVREMEAELE 1609
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEkkeeelEELIEEQLQELERISGLTAEEAK----EILLEKVEEEARHEAAVLIKEIEEEAK 183
|
....*..
gi 528481573 1610 DERKQRA 1616
Cdd:PRK12704 184 EEADKKA 190
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
916-1292 |
4.31e-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: 45.07 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 916 LVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQK----------LQLEKVTAEA---- 981
Cdd:pfam05622 5 AQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKylllqkqleqLQEENFRLETardd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 982 ---KIKKMEEDILLLEDQNSKFLK---EKKLLED----------RVGEMTSQLAEEEEKAKNLG----KVKNKQEMMM-- 1039
Cdd:pfam05622 85 yriKCEELEKEVLELQHRNEELTSlaeEAQALKDemdilressdKVKKLEATVETYKKKLEDLGdlrrQVKLLEERNAey 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1040 ----VDLEERLKKEEKTRQELEKAKRKLdaetTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNN---A 1112
Cdd:pfam05622 165 mqrtLQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTlreT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1113 LKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLseeleaLKTELEDTLdttaaqqeLRSKREQEVAELKKAIDDETRn 1192
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEI------MPAEIREKL--------IRLQHENKMLRLGQEGSYRER- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1193 hesqiqemrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSE-------SEHKRKKLEAQLQ 1265
Cdd:pfam05622 306 ---------------LTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEqgskaedSSLLKQKLEEHLE 370
|
410 420
....*....|....*....|....*..
gi 528481573 1266 EVMARFSEGEKVKGELADRTHKIQTEL 1292
Cdd:pfam05622 371 KLHEAQSELQKKKEQIEELEPKQDSNL 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
882-1215 |
4.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 882 ERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQ--SLQNEKKkmqsHIQDLE 959
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELE----RLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 960 EQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKaknlgkvknkqemmm 1039
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--------------- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1040 vDLEERLKKEEKTRQELEKAKRkldaettdLQDQIAELQAQIDELKIQLAKKEEELQ----AVLARGDEEVAQKNNALKQ 1115
Cdd:COG4913 750 -LLEERFAAALGDAVERELREN--------LEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLAL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1116 LRELQAQ-LAELQEDLESEKAARNKAEK--LKRDLSEELEALKTELE---DTL------DTTAAQQELRSKREQEVAELK 1183
Cdd:COG4913 821 LDRLEEDgLPEYEERFKELLNENSIEFVadLLSKLRRAIREIKERIDplnDSLkripfgPGRYLRLEARPRPDPEVREFR 900
|
330 340 350
....*....|....*....|....*....|..
gi 528481573 1184 KAIDDETRNHESQIQEMRQRHGTALEEISEQL 1215
Cdd:COG4913 901 QELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1079-1189 |
4.80e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1079 AQIDELKIQLAKKEEELQAVLARGDEEVAQKnnalkqLRELQAQLAELQEDLESEKaARNKAEKlkrDLSEELEALKTEL 1158
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALK-ARWEAEK---ELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 528481573 1159 EDTLDTTAAQQELRSKREQEVAELKKAIDDE 1189
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
948-1329 |
4.88e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 948 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVT----------------------AEAKIKKMEEDILLLEDQNSK--FLKE 1003
Cdd:PRK04778 24 RKRNYKRIDELEERKQELENLPVNDELEKVKklnltgqseekfeewrqkwdeiVTNSLPDIEEQLFEAEELNDKfrFRKA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1004 KKLLedrvGEMTSQLAEEEEKAKNLgkvknKQEMM-MVDLEERLKKE-EKTRQELEKAKRKLDAETTDLQDQIAELQAQI 1081
Cdd:PRK04778 104 KHEI----NEIESLLDLIEEDIEQI-----LEELQeLLESEEKNREEvEQLKDLYRELRKSLLANRFSFGPALDELEKQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1082 DELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDT 1161
Cdd:PRK04778 175 ENLEEEFSQFVELTES----GDYVEAR-----EILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1162 ---LDTTAAQQELRSKREQeVAELKKAID----DETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEKNKQTLES 1234
Cdd:PRK04778 246 gyhLDHLDIEKEIQDLKEQ-IDENLALLEeldlDEAEEKNEEIQE-------RIDQLYDILEREVKARKYVEKNSDTLPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1235 D-------NKELTNEVKSLQQAK--SESE-HKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEK 1304
Cdd:PRK04778 318 FlehakeqNKELKEEIDRVKQSYtlNESElESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEK 397
|
410 420
....*....|....*....|....*
gi 528481573 1305 KGIKLTKDVSSLESQLQDTQELLQE 1329
Cdd:PRK04778 398 EQEKLSEMLQGLRKDELEAREKLER 422
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1581-1790 |
5.30e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1581 RDLQARDEQNEEKKRALVKQVREMEAELEDerkqralAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1660
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1661 QRELEEARTSRD--EIFTQSKENEKKLKSLEA----------EILQLQEDLASSERARRHAEQERDELADEISNSASGKA 1728
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSESFSDFLDRLSAlskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481573 1729 ALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENAR 1790
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1043-1263 |
5.49e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1043 EERLKKEEKTRQEleKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQ 1122
Cdd:PRK05035 459 QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAE 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1123 LAELQEDLESEKA-----ARNKAEKLKR-----DLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRN 1192
Cdd:PRK05035 537 KQAAAAADPKKAAvaaaiARAKAKKAAQqaanaEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAA 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1193 HESQIQEMR-QRHGTALEEISEQLEQAK--RVKGNLEKNK-----QTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQ 1263
Cdd:PRK05035 617 VAAAIARAKaKKAEQQANAEPEEPVDPRkaAVAAAIARAKarkaaQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1046-1346 |
5.63e-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: 44.42 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1046 LKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAqlae 1125
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTR---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1126 lQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQElrskreqevaelkkaiddetrNHESQIQEMrQRHg 1205
Cdd:pfam15905 137 -VNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQE---------------------GMEGKLQVT-QKN- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1206 taLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLeAQLQEVMArfsegekvkgELADRT 1285
Cdd:pfam15905 193 --LEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDI-AQLEELLK----------EKNDEI 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481573 1286 HKIQTELDNVSCLLEdaekkgiKLTKDVSSLESQLQ-DTQELLQEETRQKLNLSSRIRQLEE 1346
Cdd:pfam15905 260 ESLKQSLEEKEQELS-------KQIKDLNEKCKLLEsEKEELLREYEEKEQTLNAELEELKE 314
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
861-1159 |
5.71e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 861 DEELIKVKERQVKVENELVEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLVAKkqELEEILHDLESRVEE 936
Cdd:PRK05771 27 ELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklRSYLPKLNPLREEKKKVSVKSLEELIK--DVEEELEKIEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 937 EEERNQSLQNEKKKMQSHIQdleeqldeeeaarqklQLEKVtaeakiKKMEEDIllledqnsKFLKEKKLLEDRVGEMTS 1016
