|
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 ... |
848-1928 |
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: 1434.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 848 TRQEEEMQAKEEEMQKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEM 927
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 928 EARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEER 1007
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1008 VSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAK 1087
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1088 KEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQE 1167
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1168 LRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAK 1247
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1248 QEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEE 1327
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1328 TRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQ 1407
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1408 YEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALS 1487
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1488 LARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEV 1567
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1568 NMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQL 1647
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1648 RKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTL 1727
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1728 QDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGA 1807
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1808 VKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLE 1887
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 241982718 1888 EAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-771 |
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: 1327.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 338
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 339 NEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 419 FAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 499 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTEFSII 578
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 658
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 241982718 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-771 |
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: 1323.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDSSIT-GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYT-FLSNGFVPIPAAQDDEMFQETLEAMSIM 336
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 337 GFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQ 416
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 417 ADFAIEALAKATYERLFRWILSRVNKALDKThRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 497 EEYQREGIEWNFIDFGLDLQPCIELIERPNnpPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPK-FQKPKQLKDKTEF 575
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPN--MGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 576 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtESSLPSASKTKKGMFRTVGQ 655
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 656 LYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA 735
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 241982718 736 IPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
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: 1300.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 339 NEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 419 FAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 499 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTEFSII 578
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 658
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 241982718 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
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: 1209.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDSSIT----GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMS 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 335 IMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTK 414
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 415 EQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 495 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTE 574
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTEsSLPSASKTKKGMFRTVG 654
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 734
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 241982718 735 AIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
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: 1162.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDSsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 339 NEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 419 FAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 499 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTEFSII 578
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 658
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 241982718 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
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: 1139.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDSS----ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMS 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 335 IMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTK 414
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 415 EQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 495 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTE 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTEssLPSASKTKKGMFRTVG 654
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 734
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 241982718 735 AIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
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 ... |
99-771 |
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: 1133.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASS---------HKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 250 FDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQET 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 330 LEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQ 409
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 410 KAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKpKQL 569
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 570 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrIVGLDQMAkMTESSLpsASKTKKGM 649
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF--GARTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 730 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-771 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1129.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 87 VEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 167 QDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKdssiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN----VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 247 RINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSN-GFVPIPAAQDDEM 325
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 326 FQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGR 405
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 406 DVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQK 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 566 PKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVgldqMAKMTESSLPSASKT 645
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAE----SAAANESGKSTPKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 646 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 241982718 726 QRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
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: 1087.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAaQDDEMFQETLEAMSIMGF 338
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 339 NEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 419 FAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 499 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTEFSII 578
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESslPSASKTKKGMFRTVGQLYK 658
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 241982718 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-783 |
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: 1009.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 80 NPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIAD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 160 TAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKkdssitGELEKQLLQANPILEAFGNAKTVKNDNS 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 240 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPA 319
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 320 AQDD-EMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNT-AAQKVCHLVGINVTDFTRAIL 397
Cdd:smart00242 235 GIDDaEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 398 TPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCIN 477
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCSEQ 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 558 GNHPKFQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmakmtes 637
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG--------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 638 slpSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 717
Cdd:smart00242 535 ---VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 718 RIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERD 783
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1462 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 886.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 36 VWVPSEKQGFEAASIKEEKGDEVVVEL---VENGKKVTVGKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLRERYF 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 111 SGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 191 VIQYLAVVASSHkgkkdSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 270
Cdd:COG5022 172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 271 AIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVP-IPAAQDDEMFQETLEAMSIMGFNEEEQLAILKV 349
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 350 VSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATY 429
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 430 ERLFRWILSRVNKALDKTHRQGaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 509
Cdd:COG5022 406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 510 DFgLDLQPCIELIERpNNPPGVLALLDEECWFPKATDKSFVEKLCS--EQGNHPKFQKPKQLKDKteFSIIHYAGKVDYN 587
Cdd:COG5022 485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 588 ASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVgldqmakmtesslpsasktKKGMFRTVGQLYKEQLGKLMTT 667
Cdd:COG5022 561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 668 LRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA----IPKGFMDG 743
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 744 KQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIMAFQAMCRGYLARKAFTKRQQQLTAMKVIQRNC 823
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 824 AAYLKLRNWQWWRLFTKVKPLLQVTrqeeemqakeeemqKIKERQQKAETELKELEQKhtqlAEEKTLLQEQLQAETELY 903
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLL--------------GSRKEYRSYLACIIKLQKT----IKREKKLRETEEVEFSLK 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 904 AEAEEMRVRLAAKKQEL------EEILHEMEARLEEEEDRGQQLQAERKKMAQqmldleeqleeeeAARQKLQLEKVTAE 977
Cdd:COG5022 844 AEVLIQKFGRSLKAKKRfsllkkETIYLQSAQRVELAERQLQELKIDVKSISS-------------LKLVNLELESEIIE 910
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 978 AKIKKLEDDILVMDDQNSKLSKERKLLEER--VSDLTTNLAEEEEKAKNLTKLKSKHESmISELEVRLKKEE-------K 1048
Cdd:COG5022 911 LKKSLSSDLIENLEFKTELIARLKKLLNNIdlEEGPSIEYVKLPELNKLHEVESKLKET-SEEYEDLLKKSTilvregnK 989
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1049 SRQELEKLKRKLEGdasdFHEQIADLQAQIAELKmQLAKKEEELQAALARLDEEIAQKNNaLKKIRELEGHISDLQEDLd 1128
Cdd:COG5022 990 ANSELKNFKKELAE----LSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTELSI-LKPLQKLKGLLLLENNQL- 1062
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1129 serAARNKAEKQKRDLGEELEALKTELEDT--LDSTATQQELRAKREQevTVLKKALDEETRSheaqvQEMRQKHTQAVE 1206
Cdd:COG5022 1063 ---QARYKALKLRRENSLLDDKQLYQLESTenLLKTINVKDLEVTNRN--LVKPANVLQFIVA-----QMIKLNLLQEIS 1132
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1207 ELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGE-------------- 1272
Cdd:COG5022 1133 KFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEvndlknelialfsk 1212
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1273 -RARAELSDKVHKLQNEVESVTGM---LNEAEGKAIKLA----KDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDE 1344
Cdd:COG5022 1213 iFSGWPRGDKLKKLISEGWVPTEYstsLKGFNNLNKKFDtpasMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQY 1292
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1345 RNSLQDQL------DEEMEAKQNLERHVSTL-----NIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAA 1413
Cdd:COG5022 1293 INVGLFNAlrtkasSLRWKSATEVNYNSEELddwcrEFEISDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPA 1372
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1414 AYDKLEKTKNRLQQE-------LDDLVVDLDNQRQLVSNLEKK--QKKFDQLLAEEKN 1462
Cdd:COG5022 1373 EIQNLKSRYDPADKEnnlpkeiLKKIEALLIKQELQLSLEGKDetEVHLSEIFSEEKS 1430
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-771 |
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: 885.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAVVASSHKGKKDSSiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFL-----SNGFVPIPAAQDDEMFQETLEA 332
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 333 MSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNT--DQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQK 410
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 411 AQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQ-GASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQl 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 570 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfvadlwkdvdrivgldqmakmtesslpsasktkkgm 649
Cdd:cd00124 476 KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 650 frtvgqlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 730 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-771 |
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: 789.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVAS-----SHKGKKDSSITG-ELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdgpGKKAQFLATKTGgTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKsDLLLESFNSYT--FLSNGFVPIPAAQDDEMFQETL 330
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNPYDyhFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 331 EAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQK 410
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 411 AQTKEQADFAIEALAKATYERLFRWILSRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKP-- 566
Cdd:cd14927 398 HMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrp 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 567 -KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKmtESSLPSASKT 645
Cdd:cd14927 475 dKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDSTED--PKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 646 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14927 550 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 241982718 726 QRYEILAANAIPK-GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-771 |
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: 774.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVASSH--KGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMkSDLLLESFNSYT--FLSNGFVPIPAAQDDEMFQETLEAMSI 335
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 336 MGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTK 414
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 415 EQADFAIEALAKATYERLFRWILSRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKDK 572
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVVKGR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGldqmakmtESSLPSASKTKKGMF 650
Cdd:cd14913 475 AEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADA--------DSGKKKVAKKKGSSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14913 547 QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14913 627 LNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-771 |
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: 755.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLL-ESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 418 DFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 498 EYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLK---DKT 573
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslpSASKTKKGMFRTV 653
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAK-------GGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 241982718 734 NAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
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 ... |
99-771 |
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: 745.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASShkGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAK-EKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 418 DFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 498 EYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKDK---T 573
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkdvdriVGLDQMAKMTESSLPSASKTKKGM-FRT 652
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 241982718 733 ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-771 |
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: 714.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDssiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK---LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEkmKSDLLLESFN--SYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 336
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 337 GFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQ 416
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 417 ADFAIEALAKATYERLFRWILSRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14929 316 VTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 496 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKDKTE 574
Cdd:cd14929 394 QEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKFE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 575 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLW-KDVdrivgldqmakMTESSLPSASKT-KKGM- 649
Cdd:cd14929 471 ahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFeNYI-----------STDSAIQFGEKKrKKGAs 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14929 540 FQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYC 619
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 241982718 730 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14929 620 ILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-771 |
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: 712.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSG-LIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASShkgkkdSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS------SSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVP-IPAAQDDEMFQETLEAMSIMG 337
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 418 DFAIEALAKATYERLFRWILSRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 497 EEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPK--FQKPKQlkDKTE 574
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRF--SNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNassdkfvadlwkdvdrivgldqmakmtesslpsASKTKKgmfRTVG 654
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLK---------------------------------ASKNRK---KTVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaan 734
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL--- 590
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 241982718 735 aIPKGF---MDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01380 591 -LPSKEwlrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-771 |
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: 698.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVAS-SHKGKKDSSI-TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQTPgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMkSDLLLESFN--SYTFLSNGFVPIPAAQDDEMFQETLEAMSI 335
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 336 MGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTK 414
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 415 EQADFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 495 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKDKT 573
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKP 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 574 E--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKmtesslPSASKTKKG-MF 650
Cdd:cd14917 476 EahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGADAPIE------KGKGKAKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14917 547 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14917 627 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-771 |
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: 697.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 101 VLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 181 GAGKTENTKKVIQYLAVVASSHKGKKDSS--ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFN-SYTFLSNGFVPIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQ 416
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 417 ADFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 497 EEYQREGIEWNFIDFGLDLQPCIELIERpnnPPGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKDKTE- 574