Cdd:PRK05771 105 LEEEISELENEIKELEQEIE----------------RLEPW------GNFDLDL--------SLLLGFKYVSVFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1017 QLAEEEEKAKNLGKV----KNKQEMMMV---------DLEERLKKEEKTRQELEkAKRKLDAETTDLQDQIAELQAQIDE 1083
Cdd:PRK05771 155 DKLEELKLESDVENVeyisTDKGYVYVVvvvlkelsdEVEEELKKLGFERLELE-EEGTPSELIREIKEELEEIEKERES 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1084 LK---IQLAKKEEELQAVLARGDEEVAQKNNALKQLRE------LQA-----QLAELQEDLesEKAARNKAEKLKRDLSE 1149
Cdd:PRK05771 234 LLeelKELAKKYLEELLALYEYLEIELERAEALSKFLKtdktfaIEGwvpedRVKKLKELI--DKATGGSAYVEFVEPDE 311
|
330
....*....|
gi 528481573 1150 ELEALKTELE 1159
Cdd:PRK05771 312 EEEEVPTKLK 321
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1007-1091 |
6.83e-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: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1007 LEDRVGEMTSQLAEEEEKAKNLGKVKNkqEMMMVDLEERLK----------KEEKTRQELEKAKRKLDAETTDLQDQIAE 1076
Cdd:cd23165 11 LNARLHELKEELKAKKKELENLEDASD--ELELADDDEPVPykigevfvhlSLEEAQERLEKAKEELEEEIEKLEEEIDE 88
|
90
....*....|....*
gi 528481573 1077 LQAQIDELKIQLAKK 1091
Cdd:cd23165 89 IEEEMKELKVQLYAK 103
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1038-1177 |
6.85e-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: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1038 MMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQavlargdEEVAQKNNALKQLR 1117
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLA-------TERSARREAEAELE 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1118 ELQAQLAELQEDLESEKAARnkaEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQ 1177
Cdd:pfam09787 118 RLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQ 174
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1196-1347 |
7.03e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 44.65 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1196 QIQEMR----QRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARF 1271
Cdd:pfam10168 540 ATQVFReeylKKHDLAREEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1272 -------SEGEKvkgELADRTHKIQTELDNVSCLLEDAEKK------------GIKLTKDVSSLESQLQDTQELLQEETR 1332
Cdd:pfam10168 620 nsqlpvlSDAER---EMKKELETINEQLKHLANAIKQAKKKmnyqryqiaksqSIRKKSSLSLSEKQRKTIKEILKQLGS 696
|
170
....*....|....*
gi 528481573 1333 QKLNLSSRIRQLEEE 1347
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 ... |
1688-1826 |
7.70e-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: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1688 LEAEILQLQEDLASSERARRHAEQERD---ELADEISNSASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1764
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDrlqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1765 TTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKS---KLQELEGSVKSKFKASIAALEAKI 1826
Cdd:pfam00529 136 GGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQsaaENQAEVRSELSGAQLQIAEAEAEL 200
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1036-1170 |
7.94e-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: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1036 EMMMVDLEERLKKE--EKTRQELEKAKRKLDAETTDLQD------------QIAELQAQIDELKIQLAKKEEELQAVLAR 1101
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481573 1102 GDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLkrdlsEELEALKTEL---EDTLDTTAAQQE 1170
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
970-1170 |
7.95e-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: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 970 QKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLgkvknkqemmMVDLEERLKKE 1049
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA----------LTKGNEELARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1050 EKTR-QELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARgdEEVAQKNNALKQLR---------EL 1119
Cdd:pfam04012 88 ALAEkKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTSLgslstssatDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 528481573 1120 QAQLAELQEDLESEKAARNKAEKlKRDLSEELEALKTELEDTLDTTAAQQE 1170
Cdd:pfam04012 166 FERIEEKIEEREARADAAAELAS-AVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1532-1717 |
9.26e-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: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1532 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDE 1611
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1612 RKQRALAVAAKKKLEmdlkdveaqiEAANKARDEAIKqlrKLQAQMKdyqRELEEARTSRDEIFTQSKENEKKLKSLEAE 1691
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 528481573 1692 ILQLQEDLASSERARRHAEQERDELA 1717
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1646-1933 |
1.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1646 AIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAE---QERDELADEISN 1722
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1723 SASGKAALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttmqvdtlntelAGERSAAQKSENARQQLERQNKDLKS 1802
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1803 KLQELEgSVKSKFKASIAALEAKIlqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANsRM 1882
Cdd:PRK03918 308 ELREIE-KRLSRLEEEINGIEERI-----------KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-EL 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 528481573 1883 KQLKRQLeeaeeeatrANASRRKLQRELDDATEASEGLSREVNTLKNRLRR 1933
Cdd:PRK03918 375 ERLKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1016-1154 |
1.09e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1016 SQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEEL 1095
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR-APAWLAA 607
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1096 QAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEAL 1154
Cdd:COG3096 608 QDALERLREQSGE---ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1260-1609 |
1.14e-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: 43.73 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1260 LEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKgikLTKDVSSLESQLQDTQELLQEETRQKLNLSS 1339
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE---LESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1340 RIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLE------DDVGALEGLEEVKRK-LQKDMEVTSQKLE 1412
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELErmkeraKKAGAQRKEEEAERKqLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1413 EKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMA 1492
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1493 RALDEALEAKEEFERLNKQL--------------RAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL 1558
Cdd:pfam07888 269 RTQAELHQARLQAAQLTLQLadaslalregrarwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVEL 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1559 QATEDAKL----RLEVNMQAMKAQFdRDLQARDEQNEEKKRALVKQVREMEAELE 1609
Cdd:pfam07888 349 GREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
864-1094 |
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 528481573 864 LIKVKERQVKVENELVEMERKH--QQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERN 941
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 942 QSLQNEKKKMQShiqdleeqldeeEAARQKLQLEKVTAEAK--------------IKKMEEDILLLEDQNSKFLKEKKLL 1007
Cdd:PHA02562 251 EDPSAALNKLNT------------AAAKIKSKIEQFQKVIKmyekggvcptctqqISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1008 EDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQ 1087
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKIS----TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
....*..