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEK---PLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVVKGKAEa 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 575 -FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqMAKMTESSLPSASKTKKGMFRTV 653
Cdd:cd14918 478 hFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14918 550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 241982718 734 NAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14918 630 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
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: 690.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVASSHKGKKD---SSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 257 VGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMkSDLLLESFNSYT--FLSNGFVPIPAAQDDEMFQETLEAMS 334
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 335 IMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQT 413
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 414 KEQADFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKDK 572
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslPSASKTKKGMF 650
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGS------KKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-771 |
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: 688.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVASSHKGKKDS----SITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFN-SYTFLSNGFVPIPAAQDDEMFQETLEAMS 334
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 335 IMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQT 413
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 414 KEQADFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKDK 572
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKKGMF 650
Cdd:cd14910 477 VEahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA-------AAAEAEEGGGKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14910 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-771 |
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: 687.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVAS-SHKGKKD--SSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 257 VGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMkSDLLLESFN--SYTFLSNGFVPIPAAQDDEMFQETLEAMS 334
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 335 IMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQT 413
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 414 KEQADFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKDK 572
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKKGMF 650
Cdd:cd14916 476 QEahFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSSF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-771 |
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: 685.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVASSHKGKKDS----SITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFN-SYTFLSNGFVPIPAAQDDEMFQETLEAMS 334
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 335 IMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQT 413
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 414 KEQADFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKDK 572
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVVKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGldqmaKMTESSLPSASKTKKGMF 650
Cdd:cd14912 477 AEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG-----ASAGGGAKKGGKKKGSSF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14912 552 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14912 632 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
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: 681.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVASSHKGKKDSSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMkSDLLLESFNSYTF--LSNGFVPIPAAQDDEMFQETLEAM 333
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 334 SIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQ 412
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 413 TKEQADFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 493 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCSEQ-GNHPKFQKPKQLKD 571
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 572 KTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivglDQMAKMTESSLPSASKTKKGM 649
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 241982718 730 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-771 |
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: 667.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVASSHKgkkdssitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 260 NIETYLLEKSRAIRQARDERTFHIFYYLLAGAKE--KMKSDLLLESFNSYTFLS-NGFVPIPAAQDDEMFQETLEAMSIM 336
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 337 GFNEEEQLAILKVVSSVLQLGNIVFKK-ERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKE 415
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 416 QADFAIEALAKATYERLFRWILSRVNKALDK---THRqgasFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPgqkNSR----FIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 493 ILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDK 572
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 573 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVD--RIVGLDQMAKMTESSlpsaSKTKKGMf 650
Cdd:cd14883 466 TEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDllALTGLSISLGGDTTS----RGTSKGK- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 241982718 731 LAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14883 621 LDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-771 |
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: 653.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVASSHKGkkdssitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 260 NIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLS-NGFVPIPAAQDDEMFQETLEAMSIMGF 338
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 339 NEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 419 FAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 499 YQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKpkqlKDKTEFSII 578
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----ERGGAFTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLwkdvdRIVGLDQMAKMTESSLPSASKTKKgmfRTVGQLYK 658
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF-----ASKMLDASRKALPLTKASGSDSQK---QSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIpK 738
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-S 614
|
650 660 670
....*....|....*....|....*....|...
gi 241982718 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01383 615 ASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-771 |
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: 651.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVASSHkgkkDSSItGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS----ESEV-ERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 260 NIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEM-FQETLEAMSIMGF 338
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAAdFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 339 NEEEQLAILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVG---RDVVQKAQTKE 415
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 416 QADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 496 QEEYQREGIEWNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWFP-KATDKSFVEKLCSEQGNHPKFQKPKQLKD--K 572
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 573 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakmtesslpsaSKTKKGMFRT 652
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV-------------------DLDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 241982718 733 ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-771 |
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: 622.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAvvassHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA-----YMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFL--SNGFvPIPAAQDDEMFQETLEAMSI 335
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 336 MGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPD---NTAAQKVCHLVGINVTDFTRAiLTPRIKVGRD-VVQKA 411
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 412 QTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 492 FILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKqlKD 571
Cdd:cd01384 393 FKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 572 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtesslpsaSKTKKGM-F 650
Cdd:cd01384 468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------------EGTSSSSkF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd01384 530 SSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 241982718 731 LAANAiPKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd01384 610 LAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-771 |
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: 612.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHkgkkdSSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQH-----SWI----EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNG-FVPIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKK--ERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKE 415
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 416 QADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFL--GILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSRTsiGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 494 LEQEEYQREGIEWNFIDFgLDLQPCIELI-ERPNNppgVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDK 572
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 573 TeFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkDVDRIVGLDqmakmtesslpSASKTKkgmfrT 652
Cdd:cd01381 468 S-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TRKKSP-----T 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd01381 530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 241982718 733 ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01381 610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-771 |
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: 590.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAVVASSHkgkkdssiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG--------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLesfnsytflsngfvpIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNT-------DQASMPDNTAAQKvchLVGINVTDF-----TRAILTPRIKVGR 405
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 406 DVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALdkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 485
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCI--PFETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 486 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQK 565
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 566 P--------KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkdvdrivgldqmAKMTES 637
Cdd:cd01382 450 PrksklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF------------ESSTNN 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 638 SLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 717
Cdd:cd01382 518 NKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 241982718 718 RIVFQEFRQRYEILAANAIPKgfMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
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 ... |
99-771 |
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: 572.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASShkgkkdssiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS---------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKekMKSDLLLESFNSYTFLS-NGFVPIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASPD--PASRGGWGSSAAYGYLSlSGCIEVEGVDDVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNTDQAS---MPDNTAAQKVCHLVGINVTDFTRAILTPRIKV-GRDVVQKAQT 413
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 414 KEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14872 310 PAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 494 LEQEEYQREGIEWNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKT 573
Cdd:cd14872 390 LEEALYQSEGVKFEHIDF-IDNQPVLDLIE--KKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFvadlwkdvdrivgldqMAKMTESSLPSaSKTKKGmfrTV 653
Cdd:cd14872 467 EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKL----------------IAVLFPPSEGD-QKTSKV---TL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14872 527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK 606
|
650 660 670
....*....|....*....|....*....|....*....
gi 241982718 734 nAIPKGFM-DGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14872 607 -TIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-771 |
0e+00 |
|
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: 564.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 174 ILCTGESGAGKTENTKKVIQYLAVVASSHKGKK----------DSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGAsgegeaaseaIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 244 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDD 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 324 EMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASmpDNTAAQ---KVCHLVGINVTDFTRAILTPR 400
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQslkLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 401 IKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTN 480
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 481 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIE-RPNNPPGVLALLDeECWFPKAT--DKSFVEKL---- 553
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 554 ---------CSEQGNHPKFQKPKQLKDKtEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkdvdr 624
Cdd:cd14890 476 grksgsggtRRGSSQHPHFVHPKFDADK-QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 625 ivgldqmakmteSSLPSASktkkgmfrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGV 704
Cdd:cd14890 542 ------------RSIREVS---------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 705 LEGIRICRQGFPNRIVFQEFRQRYEILAANAipkgfMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-771 |
2.41e-174 |
|
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: 546.97 E-value: 2.41e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLavVASSHKGKKDSsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGSG-----VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLsNGFVPIPAAQDDEM--FQETLEAMSIM 336
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYL-NQSDCYTLEGEDEKyeFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 337 GFNEEEQLAILKVVSSVLQLGNIVFKKER-NTDQASMPDNTAAQK-VCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTK 414
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 415 EQADFAIEALAKATYERLFRWILSRVNKAL----DKTHRQGASfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPkQLK 570
Cdd:cd01385 392 IFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 571 DkTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLwkdvdriVGLD---------------QMAKMT 635
Cdd:cd01385 468 E-PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDpvavfrwavlraffrAMAAFR 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 636 ESSLPSASKT-------------------KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVL 696
Cdd:cd01385 540 EAGRRRAQRTaghsltlhdrttksllhlhKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVL 619
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 697 EQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaanaIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01385 620 RQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-771 |
4.82e-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: 545.12 E-value: 4.82e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASShkgkKDSSITgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR----RNNLVT----EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNG-FVPIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNTDQ---ASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTK 414
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 415 EQADFAIEALAKATYERLFRWILSRVN----KALDKTHRqgasfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNaivySGTQDTLS-----IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQlk 570
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 571 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldQMAKMTESSLPSASK----TK 646
Cdd:cd01387 462 PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPRLGKgrfvTM 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 647 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd01387 533 KPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFID 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 241982718 727 RYEILAANAIPKGfMDGKQACILMIKALELDP-NLYRIGQSKIFFR 771
Cdd:cd01387 613 RYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-771 |
7.16e-173 |
|
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: 542.06 E-value: 7.16e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAVVASshkGKKDSSItgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFlSNGFVPIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALSLIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASM--PDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKE 415
Cdd:cd14903 232 VSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 416 QADFAIEALAKATYERLFRWILSRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14903 312 QAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 496 QEEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCS---EQGNHPKFQKpkqlKDK 572
Cdd:cd14903 391 QIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLSSihkDEQDVIEFPR----TSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 573 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrIVGLDQMAKMTESSLPSASKTKKGMFRT 652
Cdd:cd14903 463 TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALTTTT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd14903 540 VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 241982718 733 ANAiPKGFMDGKQACILMIKALELD-PNLYRIGQSKIFFR 771
Cdd:cd14903 620 PEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-771 |
6.02e-172 |
|
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: 538.51 E-value: 6.02e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKK-RHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAvvasshkgKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLM--------KLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDE-------MFQETL 330
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEeleyyrqMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 331 EAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQK 410
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 411 AQTKEQADFAIEALAKATYERLFRWILSRVNKAL----DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 486
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 487 FNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKP 566
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 567 KqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldqmakmtesslpsasktk 646
Cdd:cd14897 470 P--GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 647 kgmfrtvgQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14897 522 --------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 241982718 727 RYEILAANAiPKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-769 |
1.26e-169 |
|
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: 532.83 E-value: 1.26e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMY------KGKKRHEMPPHIYAIADTAYRSMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 171 --DQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 249 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFL--SNGFVPIPAAQDDEMF 326
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 327 QETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVF-KKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGR 405
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 406 DVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGAS-FLGILDIAGFEIFEVNSFEQLCINYTNEKLQ 484
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 485 QLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNH 560
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEA--RPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 561 PKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADlwkdvdrivgldqmakmtesslp 640
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 641 sasktkkgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 721 FQEFRQRYEILAANAIPKGFMDGKQACILMIKA------LELDPNLYrIGQSKIF 769
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-732 |
1.81e-168 |
|
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: 530.42 E-value: 1.81e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKgKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAVVASSHKGKKDSsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVT---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL-----VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 254 -----GYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVP------------ 316
Cdd:cd14888 155 msgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 317 ------------IPAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQ---KV 381
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 382 CHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIA 461
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 462 GFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWF 541
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 542 PKATDKSFVEKLCSEQGNHPKFQKPKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 622 -VDRIVGldqmakmtesslpsaSKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLR 700
Cdd:cd14888 550 yLRRGTD---------------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|..
gi 241982718 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL 646
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-771 |
2.48e-168 |
|
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: 529.37 E-value: 2.48e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAVVASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLS-NGFVPIPAAQDDEMFQETLEAMSIM 336
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 337 GFNEEEQLAILKVVSSVLQLGNIVFKkerNTDQASMPDNTAAQKVCHLVGINVTDFTRAiLTPRIKVGR-DVVQKAQTKE 415
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 416 QADFAIEALAKATYERLFRWILSRVNKALDKthRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRIKG--KEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 496 QEEYQREGIEWNFIDFgLDLQPCIELIERpnnPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQlkDKTEF 575
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEK---KLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRV--AVNNF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 576 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmAKMTESSLPSASKTKKgmfRTVGQ 655
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSKHRR---PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 656 LYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA 735
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 241982718 736 IPKGFMDGKqaCILMIKALELDPNLYRIGQSKIFFR 771
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 ... |
100-771 |
3.74e-167 |
|
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: 525.30 E-value: 3.74e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVasshkGKKDssiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKAN---NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 260 NIETYLLEKSRAIRQARDERTFHIFYYLLAG--AKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDD---EMFQETLEAMS 334
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGlaEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 335 IMGFNEEEQLAILKVVSSVLQLGNIVFK---KERNTDQASM-PDNTAAQKVCHLVGINVTDFTRAiLTPRIKVGR-DVVQ 409
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADELQEA-LTSHSVVTRgETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 410 KAQTKEQADFAIEALAKATYERLFRWILSRVNKAL--DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 487
Cdd:cd01379 313 RNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 488 NHTMFILEQEEYQREGIEWNFIDFG-----LDLqpcieLIERPNnppGVLALLDEECWFPKATDKSFVEKLcseQGN--H 560
Cdd:cd01379 393 NQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPM---GLLALLDEESRFPKATDQTLVEKF---HNNikS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 561 PKFQKPKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVadlwkdvdrivgldqmaKMTESSlp 640
Cdd:cd01379 462 KYYWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-----------------RQTVAT-- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 641 sasktkkgMFRtvgqlY--KEQLGKLMTtlrnTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNR 718
Cdd:cd01379 521 --------YFR-----YslMDLLSKMVV----GQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHR 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 719 IVFQEFRQRYEILA--ANAIPKGfmdGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd01379 584 ILFADFLKRYYFLAfkWNEEVVA---NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-771 |
1.95e-163 |
|
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: 516.23 E-value: 1.95e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEM---PPHIYAIADTAYRSMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 172 QSILCTGESGAGKTENTKKVIQYLAV----VASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATasklAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 248 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNG-FVPIPAAQDDEMF 326
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 327 QETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFkkERNTDQ----ASMPDNTAAQKVCHLVGINVTDFTRAILTPRIK 402
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 403 VGR-DVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQ---------GASFLGILDIAGFEIFEVNSFE 472
Cdd:cd14892 319 TARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFP-KATDKSFVE 551
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 552 KLCSEQ-GNHPKFQKPKQLKDktEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfvadlwkdvdrivgldq 630
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 631 makmtesslpsasktkkgmFRTvgqlykeQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRI 710
Cdd:cd14892 536 -------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 711 CRQGFPNRIVFQEFRQRYEILAAN-AIPKGFMDGKQACILMIKALE-----LDPNLYRIGQSKIFFR 771
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-771 |
4.80e-151 |
|
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: 482.48 E-value: 4.80e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 101 VLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 177 TGESGAGKTENTKKVIQYLAVVASSHKgkkdssitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 257 VGANIETYLLEKSRAIRQARDERTFHIFYYLLAG--AKEKMKSDLLLESFnsYTFLSNGFvpipaAQDDEM------FQE 328
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA-----GCKREVqywkkkYDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 329 TLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFkkERNTDQASMPDNTA---AQKVCHLVGINVTDFTRAiLTPRIKVGR 405
Cdd:cd14889 226 VCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSngwLKAAAGQFGVSEEDLLKT-LTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 406 -DVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQG--ASFLGILDIAGFEIFEVNSFEQLCINYTNEK 482
Cdd:cd14889 303 gEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 483 LQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIerPNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPK 562
Cdd:cd14889 383 LQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 563 FQKPKQLKDKteFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWK-DVDRIVGLDQMAKMTESSLPS 641
Cdd:cd14889 460 YGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLPQAGSDN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 642 ASKTKKgmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVF 721
Cdd:cd14889 538 FNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 241982718 722 QEFRQRYEILAANAIPKGfmdGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14889 615 AEFAERYKILLCEPALPG---TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-734 |
3.06e-149 |
|
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: 477.60 E-value: 3.06e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKRH--------EMPPHIYAIADTAYRSMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 170 EDQSILCTGESGAGKTENTKKVIQYLaVVASSHKGKKDSSITGE------------LEKQLLQANPILEAFGNAKTVKND 237
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFL-TQLSQQEQNSEEVLTLTssiratskstksIEQKILSCNPILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 238 NSSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLE---SFNSYTFLS-N 312
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlSGDRYDYLKkS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 313 GFVPIPAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQA--SMPDNTAAQKVCHLVGINVT 390
Cdd:cd14907 240 NCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 391 DFTRAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKAL------DKTHRQGASF-LGILDIAGF 463
Cdd:cd14907 320 ELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 464 EIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWF 541
Cdd:cd14907 400 EVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLD--KPPIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 542 PKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTeFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkd 621
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF-- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 622 vdriVGLDQMAKMTESSLPSASKTKKgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRC 701
Cdd:cd14907 554 ----SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670
....*....|....*....|....*....|...
gi 241982718 702 NGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 734
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-771 |
1.86e-144 |
|
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: 463.36 E-value: 1.86e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERyfSGLI----YTYSGLFCVVVNPYKYLPiysEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 172 QSILCTGESGAGKTENTKKVIQYL---AVVASSHKG-------KKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSR 241
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttrAVGGKKASGqdieqssKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 242 FGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLS-NGFVPIPA 319
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 320 AQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKK----ERNTDQASMPDNTAAQKVCHLVGINVTDFTRA 395
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 396 ILTPRIkVGRDVVQKAQ-TKEQADFAIEALAKATYERLFRWILSRVNKALDKtHRQGASFLGILDIAGFEIFE-VNSFEQ 473
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFEtKNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 474 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELI-ERPNnppGVLALLDEECWFPKATDKSFVEK 552
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPN---GILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 553 LCSEQGNHPKFQKPKQlKDKTE-FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLnASSDKFvadlwkdvdrivgLDQM 631
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLL-ASSAKF-------------SDQM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 632 AkmtesslpsasktkkgmfrtvgqlykeqlgKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRIC 711
Cdd:cd14891 535 Q------------------------------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 712 RQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIK-ALELDPNLYRIGQSKIFFR 771
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-737 |
2.44e-139 |
|
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: 448.60 E-value: 2.44e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMY-----------KGKKRHEMPPHIYAIADTAYRSM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAVV------ASSHKGKKDSSITGelekQLLQANPILEAFGNAKTVKND 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSGIAA----KVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 238 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEkmksdlllesfnsytflsngfvpi 317
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE------------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 318 pAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTD-QASMPDNTAAQKV------CHLVGINVT 390
Cdd:cd14900 214 -AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 391 DFTRAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALD----KTHRQGASFLGILDIAGFEIF 466
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmddsSKSHGGLHFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 467 EVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKATD 546
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISQ--RPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 547 KSFVEKLCSEQGNHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVtsllnassdkfvadlwkdVDriv 626
Cdd:cd14900 450 TTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEA------------------VD--- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 627 gldqmakmtesslpsasktkkgMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLE 706
Cdd:cd14900 509 ----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660 670
....*....|....*....|....*....|.