gi 528481573 1088 LAKKEEE 1094
Cdd:PHA02562 395 KSELVKE 401
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1615-1824 |
1.19e-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: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1615 RALAVAAKKKLEMDLKD-----VEAQIEAANKARDEA---IKQLRKLQAQMKDYQRELEEARTSRDEIFTQ--SKENEKK 1684
Cdd:cd22656 101 DDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAakvVDKLTDFENQTEKDQTALETLEKALKDLLTDegGAIARKE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1685 LKSLEAEILQLQEDLAsserarRHAEQERDELADEISNsasgkaalLDEKRRLEARIaqleeeleeeQSNMELLNDrfrk 1764
Cdd:cd22656 181 IKDLQKELEKLNEEYA------AKLKAKIDELKALIAD--------DEAKLAAALRL----------IADLTAADT---- 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1765 ttmQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEA 1824
Cdd:cd22656 233 ---DLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1050-1336 |
1.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1050 EKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQED 1129
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1130 LESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMRQRHGTALE 1209
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1210 EISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHkRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQ 1289
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL-SALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 528481573 1290 TELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLN 1336
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
947-1149 |
1.36e-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: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 947 EKKKMQSHIQDLEEQLDEEEAARQKLQLEKVtaEAKIKKMEEDILLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAK 1026
Cdd:pfam06160 231 EHLNVDKEIQQLEEQLEENLALLENLELDEA--EEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1027 NLgkvknKQEMMMVDLEERLKKEEKTRQElekakrkldaettDLQDQIAELQAQIDELKIQLAKKE---EELQAVLargd 1103
Cdd:pfam06160 309 EL-----KEELERVQQSYTLNENELERVR-------------GLEKQLEELEKRYDEIVERLEEKEvaySELQEEL---- 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528481573 1104 eevaqkNNALKQLRELQAQLAELQEDLES----EKAARNKAEKLKRDLSE 1149
Cdd:pfam06160 367 ------EEILEQLEEIEEEQEEFKESLQSlrkdELEAREKLDEFKLELRE 410
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1021-1565 |
1.36e-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: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1021 EEEKAKNLGKVKNKQEMMMVDL----EERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQ 1096
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1097 A-----------VLARGDEEVAQKNNALKQlRELQAQLAELQEDLESEKAA------RNKAEKLKRDLSEELEALKTELE 1159
Cdd:pfam07111 215 AqvtlveslrkyVGEQVPPEVHSQTWELER-QELLDTMQHLQEDRADLQATvellqvRVQSLTHMLALQEEELTRKIQPS 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1160 DTLD---TTAAQQELRSKREQeVAELKKAIDDETRNHESQIQEMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDN 1236
Cdd:pfam07111 294 DSLEpefPKKCRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVER 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1237 ---KELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKK--GIK-LT 1310
Cdd:pfam07111 373 msaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhTIKgLM 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1311 KDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeeSRKNLEKQLATLQAQLvETKKKLEDDVGAL 1390
Cdd:pfam07111 453 ARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREER------------NRLDAELQLSAHLIQQ-EVGRAREQGEAER 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1391 EGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVDLDHQRQIVSnlekkqKKFDQMLAEEKTISARY 1470
Cdd:pfam07111 520 QQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYG------QALQEKVAEVETRLREQ 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1471 AEERDRAEAEAREKDTKALSMARALDEalEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKR----TLEQQVEE 1546
Cdd:pfam07111 594 LSDTKRRLNEARREQAKAVVSLRQIQH--RATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNlmlaTLQQEGLL 671
|
570
....*....|....*....
gi 528481573 1547 MRTQLEELEDELQATEDAK 1565
Cdd:pfam07111 672 SRYKQQRLLAVLPSGLDKK 690
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1610-1800 |
1.44e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1610 DERKQRALAVAAKKKLEMDLK---DVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKEN----- 1681
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrq 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1682 -EKKLKSLEAEILQLQEDLAS-----------SERARR---HAEQERDELADEISNSASGKAALLDEKR-RLEARIAQle 1745
Cdd:PRK11281 126 lESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQAEQAL-- 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1746 eeleeeqsnMELLNDrFRKTTMQVDTLNTELaGERSAAQKSENArQQLERQNKDL 1800
Cdd:PRK11281 204 ---------LNAQND-LQRKSLEGNTQLQDL-LQKQRDYLTARI-QRLEHQLQLL 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1001-1672 |
1.65e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1001 LKEKKLLEDRVGEMTSQLAE----------EEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDL 1070
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSEleqrlrqqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1071 QDQIAELQAQIDELKiQLAKKEEELQAVLARGDEEVAQknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1150
Cdd:PRK04863 585 RQQLEQLQARIQRLA-ARAPAWLAAQDALARLREQSGE---EFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1151 LEALkteledTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEMR---QRHGTALEEISeqleqakRVKGNLEK 1227
Cdd:PRK04863 661 IERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLS-------DAAEQLAG 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1228 NKQTLEsDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSE--GEKVKGELA--DRTHKIQTELDNVSCLLEdae 1303
Cdd:PRK04863 728 LEDCPE-DLYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRfpEVPLFGRAAreKRIEQLRAEREELAERYA--- 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1304 kkgiKLTKDVSSLESQLQDTQELLQ-----------EETRQKLNlsSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATL 1372
Cdd:PRK04863 804 ----TLSFDVQKLQRLHQAFSRFIGshlavafeadpEAELRQLN--RRRVELERALADHESQEQQQRSQLEQAKEGLSAL 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1373 QAQLVETKKKLEDDVGalEGLEEVKRKLqKDMEVTSQKLEEKAIAFDKLEKTKNRLQ---QELDDLMVDLDHQRQIVSNL 1449
Cdd:PRK04863 878 NRLLPRLNLLADETLA--DRVEEIREQL-DEAEEAKRFVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDA 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1450 ekKQKKFDqmlaeektisarYAEERDRAEAEAREKDTKALSMARALDEALEAK-EEFERLNKQLRAEMEDLISSKDDVGK 1528
Cdd:PRK04863 955 --KQQAFA------------LTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRlEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1529 NVHELEKSKRTLEQQVEEMRTQLEELedELQATEDAklrlevnmqAMKAQFDRD-LQARDEQNEEKKRALVKQVREMEAE 1607
Cdd:PRK04863 1021 VLASLKSSYDAKRQMLQELKQELQDL--GVPADSGA---------EERARARRDeLHARLSANRSRRNQLEKQLTFCEAE 1089
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1608 LEDERKQralavaaKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQREL-----EEARTSRD 1672
Cdd:PRK04863 1090 MDNLTKK-------LRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELaylsaDELRSMSD 1152
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1081-1263 |
1.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1081 IDELKIQLAKKEEELQAvlargdEEVAQKNNALKQLRELQAQ--LAELQEDLESE-KAARNKAEKLKRDLSEELEALKTE 1157
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIL------EEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1158 LEDTLDTTA---AQQELRSKREQEVAELKKaiddetrnhesQIQEMRQRHGTALEEISE-QLEQAKRVKgnLEKNKQTLE 1233
Cdd:PRK12704 102 LELLEKREEeleKKEKELEQKQQELEKKEE-----------ELEELIEEQLQELERISGlTAEEAKEIL--LEKVEEEAR 168
|
170 180 190
....*....|....*....|....*....|
gi 528481573 1234 SDNKELTNEVKslQQAKSESEHKRKKLEAQ 1263
Cdd:PRK12704 169 HEAAVLIKEIE--EEAKEEADKKAKEILAQ 196
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1591-1864 |
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 528481573 1591 EEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTS 1670
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1671 RDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLEEELEE 1750
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1751 EQSNMELLNDRFRKTTMQ-VDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAKILQL 1829
Cdd:COG4372 190 KEANRNAEKEEELAEAEKlIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270
....*....|....*....|....*....|....*
gi 528481573 1830 EEQLEQEAKERAAANKIVRRTEKKLKEVFMQVEDE 1864
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1650-1813 |
1.89e-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: 42.96 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1650 LRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEisnsasgKAA 1729
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE-------KDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1730 LLDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEG 1809
Cdd:pfam07888 120 LLAQRAAHEARIRE--------------LEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
....