gi 241982718 707 GIRICRQGFPNRIVFQEFRQRYEILAANAIP 737
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-771 |
4.20e-139 |
|
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: 450.94 E-value: 4.20e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPiyseKIVDMYKgkKRHEMP------PHIYAIADTAYRSMLQ------ 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP----GLYDLHK--YREEMPgwtalpPHVFSIAEGAYRSLRRrlhepg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 168 -DREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDSS----ITGElekQLLQANPILEAFGNAKTVKNDNSSRF 242
Cdd:cd14895 76 aSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKrrraISGS---ELLSANPILESFGNARTLRNDNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 243 GKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTF--LSNG-- 313
Cdd:cd14895 153 GKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFqyISGGqc 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 314 FVPIPAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERntDQASMPDNTAAQKVCHLVGINVTDFT 393
Cdd:cd14895 233 YQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASS--EDEGEEDNGAASAPCRLASASPSSLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 394 --------------------RAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDK------- 446
Cdd:cd14895 311 vqqhldivsklfavdqdelvSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfalnp 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 447 ---THRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIELIE 523
Cdd:cd14895 391 nkaANKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 524 RpnNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNV 603
Cdd:cd14895 470 Q--RPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 604 TSLLNASSDKFVADLWKDVDRIVGldqmAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNH 683
Cdd:cd14895 548 FSVLGKTSDAHLRELFEFFKASES----AELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 684 EKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELdpnlyri 763
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------- 696
|
....*...
gi 241982718 764 GQSKIFFR 771
Cdd:cd14895 697 GKTRVFLR 704
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-728 |
1.76e-137 |
|
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: 446.65 E-value: 1.76e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYK--------GKKRHEMPPHIYAIADTAYRSMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 169 REDQSILCTGESGAGKTENTKKVIQYLAVV-ASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 248 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSN---GFVPIPAAQDD- 323
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKRAVADKy 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 324 -EMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKE-RNTDQASMPDNTAAQ--KVCHLVGINVTDFTRAILTP 399
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 400 RIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALD--------KTHRQGASFLGILDIAGFEIFEVNSF 471
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 472 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVE 551
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFD--DKSNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 552 KLCSEQGNhpkfqkpkqlkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfvadlwkDVDRIVGLDQM 631
Cdd:cd14902 478 KFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 632 AKMTESSLPSASKTKKGMFRT--VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIR 709
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650
....*....|....*....
gi 241982718 710 ICRQGFPNRIVFQEFRQRY 728
Cdd:cd14902 618 IARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-771 |
2.74e-137 |
|
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: 444.00 E-value: 2.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAVVASshkGKKDSSITgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFL--SNGFVPIPAAQDDEMFQETLEAMSI 335
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 336 MGFNEEEQLAILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKVCHLVGINVTDF-----TRAILT--PRIKVGRDVV 408
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIeealcNRSVVTrnESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 409 QKAQTKeqadfaiEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 488
Cdd:cd14904 312 EAEENR-------DALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 489 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKL---CSEQGNHPKFQK 565
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 566 PKQlkDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakMTESSLPSASKT 645
Cdd:cd14904 461 PKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----------APSETKEGKSGK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 646 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14904 529 GTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELA 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 241982718 726 QRYEILAANAIPKGfmDGKQACILMIKAL-ELDPNLYRIGQSKIFFR 771
Cdd:cd14904 609 TRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-771 |
2.30e-136 |
|
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: 442.52 E-value: 2.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVAsshkGKKDSSITGElekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAA----GSVGGVLSVE---KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSytflSNGFVPIPAAQDDEM------FQETLEA 332
Cdd:cd01386 154 ASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 333 MSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAI------------LTPR 400
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 401 IKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLgILDIAGFEifevN----------S 470
Cdd:cd01386 310 GQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGFQ----NpahsgsqrgaT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 471 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPN------------NPPGVLALLDEE 538
Cdd:cd01386 385 FEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdeDRRGLLWLLDEE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 539 CWFPKATDKSFVEKLCSEQG--NHPKFQKPKQLKDKT-EFSIIHYAGK--VDYNASAWLTK-NMDPLNDNVTSLLNASSD 612
Cdd:cd01386 465 ALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 613 KFVAdlwkdvdrivgldqmakmtesslpsasKTKKGMFRTVgqlyKEQLGKLMTTLRNTTPNFVRCIIPNH--EKRSGK- 689
Cdd:cd01386 545 ETAA---------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERSt 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 690 ---------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGF-----MDGKQACILMIKALE 755
Cdd:cd01386 594 sspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELD 673
|
730
....*....|....*.
gi 241982718 756 LDPNLYRIGQSKIFFR 771
Cdd:cd01386 674 LEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-771 |
4.51e-135 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 437.29 E-value: 4.51e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLavvaSSHKGKKDSSITGELEKQLlqanPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL----SSLYQDQTEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFV-PIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNTDQ--ASMPDNTAAQKVCHLVGINvTDFTRAILTPRIKV-GRDVVQKAQTK 414
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 415 EQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 494 LEQEEYQREGIEWNFIDfGLDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQlkDKT 573
Cdd:cd14896 391 QEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslpsasktkkgmfrTV 653
Cdd:cd14896 466 VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------------TL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS 607
|
650 660 670
....*....|....*....|....*....|....*...
gi 241982718 734 NAIPkGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14896 608 ERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
64-814 |
1.89e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 439.08 E-value: 1.89e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 64 ENGKKVTVGKDDIQKMNPP-KFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMY 142
Cdd:PTZ00014 74 PTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 143 KGKKRHE-MPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAvvaSSHKGKKDSSItgelEKQLLQA 221
Cdd:PTZ00014 154 RDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 222 NPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLL 301
Cdd:PTZ00014 227 NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 302 ESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVF--KKERNTDQASM--PDNTA 377
Cdd:PTZ00014 307 KSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 378 A-QKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKThrQG-ASFL 455
Cdd:PTZ00014 387 VfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPP--GGfKVFI 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 456 GILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALL 535
Cdd:PTZ00014 465 GMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSIL 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 536 DEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKtEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFV 615
Cdd:PTZ00014 542 EDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLV 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 616 ADLWKDVdrivgldqmaKMTEsslpsaSKTKKGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLV 695
Cdd:PTZ00014 621 RDLFEGV----------EVEK------GKLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKV 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 696 LEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFF-RTGV 774
Cdd:PTZ00014 683 LIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkKDAA 762
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 241982718 775 --LAHLEEERDLKITDVIMAFQAMCRGYLARKAFTKRQQQLT 814
Cdd:PTZ00014 763 keLTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNIKSLV 804
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-757 |
2.72e-132 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 430.87 E-value: 2.72e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYK--GKKRHE-------MPPHIYAIADTAYRSMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 169 REDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDSSitGELEK-----QLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEG--EELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 244 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKS--------DLLLESFNSYTFLSNGFV 315
Cdd:cd14908 159 KFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 316 P-IPAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQK----VCHLVGINVT 390
Cdd:cd14908 239 PdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 391 DFTRAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGA-SFLGILDIAGFEIFEVN 469
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 470 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFP-KATDKS 548
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDAN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 549 FVEKL--------CSEQGNHPKFQKPKQLKDKTEFSIIHYAGKVDYNA-SAWLTKNMDPLndnvtsllnassdkfvadlw 619
Cdd:cd14908 475 YASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI-------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 620 kdvdrivgldqmakmtesslpsaSKTKKGMFRTvGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQL 699
Cdd:cd14908 535 -----------------------PLTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 241982718 700 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnAIPK----GFMDGKQACILMIKALELD 757
Cdd:cd14908 591 RYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKD 651
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-769 |
1.20e-127 |
|
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: 416.70 E-value: 1.20e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAvvaSSHKGKKDSSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKErntDQASMPDntAA----------QKVCHLVGINVTDFTRAILTPRIKVGRDV 407
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 408 VQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGAsFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 487
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 488 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFqKPK 567
Cdd:cd14876 388 IDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 568 QLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmaKMTesslpsASKTKK 647
Cdd:cd14876 464 KVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV----------VVE------KGKIAK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 648 GMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 727
Cdd:cd14876 528 GSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQ 605
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 728 YEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIF 769
Cdd:cd14876 606 FKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-767 |
1.19e-119 |
|
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: 396.27 E-value: 1.19e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKR-HEMPPHIYAIADTAYRSMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 177 TGESGAGKTENTKKVIQYLAVVASS--HKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 255 YIV-GANIETYLLEKSR-AIRQARDERTFHIFYYLLAGAKEKMKSDLLLES-FNSYTFL--------------SNGFVPI 317
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 318 PAAQD-DEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQAS--MPDNTAA-QKVCHLVGINVTDFT 393
Cdd:cd14906 241 NNKTEsIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 394 RAILTPRIKVG---------RDVVQKAQTKEqadfaieALAKATYERLFRWILSRVNKALDK----------THRQGASF 454
Cdd:cd14906 321 QALLNRNLKAGgrgsvycrpMEVAQSEQTRD-------ALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 455 LGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLAL 534
Cdd:cd14906 394 IGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 535 LDEECWFPKATDKSFVEKlCSEQgNHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKF 614
Cdd:cd14906 471 LDDECIMPKGSEQSLLEK-YNKQ-YHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 615 VADLWkdvdrivgldqmaKMTESSLPSASKTKKGMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFL 694
Cdd:cd14906 549 KKSLF-------------QQQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVH 614
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 695 VLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSK 767
Cdd:cd14906 615 VLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-732 |
5.22e-118 |
|
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: 389.59 E-value: 5.22e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKR-HEMPPHIYAIADTAYRSMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 175 LCTGESGAGKTENTKKVIQYLAVVASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGfvpiPAAQDDEMFQETLEAMS 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 335 IMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKV---CHLVGINVTDFTRAILTPRIKVGRD--VVQ 409
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVrtsALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 410 KAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 490 TMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKS-FVEKLCSEQGNHPKFQKPKq 568
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGNPCLGHNK- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 569 LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtESSLPSASKTKKG 648
Cdd:cd14880 473 LSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSRA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 649 MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14880 542 PVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERY 621
|
....
gi 241982718 729 EILA 732
Cdd:cd14880 622 KLLR 625
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-771 |
1.77e-113 |
|
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: 376.84 E-value: 1.77e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERyFSGLIYTYS--GLFCVVVNPYKYLPIYSEKIVDMY-KGKKRHEMPPHIYAIADTAYRSM-LQDREDQSI 174
Cdd:cd14875 1 ATLLHCIKER-FEKLHQQYSlmGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 175 LCTGESGAGKTENTKKVIQYLAVVASSHKGK-KDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-V 252
Cdd:cd14875 80 VISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDL-LLESFNSY-------TFLSNGfVPIPAAQDDE 324
Cdd:cd14875 160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYkclnggnTFVRRG-VDGKTLDDAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 325 MFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLVGINVTDFTRAILtprIKVG 404
Cdd:cd14875 239 EFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 405 RDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALD-KTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKL 483
Cdd:cd14875 315 TSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 484 QQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCSEQGN-HPK 562
Cdd:cd14875 395 QNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKRT--GIFSMLDEECNFKGGTTERFTTNLWDQWANkSPY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 563 FQKPKQLKdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkdvdrivgldqmakmteSSLPSA 642
Cdd:cd14875 472 FVLPKSTI-PNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL-----------------STEKGL 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 643 SKTKKgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 722
Cdd:cd14875 534 ARRKQ----TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIE 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 723 EF-RQRYEILAANAIpKGFMDGK--QACILMIKALE-----LDPNlYRIGQSKIFFR 771
Cdd:cd14875 610 QFcRYFYLIMPRSTA-SLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-771 |
8.30e-111 |
|
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: 368.45 E-value: 8.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKRH-----EMPPHIYAIADTAYRSMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 173 SILCTGESGAGKTENTKKVIQYLAVVASSHkgkkdssiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS--------STDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNG-FVPIPAAQDDEMFQETLE 331
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASkCYDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 332 AMSIMgFNEEEQLAILKVVSSVLQLGNIVFKKERN--TDQASMPDNTAA-QKVCHLVGINVTDFTRAILTPRIKVGRDVV 408
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 409 QKAQTKEQADFAIEALAKATYERLFRWILSRVNKALdKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 488
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 489 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKlCSEQGNHPKF--QKP 566
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSS-CKSKIKNNSFipGKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 567 KQLKdkteFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVadlwkdvdrivgldqmaKMTESSLPSASKTK 646
Cdd:cd14886 467 SQCN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV-----------------NKAFSDIPNEDGNM 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 647 KGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14886 526 KGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFH 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 241982718 727 RYEILA--ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14886 604 RNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-728 |
3.39e-108 |
|
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: 363.26 E-value: 3.39e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMY----------KGKKRHEMPPHIYAIADTAYRSMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 168 DREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDSSITGE---------LEKQLLQANPILEAFGNAKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 239 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAG-----AKEKMKSDLLLESFNSYTFLSN 312
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 313 GFVPI--PAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVF-----KKERNT--DQASMPDNTAA----- 378
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 379 QKVCHLVGINVTDFTRAiLTPR--------IKVGRDVVQKAQTKEqadfaieALAKATYERLFRWILSRVNKAL------ 444
Cdd:cd14899 321 TKAAELLGVSTEALDHA-LTKRwlhasnetLVVGVDVAHARNTRN-------ALTMECYRLLFEWLVARVNNKLqrqasa 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 445 --------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQ 516
Cdd:cd14899 393 pwgadesdVDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 517 PCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCSE---QGNHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLT 593
Cdd:cd14899 472 ACLELFE--HRPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 594 KNMDPLNDNVTSLLNASSDKFVADLWK-DVDRIVGLDQMAKMTESSLPSASKTKKGMFrTVGQLYKEQLGKLMTTLRNTT 672
Cdd:cd14899 550 KNKDSFCESAAQLLAGSSNPLIQALAAgSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATT 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 673 PNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14899 629 PRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-771 |
8.72e-99 |
|
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: 336.24 E-value: 8.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFS--------GLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 171 DQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDSSitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 251 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLlesfnsytflsngfvpiPAAQDDEMF--QE 328
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDPESTdlRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 329 TLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTA--------AQKVCHLV-------GINVTDFT 393
Cdd:cd14887 220 ITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEAS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 394 RAILTPRIK------------------VGRDV--VQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHR---- 449
Cdd:cd14887 300 RKHLKTVARllglppgvegeemlrlalVSRSVreTRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpses 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 450 ---------QGASFLGILDIAGFEIFE---VNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDL 515
Cdd:cd14887 380 dsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 516 QPCIELIERPNN----------------------PPGVLALLDEECWFPKATDKSFVEKLCSEQGNHP-------KFQKP 566
Cdd:cd14887 460 PLASTLTSSPSStspfsptpsfrsssafatspslPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNiinsakyKNITP 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 567 KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkDVDRIVGLDQmakmteSSLPSASKTK 646
Cdd:cd14887 540 ALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACS---------TYTRLVGSKK------NSGVRAISSR 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 647 KgmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14887 605 R---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWR 681
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 241982718 727 RYEILAANAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14887 682 RYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-770 |
2.47e-98 |
|
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: 332.21 E-value: 2.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 96 LNEASVLHNLRERYFSGLIYTY---SGLfcVVVNPYKYLPI--------YSEKIVDMYKGKKRHEMPpHIYAIADTAYRS 164
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLPP-HAYDLAARAYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 165 MLQDREDQSILCTGESGAGKTENTKKVI-QYLAVVASSHKGKKdssitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14879 78 MRRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 244 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFL--SNGF--VPIPA 319
Cdd:cd14879 151 RYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHplPLGPG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 320 AQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVF--KKERNTDQASMpDNTAA-QKVCHLVGINVTDFtRAI 396
Cdd:cd14879 231 SDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 397 LTPRIK-VGRDVV----QKAQTKEQADfaieALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIF---EV 468
Cdd:cd14879 309 LTYKTKlVRKELCtvflDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 469 NSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIELIERPnnPPGVLALLDEEC-WFP 542
Cdd:cd14879 385 NSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILDDQTrRMP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 543 KATDKSFVEKLCSEQGNHPKFQKPKQLKDKTE---FSIIHYAGKVDYNASAWLTKNMDPLndnvtsllnaSSDkFVAdlw 619
Cdd:cd14879 457 KKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN--- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 620 kdvdrivgldqmakmtesslpsasktkkgMFRTVGQLyKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQL 699
Cdd:cd14879 523 -----------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQI 572
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 700 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnaipkgFMDGKQACILMIKALELDPNLYRIGQSKIFF 770
Cdd:cd14879 573 RSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-771 |
5.39e-97 |
|
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: 328.70 E-value: 5.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 176 CTGESGAGKTENTKKVIQYLAVVASSHKGKKDSSITgelekqllQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFK--------HVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVP-IPAA---QDDEMFQETL 330
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREdVSTAersLNREKLAVLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 331 EAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQK 410
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 411 AQTKEQADFAIEALAKATYERLFRWILSRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 487
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 488 NHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKSFVEKLCS- 555
Cdd:cd14878 393 NEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLQSl 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 556 -EQGNHPKFQKPKQ-------LKDK-TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdriv 626
Cdd:cd14878 460 lESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 627 gldqmAKMTesslpsasktkkgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLE 706
Cdd:cd14878 534 -----SKLV----------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLE 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 707 GIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14878 593 MVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-735 |
4.48e-94 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 317.61 E-value: 4.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKylPIYSEKIVDMYKGKKRHeMPPHIYAIADTAYRSMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVASShkgkkdssiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvtGYIVGA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTAS---------TTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 260 NIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLlesfNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFN 339
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKYKMTCSAMKSLGIANFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 340 EEEQLAIlkvvsSVLQLGNIVFKKERNTDQASmpdNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQADF 419
Cdd:cd14898 223 SIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 420 AIEALAKATYERLFRWILSRVNKALDKThrqGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 499
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 500 QREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLcseqgnHPKFQKPKQLKDKTEFSIIH 579
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI------KKYLNGFINTKARDKIKVSH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 580 YAGKVDYNASAWLTKNMDplndnvtsllnassdkfvadlwKDVDRIVGLDQMAkmTESSLPSASKtkkgmfrtvgqLYKE 659
Cdd:cd14898 442 YAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN--DEGSKEDLVK-----------YFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 660 QLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA 735
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-771 |
5.32e-90 |
|
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: 307.71 E-value: 5.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPiysekiVDM--YKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILC 176
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVID------VDIneYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIII 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 177 TGESGAGKTENTKKVIQ-YLAVVasshkgKKDSSITgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14937 75 SGESGSGKTEASKLVIKyYLSGV------KEDNEIS----NTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSI 335
Cdd:cd14937 145 IVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 336 MGFNEEEQLAILkVVSSVLQLGNIVFK---KERNTDQASMPDNT--AAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQK 410
Cdd:cd14937 225 MNMHDMKDDLFL-TLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 411 AQTKEQADFAIEALAKATYERLFRWILSRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 491 MFILEQEEYQREGIEWNFIDFGLDlQPCIELIeRPNNppGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKqlK 570
Cdd:cd14937 383 VYEKETELYKAEDILIESVKYTTN-ESIIDLL-RGKT--SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTK--K 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 571 DKTE-FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakMTESslpsasktkKGM 649
Cdd:cd14937 457 DINKnFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSES---------LGR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYE 729
Cdd:cd14937 518 KNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFE 596
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 241982718 730 ILAANAIPKGFMDGKQACILMIKAlELDPNLYRIGQSKIFFR 771
Cdd:cd14937 597 YLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-723 |
2.88e-80 |
|
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: 280.64 E-value: 2.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKGKKRHE-------MPPHIYAIADTAYRSMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 171 DQSILCTGESGAGKTENTKKVIQYLavvassHKGKKDSSITgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF------HYIQTDSQMT-ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 251 D---------VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAG-AKEKMKSDLLLESFNSYTFL---------- 310
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 311 ----------SNGFVPIPAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKerntdqasmpdntaaqk 380
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 381 VCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGA-------- 452
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 453 ---SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnnpp 529
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 530 gVLALLDE-----ECWFPKATDKSF-----------VEKLCSEQGNHPKFQK---PKQLKDKTEFSIIHYAGKVDYNASA 590
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFryllnnerqqqLEGKVSYGFVLNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 591 WLTKNMDPLNDNVTSLLNASSDKFVADlwkdvdrivgldqmakmtesslpSASKTKKGMFRTVGQLYKEQLGKLMTTLRN 670
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 241982718 671 TTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-758 |
4.36e-77 |
|
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: 269.68 E-value: 4.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKY----LPIYSEKIVDMYkgkkrhempPHIYAIADTAYRSMLQDREDQSIL 175
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDvgnpLTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 176 CTGESGAGKTENTKKVIQYLAVVASshkgkkdssitGELE----KQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFd 251
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLFDVAG-----------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 252 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYT--FLSNGFVPIPAAQDDEMFQET 329
Cdd:cd14881 141 TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANlrYLSHGDTRQNEAEDAARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 330 LEAMSIMG--FneeeqLAILKVVSSVLQLGNIVFKkERNTDQASMPDNTAAQKVCHLVGINVTDFTRAiLTPRIK-VGRD 406
Cdd:cd14881 221 KACLGILGipF-----LDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 407 VVQKAQTKEQADFAIEALAKATYERLFRWILSRVN--KALDKTHRQGAS--FLGILDIAGFEIFEVNSFEQLCINYTNEK 482
Cdd:cd14881 294 LVKSVCDANMSNMTRDALAKALYCRTVATIVRRANslKRLGSTLGTHATdgFIGILDMFGFEDPKPSQLEHLCINLCAET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 483 LQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIELIErpNNPPGVLALLDEECwFPKATDKSFVEKLCSEQGNHP 561
Cdd:cd14881 374 MQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 562 KFQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFvadlwkdvdrivgldqmakmtesslps 641
Cdd:cd14881 450 RLFEAKP-QDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF--------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 642 asktkkgMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVF 721
Cdd:cd14881 502 -------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRF 574
|
650 660 670
....*....|....*....|....*....|....*....