gi 528481573 1810 SVKS 1813
Cdd:pfam07888 186 ELRS 189
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1041-1196 |
1.89e-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: 41.90 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1041 DLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNALK-QLREL 1119
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAAL 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528481573 1120 QAQLAELQEDLESeKAARNKAEKLKRDL-SEELEALKTELEdtldttAAQQELRSKREQEVAELKKAIDDETRNHESQ 1196
Cdd:pfam12795 162 KAQIDMLEQELLS-NNNRQDLLKARRDLlTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
897-1303 |
2.08e-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: 42.92 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 897 EQLQAETELFAEAEEMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEkkkmqshiqdleeqldeeeaarqklqlek 976
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT----------------------------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 977 vtaeakikkmeedillLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEE--------KAKnlgKVKNKQEMMMVDLEERLkk 1048
Cdd:pfam06160 137 ----------------LLANRFSYGPAIDELEKQLAEIEEEFSQFEEltesgdylEAR---EVLEKLEEETDALEELM-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1049 eEKTRQELEKAKRKLDAETTDLQDQIAELQAQ---IDELKI-----QLAKKEEELQAVLARGDEEVAQKNNalkqlRELQ 1120
Cdd:pfam06160 196 -EDIPPLYEELKTELPDQLEELKEGYREMEEEgyaLEHLNVdkeiqQLEEQLEENLALLENLELDEAEEAL-----EEIE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1121 AQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTELEDTLDTTA--------AQQELRSKR--EQEVAELKKA---ID 1187
Cdd:pfam06160 270 ERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELErvqqsytlNENELERVRglEKQLEELEKRydeIV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1188 DETRNHE---SQIQEMrqrhgtaLEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKseSEHKRKKLEAQL 1264
Cdd:pfam06160 350 ERLEEKEvaySELQEE-------LEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL--REIKRLVEKSNL 420
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 528481573 1265 ----QEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAE 1303
Cdd:pfam06160 421 pglpESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQ 463
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1517-1691 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1517 EDLISSKDDvGKNVHELEkSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQARDEQNEEKKRA 1596
Cdd:pfam09787 24 EKLIASLKE-GSGVEGLD-SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1597 LVKQV---REMEAEL-----------EDERKQRALAVAAKKKLEMDLKDVEAQIEA---ANKARDEAIKQLRKLQAQMKD 1659
Cdd:pfam09787 102 LATERsarREAEAELerlqeelryleEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQ 181
|
170 180 190
....*....|....*....|....*....|..
gi 528481573 1660 YQRELEEARTSRDEIFTQSKENEKKLKSLEAE 1691
Cdd:pfam09787 182 KQTMLEALSTEKNSLVLQLERMEQQIKELQGE 213
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1000-1155 |
2.26e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1000 FLKEKKLLEDRvGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELqa 1079
Cdd:PRK12705 24 LLKKRQRLAKE-AERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1080 qiDELKIQLAKKEEELQAVLARGDEEVAQKNNALKQ---LRELQAQ---LAELQEDLESEKAARNKAEKLKRDLSEELEA 1153
Cdd:PRK12705 101 --DNLENQLEEREKALSARELELEELEKQLDNELYRvagLTPEQARkllLKLLDAELEEEKAQRVKKIEEEADLEAERKA 178
|
..
gi 528481573 1154 LK 1155
Cdd:PRK12705 179 QN 180
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1532-1743 |
2.29e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1532 ELEKSKRTLEQQVEEMRTQLEELED-ELQATEDAKLRLEVNMQAmkaqfdrdlqardeqNEEKKRALVKQVREMeaeL-E 1609
Cdd:COG0497 176 ELRADEAERARELDLLRFQLEELEAaALQPGEEEELEEERRRLS---------------NAEKLREALQEALEA---LsG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1610 DERKQRALAVAAKKKLEmDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE---------EARTSR--------- 1671
Cdd:COG0497 238 GEGGALDLLGQALRALE-RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfdperleevEERLALlrrlarkyg 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1672 ---DEIFTQSKENEKKLKSLEAeilqLQEDLASSERARRHAEQERDELADEISNsASGKAAlldekRRLEARIAQ 1743
Cdd:COG0497 317 vtvEELLAYAEELRAELAELEN----SDERLEELEAELAEAEAELLEAAEKLSA-ARKKAA-----KKLEKAVTA 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
849-1034 |
2.32e-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: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 849 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERK----HQQLLEEKNILAEQLQA--------------ETELFAEAE 910
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 911 EMRARLVAKKQELEEILHDLESRVEEEEERNQSLQNEKKKMQShiqdleeQLDEEEAARQKLQLEKVTAEAKIKKMEEDI 990
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 528481573 991 LLLEDQNSKFLKEKKLLEDRVGEMTSQLAEEEEKAKNLGKVKNK 1034
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1426-1860 |
2.52e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1426 NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaeEKTISARYAEERDRAEAEAREKDTKALsMARALDEALEAKEEF 1505
Cdd:COG5278 89 DELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRARLLLLALAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1506 ERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFDRDLQA 1585
Cdd:COG5278 166 AALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1586 RDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELE 1665
Cdd:COG5278 246 LAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAAL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1666 EARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKAALLDEKRRLEARIAQLE 1745
Cdd:COG5278 326 AALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1746 EELEEEQSNMELLNDRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKASIAALEAK 1825
Cdd:COG5278 406 AAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALA 485
|
410 420 430
....*....|....*....|....*....|....*
gi 528481573 1826 ILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQ 1860
Cdd:COG5278 486 EAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1131-1348 |
2.76e-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: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1131 ESEKAARNKAEKLKRdlSEELEALKTELEDTLDTTAAQQELRSKREQEvAELKKAIDDETRNhESQIQEMRQRHGTALEE 1210
Cdd:TIGR00927 637 EAEHTGERTGEEGER--PTEAEGENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEG-EGEIEAKEADHKGETEA 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1211 ISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGEL-ADRTHKIQ 1289
Cdd:TIGR00927 713 EEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIqAGEDGEMK 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1290 TElDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1348
Cdd:TIGR00927 793 GD-EGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEK 850
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1044-1153 |
2.78e-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: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1044 ERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQlAKKEEELQAvlARGDEEVAQKNNALKQLRELQAQL 1123
Cdd:COG2268 220 NREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEAAYEIAE--ANAEREVQRQLEIAEREREIELQE 296
|
90 100 110
....*....|....*....|....*....|...