gi 241982718 722 QEFRQRYEILAANAIPKGFMDGKQAC--ILMIKALELDP 758
Cdd:cd14881 575 KAFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQPP 613
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-724 |
1.75e-75 |
|
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: 266.19 E-value: 1.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLP-IYSEKIVDMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVasshkgkkDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTT--------DLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 259 ANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSN-GFVPIPAAQDDEMFQETLEAMSIMG 337
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 338 FNEEEQLAILKVVSSVLQLGNIVFKKERNtdQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAqtkeqa 417
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 418 dfaiEALAKATYERLFRWILSRVNKALDKThrQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 498 EYQREGIEW-NFIDFGlDLQPCIELIERpnnppgVLALLDEECWFPKATDKSFVEKLCSEQGNHPKF-QKPKQlkdkteF 575
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------F 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 576 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDK--FVADLWKDVDRIVG-LDQMAKMTESSLPSASKTKKGMFrT 652
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKylFSRDGVFNINATVAeLNQMFDAKNTAKKSPLSIVKVLL-S 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 653 VGQLYKEQL-----------------------GKLMTTLRNTTP---------NFVRCIIPNHEKRSGKLDAFLVLEQLR 700
Cdd:cd14905 524 CGSNNPNNVnnpnnnsgggggggnsgggsgsgGSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660
....*....|....*....|....*...
gi 241982718 701 CNGVLEGIRICRQGFP----NRIVFQEF 724
Cdd:cd14905 604 SLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-771 |
5.75e-73 |
|
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: 257.75 E-value: 5.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 180 SGAGKTENTKKVIQYLAVVasshkGKKDSSITGELEKqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRVES----SIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 260 NIETYLLEKSRAIRQARDERTFHIFYYLLAG--AKEKMKsDLLLESFNSYTFL----SNGFVPIPAAQDD-----EMFQE 328
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLrippEVPPSKLKYRRDDpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 329 TLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKerNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVV 408
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 409 QKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHrqgaSFLG------ILDIAGFEIFEVNSFEQLCINYTNEK 482
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR----AVFGdkysisIHDMFGFECFHRNRLEQLMVNTLNEQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 483 LQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciELIERPNnppGVLALLDEECwfPKATDKSFVekLCSEQGN 559
Cdd:cd14882 386 MQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYI--MDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 560 HPKFQKPKQlkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivglDQMAKMtessl 639
Cdd:cd14882 456 HSQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM----- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 640 psasktkkgmfRTVGQLYKEQLGKLMTTLRNTTPN----FVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGF 715
Cdd:cd14882 521 -----------RTLAATFRATSLELLKMLSIGANSggthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGF 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 716 PNRIVFQEFRQRYEILAANAIPKGFMDgKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14882 590 SYRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-731 |
3.71e-71 |
|
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: 252.10 E-value: 3.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYkgkkrhemppHIYAIADTAYRSMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 178 GESGAGKTENTKKVIQYLAVVASSHKGKKDSSitgelekqllQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIV 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSS----------AIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 258 GANIE-TYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 336
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 337 GFNEEEQLAILKVVSSVLQLGNIVFKKERNTD---QASMPDNTAAQK-VCHLVGINVTDFTrAILTPRIKVGRDVvqkaq 412
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSEDGTTI----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 413 TKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGAsfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14874 294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 493 ILEQEEYQREGIEWNF-IDFGLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQlKD 571
Cdd:cd14874 372 HDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 572 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldqmakmtesslpSASKTKKGMFR 651
Cdd:cd14874 449 RLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE--------------------SYSSNTSDMIV 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 652 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14874 509 SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-729 |
1.65e-69 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 250.27 E-value: 1.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 102 LHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIY----------SEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 172 QSILCTGESGAGKTENTKKVIQYLAVVASS----HKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 248 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKE--KMKSDLLL-ESFNSYTFLSNGFVPIPA-AQDD 323
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMnKCVNEFVMLKQADPLATNfALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 324 EMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVF-------KKERNTDQASMPDNTA------AQ--KVCHLVGIN 388
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAKLLEVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 389 --VTD---FTRAILTpriKVGRDVVQ--KAQTKEQADFAIEALAKATYERLFRWILSRVNKAL----DKTHRQG----AS 453
Cdd:cd14893 324 pvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 454 FLGILDIAGFEIFE--VNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIELIER 524
Cdd:cd14893 401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFED 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 525 PnnPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTE------------FSIIHYAGKVDYNASAWL 592
Cdd:cd14893 481 K--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 593 TKNMDPLNDNVTSLLNASSDKfvadlwkdVDRIVGLDQM--------AKMTESSLPSASKTKKGMFR----------TVG 654
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMaaassekaAKQTEERGSTSSKFRKSASSaresknitdsAAT 630
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 655 QLYKeQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14893 631 DVYN-QADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-255 |
2.50e-62 |
|
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: 210.28 E-value: 2.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 121 FCVVVNPYKYLPIYSEKIVD-MYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIvFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 200 SSHKGKKD-------SSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
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 ... |
100-769 |
3.34e-56 |
|
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: 209.69 E-value: 3.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYK-GKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDSSITGELEKQ---------------LLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIhneentdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 244 KFIRINFDvTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDD 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 324 EMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNI-----VFKKE---------------------RNTDQASMPDNTA 377
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 378 AQKV-CHLVGINVTDFTRAILTPRIkVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHR--QGASF 454
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 455 LGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNppGVLAL 534
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 535 LDEECWFPKATDKSfveKLCS----EQGNHPKFQKPKQLK-DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNA 609
Cdd:cd14938 478 LLENVSTKTIFDKS---NLHSsiirKFSRNSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 610 SSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQ----LYKEQLGKLMTTLRNTTPNFVRCIIPNHEK 685
Cdd:cd14938 555 SENEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 686 RS-GKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnaipkgfmDGKQACILMIKALELDPNLYRIG 764
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 241982718 765 QSKIF 769
Cdd:cd14938 707 NNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1104-1913 |
4.19e-31 |
|
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: 134.03 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1104 AQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdLGEELEALKTELEDTLDSTATQQELRAKREQEvtvlkkal 1183
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLRLEELREELE-------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1184 deETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQD 1263
Cdd:TIGR02168 243 --ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1264 LQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQE------ETRQKLNVSTK 1337
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1338 -LRQLEDERNSLQDQLDEEMEAKQNLERHVSTLniQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYD 1416
Cdd:TIGR02168 401 eIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1417 KLEKTKNRLQQELDDLVVDLDNQRQL---VSNLEKKQKKF---DQLLAEEKNISSKY-----ADERDRAEAEAREKETKA 1485
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFsegVKALLKNQSGLsgiLGVLSELISVDEGYeaaieAALGGRLQAVVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1486 L----SLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDA 1561
Cdd:TIGR02168 559 KkaiaFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1562 KL------------------------RLEVNMQALKGQFE-RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAA 1616
Cdd:TIGR02168 639 KKlrpgyrivtldgdlvrpggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1617 AAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDL 1696
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1697 AAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELate 1776
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1777 rstaQKNESARQQLERQNKELRSKLQEVEGAVKaKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVL- 1855
Cdd:TIGR02168 876 ----EALLNERASLEEALALLRSELEELSEELR-ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYs 950
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 1856 LQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEE-------AEEESQRINANRRKLQRELDEATES 1913
Cdd:TIGR02168 951 LTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEA 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
829-1677 |
1.87e-28 |
|
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: 125.55 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 829 LRNWQWWRLftkvkpLLQVTRQEEEMQAKEEEMQKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQ-AETELYAeae 907
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEeLQKELYA--- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 908 emrvrLAAKKQELEEilhemearleeeedRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDI 987
Cdd:TIGR02168 293 -----LANEISRLEQ--------------QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 988 LVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDf 1067
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1068 hEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEE 1147
Cdd:TIGR02168 433 -AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1148 LEAlKTELEDTLDSTATQQELRAKREQEV-TVLKKALDeetrsheAQVQEMRQKHTQAVEELtEQLEQFKRAKANLDKSK 1226
Cdd:TIGR02168 512 LKN-QSGLSGILGVLSELISVDEGYEAAIeAALGGRLQ-------AVVVENLNAAKKAIAFL-KQNELGRVTFLPLDSIK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1227 -QTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDL--QSKCSDGERARAELSDKVHKLQNEVE----------SVT 1293
Cdd:TIGR02168 583 gTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlgGVLVVDDLDNALELAKKLRPGYRIVTldgdlvrpggVIT 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1294 GMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEetrqklnVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQL 1373
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAE-------LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1374 SDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRqlvSNLEKKQKKF 1453
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR---EALDELRAEL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1454 DQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEakeelertnkmLKAEMEDLVSSKDDVGKNVHELEKS 1533
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-----------LAAEIEELEELIEELESELEALLNE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1534 KRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHE-YETELEDERKQR 1612
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-QLELRLEGLEVRIDNLQERLSEeYSLTLEEAEALE 960
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1613 ALAAAAKKKLEGDLKDLELQADS-------AIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKE 1677
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
967-1860 |
4.72e-27 |
|
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: 120.93 E-value: 4.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 967 QKLQLEKVTAEaKIKKLEDDILVMDDQNSKLSKERklLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKE 1046
Cdd:TIGR02168 203 KSLERQAEKAE-RYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1047 EKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQED 1126
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1127 LDSERAARNKAEKQKRDLGEELEALKTELedtldstatqqelrAKREQEVTVLKKALdEETRSHEAQVQEMRQKHTQAVE 1206
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKV--------------AQLELQIASLNNEI-ERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1207 ELTEQLE--QFKRAKANLDKSKQTLEkenaDLAGELRVLGQAKQEVEHKKKKLEVQLQDLQskcsdgeraraelsDKVHK 1284
Cdd:TIGR02168 425 ELLKKLEeaELKELQAELEELEEELE----ELQEELERLEEALEELREELEEAEQALDAAE--------------RELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1285 LQNEVESVTGMLNEAEG--KAIKLAKDVASLGSQLQDT-QELLQEETRQKLNVSTKLRQledernSLQDQLdeeMEAKQN 1361
Cdd:TIGR02168 487 LQARLDSLERLQENLEGfsEGVKALLKNQSGLSGILGVlSELISVDEGYEAAIEAALGG------RLQAVV---VENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1362 LERHVSTLniqlsdsKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLvvdLDNQRq 1441
Cdd:TIGR02168 558 AKKAIAFL-------KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYL---LGGVL- 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1442 LVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARaleealeakeelertnkmlKAEMEDLVsskd 1521
Cdd:TIGR02168 627 VVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILER-------------------RREIEELE---- 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1522 dvgKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERdLQARDEQNEEKRRQLQRQLHEY 1601
Cdd:TIGR02168 684 ---EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTEL 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1602 ETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKK 1681
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1682 AKSLEADLMQLQEDLAAAERARKQADLEKEELAeelasslSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRK 1761
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELE-------SELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1762 ATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAAT 1841
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992
|
890
....*....|....*....