gi 528481573 1124 AELQEDLESEKA---ARNKAEKLKRDLSEELEA 1153
Cdd:COG2268 297 KEAEREEAELEAdvrKPAEAEKQAAEAEAEAEA 329
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1049-1181 |
2.85e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1049 EEKTRQELEKAKrKLDAE-TTDLQDQIAELQAqidELKIQLAKKEEELQAVLARGDEEvaqknNALKQLRELQAQLAELQ 1127
Cdd:PTZ00491 642 DERTRDSLQKSV-QLAIEiTTKSQEAAARHQA---ELLEQEARGRLERQKMHDKAKAE-----EQRTKLLELQAESAAVE 712
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481573 1128 ---------------EDLESE---KAARNKAEKLKRDLSEELEALKTELEDTLDTTAAQQELRSKREQEVAE 1181
Cdd:PTZ00491 713 ssgqsraealaeaeaRLIEAEaevEQAELRAKALRIEAEAELEKLRKRQELELEYEQAQNELEIAKAKELAD 784
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1491-1619 |
3.09e-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: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1491 MARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVgknVHELEKSKRTLEQQVEEMRTQLEELEDEL---QATEDAKLR 1567
Cdd:COG2433 386 IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQ---VERLEAEVEELEAELEEKDERIERLERELseaRSEERREIR 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 528481573 1568 LEVNMQAMKAQFDRdLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAV 1619
Cdd:COG2433 463 KDREISRLDREIER-LERELEEERERIEELKRKLERLKELWKLEHSGELVPV 513
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1206-1704 |
3.16e-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: 42.63 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1206 TALEEISEQLEQAKRVKGNLEKN-------KQTLESDNKELTNEVKSLQQAKSESEHKRKKleaQLQEVMARFSEgEKVK 1278
Cdd:pfam15818 7 TSLLEALEELRMRREAETQYEEQigkiiveTQELKWQKETLQNQKETLAKQHKEAMAVFKK---QLQMKMCALEE-EKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1279 GELADRTHkiQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQdTQELLQEETRQKLNlssrirQLEEEKNNLLEQQEEE 1358
Cdd:pfam15818 83 YQLATEIK--EKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQ-LHLLAKEDHHKQLN------EIEKYYATITGQFGLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1359 EESRKNLEKQLA---TLQAQLVETKKKLEDDVGAL-EGLEEVKRKLQKDmEVTSQ-KLEEKAIAFDKLEKTKNRLQQELD 1433
Cdd:pfam15818 154 KENHGKLEQNVQeaiQLNKRLSALNKKQESEICSLkKELKKVTSDLIKS-KVTCQyKMGEENINLTIKEQKFQELQERLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1434 -DLMVDLDHQRQIVSNLEKKQKKFdqmlaeektISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERlnKQL 1512
Cdd:pfam15818 233 mELELNKKINEEITHIQEEKQDII---------ISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQR--EKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1513 RAEMEDLISSKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfdrdlqarDEQNEE 1592
Cdd:pfam15818 302 KENEEKFLNLQN-------EHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQ--------KKFEED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1593 KKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQReLEeaRTSRD 1672
Cdd:pfam15818 367 KKFQNVPEVNNENSEMSTEKSENLIIQKYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQV-LE--KSFKN 443
|
490 500 510
....*....|....*....|....*....|..
gi 528481573 1673 EIFTQSKENEKKLKSLEAEILQLQEDLASSER 1704
Cdd:pfam15818 444 EIDTSVPQDKNQSEISLSKTLCTDKDLISQGQ 475
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1625-1795 |
3.23e-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: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1625 LEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQ---RELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLAs 1701
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1702 seRARRHAEQE---RDELADEISNSASGKAALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTMQVDTLNTELag 1778
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL-- 200
|
170
....*....|....*..
gi 528481573 1779 ersaaqksENARQQLER 1795
Cdd:pfam00529 201 --------KLAKLDLER 209
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1004-1167 |
3.24e-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: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1004 KKLLEDRVGEMTSQLAEEEEKAKnlgKVKNKqemmMVDLEERLKKEEKTRQELEKA-KRKLDAETTDL-QDQIAELQAQI 1081
Cdd:cd22656 116 KKTIKALLDDLLKEAKKYQDKAA---KVVDK----LTDFENQTEKDQTALETLEKAlKDLLTDEGGAIaRKEIKDLQKEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1082 DELK----IQLAKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLEsekAARNKAEKLK---RDLSEELEAL 1154
Cdd:cd22656 189 EKLNeeyaAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIG---PAIPALEKLQgawQAIATDLDSL 265
|
170
....*....|...
gi 528481573 1155 KTELEDTLDTTAA 1167
Cdd:cd22656 266 KDLLEDDISKIPA 278
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1304-1569 |
3.29e-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: 41.72 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1304 KKGIKLTKDVSSLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKL 1383
Cdd:pfam15905 63 KKSQKNLKESKDQKELEKEIRALVQERGEQ----DKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1384 EDDVGALEGLEEVKRKLQKDMEVTS--QKLEEKA-IAFDKLEKTKNRLQQelddLMVDLDHQRQIVSNLEKKQKKFDQML 1460
Cdd:pfam15905 139 ELLKAKFSEDGTQKKMSSLSMELMKlrNKLEAKMkEVMAKQEGMEGKLQV----TQKNLEHSKGKVAQLEEKLVSTEKEK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1461 AEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKrtl 1540
Cdd:pfam15905 215 IEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK--- 291
|
250 260
....*....|....*....|....*....
gi 528481573 1541 EQQVEEMRTQLEELEDELQATEDaKLRLE 1569
Cdd:pfam15905 292 EELLREYEEKEQTLNAELEELKE-KLTLE 319
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1055-1155 |
3.51e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1055 ELEKAKRKLDAETTDLQ---DQIAELQAQIDELKiQLAKK----EEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQ 1127
Cdd:COG0497 276 ELEEAASELRRYLDSLEfdpERLEEVEERLALLR-RLARKygvtVEELLAYAEELRAELAELENSDERLEELEAELAEAE 354
|
90 100 110
....*....|....*....|....*....|....