gi 241982718 1842 KSLKQKDKKLKEVLLQVED 1860
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKED 1011
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-712 |
4.74e-27 |
|
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: 120.23 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 105 LRERYFSGLIYTYSGLFCV-VVNPYKYL------PIYSEKIVDMYKGKKRHE--MPPHIYAIAD---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 160 ----TAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAVVASS--HKGKKDS-SITG-------------------- 212
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPalSKGSEETcKVSGstrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 213 --------------------------------------------------------------ELEKQL------------ 218
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 219 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------RDERTFHI 283
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 284 FYYLLAGAK-----EKMKSDLLLESFN--SYTFLSN------GFVPIPAA--QDDEMFQETLEAMSIMGFNEEEQLAILK 348
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDGIDcsALTYLGRsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 349 VVSSVLQLGNIVFKKERNTDQASMPDN---TAAQKVCHLVGI-NVTDFTRAILTPRIKV--GRDVVQKAQTKEQADFAIE 422
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 423 ALAKATYERLFRWILSRVNKAL----------------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLqql 486
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 487 fnhtmfileqeeYQREGiewNFIDFGLDLQPciELIERPN---------NPPGVLALLDEECWFPKAT----------DK 547
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRP--HLTARDSekdvlfiyeHPLGVFASLEELTILHQSEnmnaqqeekrNK 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 548 SFVEKLCSEqgNHPKFQKPKQLKDKTE-----------FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVA 616
Cdd:cd14894 626 LFVRNIYDR--NSSRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFC 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 617 DLWKDVDRivgLDQMAKMTESSLPSASKTKKGMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVL 696
Cdd:cd14894 704 RMLNESSQ---LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVE 779
|
810
....*....|....*.
gi 241982718 697 EQLRCNGVLEGIRICR 712
Cdd:cd14894 780 QQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1201-1930 |
6.83e-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: 113.61 E-value: 6.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1201 HTQAveELTEQLEQFKRAKANLDKSKQTLEKEnaDLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSD 1280
Cdd:TIGR02168 206 ERQA--EKAERYKELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1281 KVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQ 1360
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1361 NLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEkaaaydkLEKTKNRLQQElddlvvdldnQR 1440
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERLQQE----------IE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1441 QLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTnkmLKAEMEDLVSSK 1520
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA---RLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1521 DDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAklrLEVNMQAL---KGQFERDLQARDEQNEEKRRQLQRQ 1597
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRLQAVvveNLNAAKKAIAFLKQNELGRVTFLPL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1598 LHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGR----------EEAIKQLRKLQAQMKDFQRELD----- 1662
Cdd:TIGR02168 579 DSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRPGYRIVTLDGDlvrpg 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1663 --------DARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRL 1734
Cdd:TIGR02168 659 gvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1735 EARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAkLKS 1814
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1815 TVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKgntkVKQLKRQLEEA----- 1889
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA----LLNERASLEEAlallr 893
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 241982718 1890 ------EEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRR 1930
Cdd:TIGR02168 894 seleelSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1326-1922 |
3.80e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1326 EETRQKLN-VSTKLRQLEDERNSLQDQ---------LDEEMEAKQNLERhvstlniqlsdsKKKLQDFASTIEVMEEGKK 1395
Cdd:COG1196 182 EATEENLErLEDILGELERQLEPLERQaekaeryreLKEELKELEAELL------------LLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1396 RLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAE 1475
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1476 AEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDEL 1555
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1556 QATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADS 1635
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1636 AikGREEAIKQLRKLQAQMKDFQRELDDARASR------DEIFATSKENEKKAKSLEADLMQ---LQEDLAAAERARKQA 1706
Cdd:COG1196 490 A--ARLLLLLEAEADYEGFLEGVKAALLLAGLRglagavAVLIGVEAAYEAALEAALAAALQnivVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1707 DLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQgnmEAMSDRVRKATLQAEQLSNELATERSTAQKNESA 1786
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE---ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1787 RQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAE 1866
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1867 QYKEQAEKGNTKVKQLKRQ----LEEAEEESQRINANRRKLQRELDEATESNEAMGReVN 1922
Cdd:COG1196 725 ALEEQLEAEREELLEELLEeeelLEEEALEELPEPPDLEELERELERLEREIEALGP-VN 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1113-1922 |
4.88e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 107.46 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1113 IRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEA 1192
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1193 QVQEMRQKhtqaVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAK-QEVEHKKKKLEVQLQDLQSKCSDG 1271
Cdd:TIGR02169 245 QLASLEEE----LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1272 ERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQE------ETRQKL-NVSTKLRQLEDE 1344
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaETRDELkDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1345 RNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFAST-------IEVMEEGKKRLQKEMEGLSQQYEEKAAAYDK 1417
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEkedkaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1418 LEKTKNRLQQELDdlvvDLDNQRQLVSNLEKKQKKFDQLLaeEKNISSKYADERDRAEAEarEKETKALSLAraleeale 1497
Cdd:TIGR02169 481 VEKELSKLQRELA----EAEAQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVG--ERYATAIEVA-------- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1498 akeelertnkmLKAEMEDLVSSKDDVGKNVHELEKSK---RALETQMEEMKTQLEELEdelQATEDAKLRLEVNMQALKG 1574
Cdd:TIGR02169 545 -----------AGNRLNNVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1575 QFE-------RDLQARDEQNEEKRRQLQRQLHEYETELEDE--------RKQRALAAAAKKKLE------GDLKDLELQA 1633
Cdd:TIGR02169 611 KYEpafkyvfGDTLVVEDIEAARRLMGKYRMVTLEGELFEKsgamtggsRAPRGGILFSRSEPAelqrlrERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1634 DSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEEL 1713
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1714 AEELasslsgrNTLQDEKRRLEARIAQleEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQ 1793
Cdd:TIGR02169 771 EEDL-------HKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1794 NKELRSKLQEVEGAV------KAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQ 1867
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 1868 YKEQAEKGNTKVKQLKRQLEEAEEESQRInANRRKLQRELDEATESNEAMGrEVN 1922
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAELQRVEEEIRALE-PVN 974
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1604 |
1.35e-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: 106.31 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETE--LKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQ 939
Cdd:TIGR02169 214 QALLKEKREYEGYelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 940 ----QLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNL 1015
Cdd:TIGR02169 294 ekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1016 AEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAA 1095
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1096 LARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELE---ALKTELEDTLDST-ATQQELRAK 1171
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRggrAVEEVLKASIQGVhGTVAQLGSV 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1172 REQEVTVLKKAL----------DEET--------RSHEA------QVQEMRQKHTQA----------------------- 1204
Cdd:TIGR02169 534 GERYATAIEVAAgnrlnnvvveDDAVakeaiellKRRKAgratflPLNKMRDERRDLsilsedgvigfavdlvefdpkye 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1205 -----VEELTEQLEQFKRAKANLDKSK------QTLEKENADLAGELRVLGQAK---------QEVEHKKKKLEVQLQDL 1264
Cdd:TIGR02169 614 pafkyVFGDTLVVEDIEAARRLMGKYRmvtlegELFEKSGAMTGGSRAPRGGILfsrsepaelQRLRERLEGLKRELSSL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1265 QSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDE 1344
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1345 RNSLQDQLdEEMEAKQNLERhVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNR 1424
Cdd:TIGR02169 774 LHKLEEAL-NDLEARLSHSR-IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1425 LQQELDDLVVDLdnqRQLVSNLEKKQKKFDQLLAEEKNISSkyadERDRAEAEAREKETKALSLARALEEALEAKeeler 1504
Cdd:TIGR02169 852 IEKEIENLNGKK---EELEEELEELEAALRDLESRLGDLKK----ERDELEAQLRELERKIEELEAQIEKKRKRL----- 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1505 tnKMLKAEMEDLVSSKDDVGKNVHELEKSKRAlETQMEEMKTQLEELEDELQATEDaklrleVNMQALKgQFER------ 1578
Cdd:TIGR02169 920 --SELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALEP------VNMLAIQ-EYEEvlkrld 989
|
810 820
....*....|....*....|....*.