gi 528481573 1128 EDLEsEKAA------RNKAEKLKRDLSEELEALK 1155
Cdd:COG0497 355 AELL-EAAEklsaarKKAAKKLEKAVTAELADLG 387
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1043-1222 |
3.55e-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: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1043 EERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKI------QLAKKEEEL---QAVLARGDEEVaqknnal 1113
Cdd:pfam10168 546 EEYLKKHDLAREEIQKRVKLLKLQK---EQQLQELQSLEEERKSlseraeKLAEKYEEIkdkQEKLMRRCKKV------- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1114 kqLRELQAQLAELqedLESEkaarnkaeklkRDLSEELEALKTELEdTLDttAAQQELRSKREQEVAELKKAIDDETRN- 1192
Cdd:pfam10168 616 --LQRLNSQLPVL---SDAE-----------REMKKELETINEQLK-HLA--NAIKQAKKKMNYQRYQIAKSQSIRKKSs 676
|
170 180 190
....*....|....*....|....*....|....*.
gi 528481573 1193 ------HESQIQEMRQRHGtalEEISEQLEQAKRVK 1222
Cdd:pfam10168 677 lslsekQRKTIKEILKQLG---SEIDELIKQVKDIN 709
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1313-1533 |
4.21e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1313 VSSLESQLqDTQELLQEETRQKlnlSSRIRQLEEEKNNLLEQQEeeeesrKNLEKQLATLQAQLVETKKKLEDDVGALEG 1392
Cdd:PHA02562 190 IDHIQQQI-KTYNKNIEEQRKK---NGENIARKQNKYDELVEEA------KTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1393 LEEVKRKLQKDME----------------VTSQKLEEKAiafDKLEKTKNR---LQQELDDLMVDLDHQRQIVSNLEKKQ 1453
Cdd:PHA02562 260 LNTAAAKIKSKIEqfqkvikmyekggvcpTCTQQISEGP---DRITKIKDKlkeLQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1454 KKFDQMLAEEKTISARYAEERDRAeaeareKDTKALsMARALDEALEAKEEFERLNKQLraemEDLISSKDDVGKNVHEL 1533
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKA------KKVKAA-IEELQAEFVDNAEELAKLQDEL----DKIVKTKSELVKEKYHR 405
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
948-1344 |
4.71e-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: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 948 KKKMQSHIQDLEEQLDEEEAARQKLQLEKVTA----------------------EAKIKKMEEDILLLEDQNSK--FLKE 1003
Cdd:pfam06160 5 RKKIYKEIDELEERKNELMNLPVQEELSKVKKlnltgetqekfeewrkkwddivTKSLPDIEELLFEAEELNDKyrFKKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1004 KKLLEdrvgEMTSQLAEEEEKAKNLGKvknkqemmmvDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQ-------IAE 1076
Cdd:pfam06160 85 KKALD----EIEELLDDIEEDIKQILE----------ELDELLESEEKNREEVEELKDKYRELRKTLLANrfsygpaIDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1077 LQAQIDELKIQLAKKEEELQAvlarGDEEVAQknnalKQLRELQAQLAELQEDLESEKAArnkAEKLKRDLSEELEALK- 1155
Cdd:pfam06160 151 LEKQLAEIEEEFSQFEELTES----GDYLEAR-----EVLEKLEEETDALEELMEDIPPL---YEELKTELPDQLEELKe 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1156 --TELE------DTLDTTAAQQELRSKREQEVAELKKAIDDETRNHESQIQEmrqrhgtALEEISEQLEQAKRVKGNLEK 1227
Cdd:pfam06160 219 gyREMEeegyalEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1228 NKQTLESD-------NKELTNEVKSLQQ----AKSESEHKR------KKLEAQLQEVMARFSEGEKVKGELADRTHKIQT 1290
Cdd:pfam06160 292 NLPEIEDYlehaeeqNKELKEELERVQQsytlNENELERVRglekqlEELEKRYDEIVERLEEKEVAYSELQEELEEILE 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 528481573 1291 ELDNVsclledaEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQL 1344
Cdd:pfam06160 372 QLEEI-------EEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1390-1899 |
4.86e-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: 41.88 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1390 LEGLEEVKRKLQKDMEVTSQKLEEKAiafdKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKTISAR 1469
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHG----KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1470 YaeerdraeaearekdtkalsmaRALDEALEAKEEFERLNKQLRAEMEDLISSKddvgkNVHELEKSKRTLEQQVEEMRT 1549
Cdd:TIGR00618 245 L----------------------TQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1550 QLEELEDELQATEDAKLRLEVNMQAM-KAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKK---L 1625
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1626 EMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIFTQSKENEKKLKSLEAEILQLQEDLASSERA 1705
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1706 RRHAEQERDELADEISNSASGKAALLDEKRRLEARIAqleeELEEEQSNMELLNDRFRKTTMQVdTLNTELAGERSAAQK 1785
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMQR 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1786 SENARQQLERQNKDLKSKLQELE---GSVKSKFKASIAALEAKILQLEEQLEQEAKERAAANKIVRRTEKKLKEVFMQVE 1862
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510
....*....|....*....|....*....|....*..
gi 528481573 1863 DERRHADQYKEQMEKANSRMKQLKRQLEEAEEEATRA 1899
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1004-1155 |
5.38e-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: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1004 KKLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLD----AETTDLQDQIAELQA 1079
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEdcdpTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1080 QIDELKIQLAKKEEELQAVlargdEEVAQKNNALKQlrELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALK 1155
Cdd:smart00787 219 EIMIKVKKLEELEEELQEL-----ESKIEDLTNKKS--ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1002-1158 |
5.42e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1002 KEKKL--LEDRVGEMTSQLAEEEEKAKNLgkvknkqEMMMVDLEERLKKEEKTRQELEKakrkLDAEttdLQDQIAELQA 1079
Cdd:PRK09039 51 KDSALdrLNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERSRLQA----LLAE---LAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528481573 1080 QIDELKIQLAkkeeELQAVLARgdeevaqknnALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEALKTEL 1158
Cdd:PRK09039 117 RAGELAQELD----SEKQVSAR----------ALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1030-1153 |
5.68e-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: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1030 KVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETtdlQDQIAELQAQIDELKiqlakkeEELQAVLARGDEEVAQK 1109
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAS---FERLAELRDELAELE-------EELEALKARWEAEKELI 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 528481573 1110 NNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEELEA 1153
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1523-1686 |
5.70e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1523 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEdaKLRLEVNMQAmkaqfdrdlqardEQNEEKKRALVkqvr 1602
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE--KLKEELEEKK-------------EKLQEEEDKLL---- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1603 emeAELEDERKQRalavaakkklemdlkdveaqIEAANKARDEAIKQLRKLQA---------QMKDYQRELEEARTSRDE 1673
Cdd:PRK00409 569 ---EEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKggyasvkahELIEARKRLNKANEKKEK 625
|
170
....*....|...
gi 528481573 1674 IFTQSKENEKKLK 1686
Cdd:PRK00409 626 KKKKQKEKQEELK 638
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1053-1155 |
5.96e-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: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1053 RQELEKAKRKLDAETTDLQDQIAELQAQIDELkIQLAKKEEELQAVLArgDEEVAQKNNALKQLRELQAQLAELQEDLES 1132
Cdd:TIGR04320 260 QAKLATAQADLAAAQTALNTAQAALTSAQTAY-AAAQAALATAQKELA--NAQAQALQTAQNNLATAQAALANAEARLAK 336
|
90 100
....*....|....*....|...
gi 528481573 1133 EKAArnkAEKLKRDLSEELEALK 1155
Cdd:TIGR04320 337 AKEA---LANLNADLAKKQAALD 356
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1004-1186 |
6.09e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1004 KKLLEDRVGEMTSQLAE-EEEKAKNLGKVKnKQEMMMVDLEERLKK-EEKTRQELEKA-----------KRKLDAETTDL 1070
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEaRQALAQVIANQK-RLERQLEELEAEAEKwEEKARLALEKGredlarealerKAELEAQAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1071 QDQIAELQAQIDELKIQLAKKEEELQAVLARGDEEVAQKNNAlkqlrELQAQLAELQEDLESEKAAR--NKAEKLKRDLS 1148
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAA-----KAQEKVNEALSGIDSDDATSalERMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 528481573 1149 EELEALKT-ELEDTLDTTAAQQELRSKREQEVAELKKAI 1186
Cdd:COG1842 179 ARAEAAAElAAGDSLDDELAELEADSEVEDELAALKAKM 217
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1581-1716 |
6.10e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1581 RDLQARDEQNEEKKRALVKQVREMEAELEDERkqralavaakkklemdLKDVEAQIEAANKARDEAIKQLRKLQAQMKDY 1660
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEE----------------IRRLEEQVERLEAEVEELEAELEEKDERIERL 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1661 QRELEEARTSRDEiftqSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDEL 1716
Cdd:COG2433 447 ERELSEARSEERR----EIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1630-1734 |
6.14e-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: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1630 KDVEAQIEAANKARDEAIKQLrklqaqmKDYQRELEEARTSRDEIFTQSKENEKKLKslEAEILQLQEDLASS-ERARRH 1708
Cdd:cd06503 33 EKIAESLEEAEKAKEEAEELL-------AEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAE 103
|
90 100
....*....|....*....|....*.
gi 528481573 1709 AEQERDELADEISNSASGKAALLDEK 1734
Cdd:cd06503 104 IEQEKEKALAELRKEVADLAVEAAEK 129
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1592-1887 |
6.28e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1592 EKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSR 1671
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1672 DEIFTQSKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASGKaALLDEKRRLEARIAQLEEELEEE 1751
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1752 QSNMELLNdRFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSKLQELEGSVKSKFKAsIAALEAKILqlee 1831
Cdd:COG1340 160 EKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK-ADELHEEII---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 528481573 1832 qleqeakeraAANKIVRRTEKKLKEVFMQVEDERRHADQyKEQMEKANSRMKQLKR 1887
Cdd:COG1340 234 ----------ELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1493-1927 |
6.57e-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: 41.38 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1493 RALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELqatedaklrlEVNM 1572
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDEL----------EKQL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1573 QAMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQ-RALAVAAKKKLEMDLKDVEA---QIEAANKA--RDEA 1646
Cdd:pfam06160 156 AEIEEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyrEMEEEGYAleHLNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1647 IKQLRKLQAQMKDYQRELEEARTsrdeiftqsKENEKKLKSLEAEILQLQEDLASSERARRHAEQERDELADEISNSASG 1726
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLEL---------DEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1727 KAALLDEKRRLeariaqleeeleeeQSNMELLND---RFRKTTMQVDTLNTELAGERSAAQKSENARQQLERQNKDLKSK 1803
Cdd:pfam06160 307 NKELKEELERV--------------QQSYTLNENeleRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1804 LQELEGSVKsKFKASIAALEakilqleeqleqeaKERAAANKIVRRTEKKLKEVFMQVEdeRRH----ADQYKEQMEKAN 1879
Cdd:pfam06160 373 LEEIEEEQE-EFKESLQSLR--------------KDELEAREKLDEFKLELREIKRLVE--KSNlpglPESYLDYFFDVS 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 528481573 1880 SRMKQLKRQLeeaeeeatraNASR---RKLQRELDDATEASEGLSREVNTL 1927
Cdd:pfam06160 436 DEIEDLADEL----------NEVPlnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1236-1465 |
6.89e-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: 41.17 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1236 NKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEG-----EKVKGELADRTHKIQTELDNVSC---------LLED 1301
Cdd:pfam05667 249 LKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSsttdtGLTKGSRFTHTEKLQFTNEAPAAtsspptkveTEEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1302 AEKKGiklTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlleqqeeeeesrKNLEKQLATLQAQlVETKK 1381
Cdd:pfam05667 329 LQQQR---EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEEL--------------EELKEQNEELEKQ-YKVKK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1382 KLeddVGALEGLEEVKRKLQKDMEVTSQKLEE-------------------KAIAFDKLEKTKNRLQ--QELDDLMvdld 1440
Cdd:pfam05667 391 KT---LDLLPDAEENIAKLQALVDASAQRLVElagqwekhrvplieeyralKEAKSNKEDESQRKLEeiKELREKI---- 463
|
250 260
....*....|....*....|....*
gi 528481573 1441 hqRQIVSNLEKKQKKFDQMLAEEKT 1465
Cdd:pfam05667 464 --KEVAEEAKQKEELYKQLVAEYER 486
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1502-1654 |
7.33e-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: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1502 KEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA--TEDAKLRLEVNMQAMKAQF 1579
Cdd:cd22656 109 DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDllTDEGGAIARKEIKDLQKEL 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481573 1580 DrdlQARDEQNEEKKRALvKQVREMEAELEDERKQRALAVAAKKKLEMDLKDVEAQIeaankarDEAIKQLRKLQ 1654
Cdd:cd22656 189 E---KLNEEYAAKLKAKI-DELKALIADDEAKLAAALRLIADLTAADTDLDNLLALI-------GPAIPALEKLQ 252
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1169-1431 |
7.65e-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: 40.56 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1169 QELRSKREQEVAELK--KAIDDETRN--HESQIQEMRQRHGTA-LEEISEQLEQAKRVKGNLEKNKQTLESDNKELTnEV 1243
Cdd:pfam15905 59 LELKKKSQKNLKESKdqKELEKEIRAlvQERGEQDKRLQALEEeLEKVEAKLNAAVREKTSLSASVASLEKQLLELT-RV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1244 KSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVKGELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDT 1323
Cdd:pfam15905 138 NELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1324 QELLQEETRQKLNLSSRIRQLEEEKNNLLEQQEEEEESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKD 1403
Cdd:pfam15905 218 KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE 297
|
250 260
....*....|....*....|....*...
gi 528481573 1404 MEVTSQKLEEkaiafdKLEKTKNRLQQE 1431
Cdd:pfam15905 298 YEEKEQTLNA------ELEELKEKLTLE 319
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1473-1716 |
7.77e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1473 ERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEmedlisskdDVGKNVHELEKSKRTLEQQVEEmRTQLE 1552
Cdd:COG5022 829 EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYL---------QSAQRVELAERQLQELKIDVKS-ISSLK 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1553 E--LEDELQATEdaklrlevnmqaMKAQFDRDLQARDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEM-DL 1629
Cdd:COG5022 899 LvnLELESEIIE------------LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVEsKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1630 KDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARTSRDEIftqsKENEKKLKSLEAEILQLQ--EDLASSERARR 1707
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAL----QESTKQLKELPVEVAELQsaSKIISSESTEL 1042
|
....*....
gi 528481573 1708 HAEQERDEL 1716
Cdd:COG5022 1043 SILKPLQKL 1051
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1472-1721 |
7.86e-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: 40.01 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1472 EERDRAEAEAREKDTKalsMARALDEALEAKEEFERLNKQLRAEMEDLISSKDDVGKNVHELEKskrtLEQQVEEMRTQL 1551
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEE----AEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1552 EELEDELQATEDAKLRLEVNMQAMKAqfdrdlqaRDEQNEEKKRALVKQVREMEAELEDERKQRALAVAAKKKLEMDLKD 1631
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKE--------IAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1632 V-------EAQIEAANKARDEAIKQLRKLQAQMKDYQRELEEArtsrdeiftqskenEKKLKSLEAEILQLQEDLASSER 1704
Cdd:pfam00261 153 VgnnlkslEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFA--------------ERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|....*..
gi 528481573 1705 ARRHAEQERDELADEIS 1721
Cdd:pfam00261 219 KYKAISEELDQTLAELN 235
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
854-1188 |
7.93e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 854 EEEMQAKDEELIKVKERQVKVENELVE--------MERKHQQLLEEKNILAEQLQAETELFAEAEEMRA-RLVAKKQELE 924
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINksineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 925 EILHDLESRVEEEEERNQSLQNEKKKMQSHIqdleeqldeeeaarqklqlekvtaeakIKKMEEDILLLEDQNSKFLKEK 1004
Cdd:PRK01156 569 SWLNALAVISLIDIETNRSRSNEIKKQLNDL---------------------------ESRLQEIEIGFPDDKSYIDKSI 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1005 KLLEDRVGEMTSQLAEEEEKAKNLGKVKNKQEmmmvdleeRLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDEL 1084
Cdd:PRK01156 622 REIENEANNLNNKYNEIQENKILIEKLRGKID--------NYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1085 KIQLAKKEEELQAVLARgdeevaqknnalkqLRELQAQLAELQEDLESEKaarnKAEKLKRDLSEELEALKTELEDTLDT 1164
Cdd:PRK01156 694 KANRARLESTIEILRTR--------------INELSDRINDINETLESMK----KIKKAIGDLKRLREAFDKSGVPAMIR 755
|
330 340
....*....|....*....|....
gi 528481573 1165 TAAQQELRSKREQEVAELKKAIDD 1188
Cdd:PRK01156 756 KSASQAMTSLTRKYLFEFNLDFDD 779
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
1049-1159 |
8.06e-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: 37.66 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1049 EEKTRQELEKAKRkldaettdlqDQIAELQAQIDELKIQLAKKEEELQAVlargDEEVAQKNNALKQLRELQAQLAELQE 1128
Cdd:pfam16516 1 EELKRKEMEKVYK----------DEIDCLQAQLQAAEEALAAKQREIDEL----KQEIAQKEEDLETISVLKAQAEVYRS 66
|
90 100 110
....*....|....*....|....*....|.
gi 528481573 1129 DLESEKAARNKAEKLKRDLSEELEALKTELE 1159
Cdd:pfam16516 67 DFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1199-1520 |
8.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1199 EMRQRHGTALEEISEQLEQAKRVKGNLEKNKQTLESDNKELTNEVKSLQQAKSESEHKRKKLEAQLQEVMARFSEGEKVK 1278
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1279 GELADRTHKIQTELDNVSCLLEDAEKKGIKLTKDVSSLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknNLLEQQEEE 1358
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1359 EESRKNLEKQLATLQAQLVETKKKLEDDVGALEGLEEVKRKLQKDMEVTSQKLEEKAIAFDKLEKTKNRLQQELDDLMVD 1438
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1439 LDHQRQIVSNLEKKQKKFDQMLAEEKTISARYAEERDRAEAEAREKDTKALSMARALDEALEAKEEFERLNKQLRAEMED 1518
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
..
gi 528481573 1519 LI 1520
Cdd:COG4372 335 LL 336
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1537-1691 |
8.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1537 KRTLEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFDRDLQARDEQNEEKKRALVKQVREMEAELED 1610
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1611 ERKQRALAVAAKKKLEMDLKDVEAQIEAANKARDEAIKQLRKLQAQMKDYQRE--LEEAR-TSRDEIFTQSKENEKKLKs 1687
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEeEARHEAAVLIKEIEEEAK- 183
|
....
gi 528481573 1688 LEAE 1691
Cdd:PRK12704 184 EEAD 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
849-1150 |
8.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 849 QVTRQEEEMQAKDEELIKVKERQVKVENELVEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLVAKKQELEEILH 928
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 929 DLESRVEEEEERNQSLQNEKKKMQSHIQDLEEQLDEEEAARQKLQLEKVTAEAKIKKMEEDILLLEDQNSKFLKEKKLLE 1008
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481573 1009 DRVGEMTSQLAEEEEKAKNLGKVKNKQEMMMVDLEERLKKEEKTRQELEKAKRKLDAETTDLQDQIAELQAQIDELKIQL 1088
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528481573 1089 AKKEEELQAVLARGDEEVAQKNNALKQLRELQAQLAELQEDLESEKAARNKAEKLKRDLSEE 1150
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
|
| |