gi 241982718 1579 DLQARDEQNEEKRRQLQRQLHEYETE 1604
Cdd:TIGR02169 990 ELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
966-1706 |
2.17e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 105.54 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 966 RQKLQLEKVTAEaKIKKLEDDIlvMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKK 1045
Cdd:TIGR02169 200 LERLRREREKAE-RYQALLKEK--REYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1046 EEKsrqeleKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQE 1125
Cdd:TIGR02169 277 LNK------KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1126 DLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQEL--RAKREQE--------VTVLKKALDEETRSHEAQVQ 1195
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleKLKREINelkreldrLQEELQRLSEELADLNAAIA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1196 EMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENA---DLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGE 1272
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQelyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1273 RARAELSDK---VHKLQNEVESV----TGMLNEAEG---------------KAIKLAKDV-------------------A 1311
Cdd:TIGR02169 511 AVEEVLKASiqgVHGTVAQLGSVgeryATAIEVAAGnrlnnvvveddavakEAIELLKRRkagratflplnkmrderrdL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1312 SLGSQ------------------------LQDT--QELLQEETRQKLNV------------------------------- 1334
Cdd:TIGR02169 591 SILSEdgvigfavdlvefdpkyepafkyvFGDTlvVEDIEAARRLMGKYrmvtlegelfeksgamtggsraprggilfsr 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1335 --STKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEvmeegkkRLQKEMEGLSQQYEEKA 1412
Cdd:TIGR02169 671 sePAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-------QLEQEEEKLKERLEELE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1413 AAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKniSSKYADERDRAEAEAREKETKALSLARAL 1492
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1493 EEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQatedaklrlevnmqal 1572
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG---------------- 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1573 kgqferDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLElQADSAIKGREEAIKQLRKLQA 1652
Cdd:TIGR02169 886 ------DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQA 958
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1653 QMKDFQRELDD-------ARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQA 1706
Cdd:TIGR02169 959 ELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
865-1561 |
3.46e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 865 KERQQKAETELKELEQKhtqLAEEKTLLQE---QLQaetELYAEAEemrvrLAAKKQELEEILHEMEARLEEEEDRGQQL 941
Cdd:COG1196 171 KERKEEAERKLEATEEN---LERLEDILGElerQLE---PLERQAE-----KAERYRELKEELKELEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 QAERKKMAQQmldleeqleEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEK 1021
Cdd:COG1196 240 ELEELEAELE---------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 AKNLtklkskhESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDE 1101
Cdd:COG1196 311 RREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1102 EIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKreqevtvlkk 1181
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE---------- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1182 aLDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQL 1261
Cdd:COG1196 454 -LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1262 QDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLnVSTKLRQL 1341
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL-VASDLREA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1342 EDERNSLQDQLDEEMEAKQNLERHVSTLniqlsdsKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKT 1421
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRA-------VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1422 KNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEE 1501
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1502 LERTNKMLKAEMEDLvsskddvGK-N---VHELEkskrALETQMEEMKTQLEELEDELQATEDA 1561
Cdd:COG1196 765 LERELERLEREIEAL-------GPvNllaIEEYE----ELEERYDFLSEQREDLEEARETLEEA 817
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
825-1432 |
2.68e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 825 AYLKLRNWQWWRLftkvkpllQVTRQEEEMQAKEEEMQKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYA 904
Cdd:COG1196 227 AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 905 EAEEMRVRLAAKKQELEEILhemearlEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLE 984
Cdd:COG1196 299 RLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 985 DDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDA 1064
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1065 SDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARN--------- 1135
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavlig 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1136 KAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQF 1215
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1216 KRAKANLDkskQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESvtgm 1295
Cdd:COG1196 612 DARYYVLG---DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL---- 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1296 LNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSD 1375
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1376 SKKKLqdfastievmeegkKRLQKEMEGLS-------QQYEEKAAAYDKLEKTKNRLQQELDDL 1432
Cdd:COG1196 765 LEREL--------------ERLEREIEALGpvnllaiEEYEELEERYDFLSEQREDLEEARETL 814
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1272-1913 |
5.47e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1272 ERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQ 1351
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1352 LDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDD 1431
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1432 LVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERtnkmlka 1511
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1512 emedlvsskddvgknvhELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKR 1591
Cdd:COG1196 457 -----------------EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1592 RQLQRQLHEyetelederkqralaaaakkkLEGDLKDLELQADSAIKGREEAIkqLRKLQAQMKDFQRELDDARASRDEI 1671
Cdd:COG1196 520 RGLAGAVAV---------------------LIGVEAAYEAALEAALAAALQNI--VVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1672 FATSKENEKKAKSLEADLMQLQEDLAAAERARKQADlekeELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGN 1751
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREAD----ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1752 MEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEvegavkakLKSTVAALEAKIAQLEEQVE 1831
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE--------EERELAEAEEERLEEELEEE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1832 QEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKgntKVKQLKRQLEE-------AEEESQRINANRRKLQ 1904
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER---ELERLEREIEAlgpvnllAIEEYEELEERYDFLS 801
|
....*....
gi 241982718 1905 RELDEATES 1913
Cdd:COG1196 802 EQREDLEEA 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1324-1942 |
1.42e-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: 99.75 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1324 LQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEG 1403
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1404 LSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKET 1483
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1484 KALSLARALEEaleakeelertnkmLKAEMEDLVSSKDDVGKNVHELEKskRALETQMEEMKTQLEELEDELQATEDAKL 1563
Cdd:TIGR02168 394 QIASLNNEIER--------------LEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1564 RLEVNMQALKGQFERDLQARDeQNEEKRRQLQRQLHEYETELEDERK--QRALAAAAKKKLEGDLKDLELQADSAIKGRE 1641
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQENLEGfsEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1642 EAIKQLrkLQAQMKDFqrELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSL 1721
Cdd:TIGR02168 537 AAIEAA--LGGRLQAV--VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1722 SGRNTLQDEKRRLeaRIAQLEEELEEEQGNMEAmsdRVRKATLQAEQLSNELATERSTAQKNeSARQQLERQNKELRSKL 1801
Cdd:TIGR02168 613 KLRKALSYLLGGV--LVVDDLDNALELAKKLRP---GYRIVTLDGDLVRPGGVITGGSAKTN-SSILERRREIEELEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1802 QEVEGAVkAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQ 1881
Cdd:TIGR02168 687 EELEEKI-AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1882 LKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNEASFVPSRRA 1942
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1146-1740 |
3.89e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.09 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1146 EELEALKTELEDTLDSTATQQElRAKREQEvtvLKKALDEetRSHEAQVQEMRQKHTQAvEELTEQLEQFKRAKANLDKS 1225
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAE-KAERYRE---LKEELKE--LEAELLLLKLRELEAEL-EELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1226 KQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIK 1305
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1306 LAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFAS 1385
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1386 TIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNL----EKKQKKFDQLLAEEK 1461
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELleelAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1462 NISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELErtnkmLKAEMEDLVSSKDDVGKNVHELEKSK---RALE 1538
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-----LAAALQNIVVEDDEVAAAAIEYLKAAkagRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1539 TQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAA 1618
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1619 KKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAA 1698
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 241982718 1699 AERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQ 1740
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1170-1924 |
1.00e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1170 AKREQEVTVLKKALDEETRSheaqvqEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQE 1249
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATE------EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1250 VEHKKKKLEVQLQDLQskcsdgeraRAELSDKVHKLQnEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETR 1329
Cdd:PTZ00121 1149 EDAKRVEIARKAEDAR---------KAEEARKAEDAK-KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1330 QklnvSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNiqlSDSKKKLQDFASTIEVMEEGKKRLQKEMeglsQQYE 1409
Cdd:PTZ00121 1219 K----AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR---KFEEARMAHFARRQAAIKAEEARKADEL----KKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1410 EKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQllAEEKNISSKYADERDRAEAEAREKETKALSLA 1489
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1490 RALEEALEAKEELERTNKMLKAEMEdlvsskddvgKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNM 1569
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEK----------KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1570 QALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRK 1649
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1650 LQAQMKDFQRELDDARASRDEIFATSKENEKKAKSL-EADLMQLQEDLAAAERARKQADLEKEELAEElasslsgrntlQ 1728
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKA-----------E 1584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1729 DEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNElATERSTAQKNESARQQLERQNKELRSklQEVEGAV 1808
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKI 1661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1809 KAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEE 1888
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
730 740 750
....*....|....*....|....*....|....*....
gi 241982718 1889 AE---EESQRINANRRKLQRELDEATESNEAMGREVNAL 1924
Cdd:PTZ00121 1742 DKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
990-1573 |
8.23e-19 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 93.16 E-value: 8.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 990 MDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHE 1069
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1070 QIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELE 1149
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1150 ALKTELEDTLDSTATQQELRAK---REQEVTVLKKALDEETRSHEAQVQEMRQKHTQ---AVEELTEQLEQFKRAKANLD 1223
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQiseLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnqLKDEQNKIKKQLSEKQKELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1224 KSKQ---TLEKENADLAGELRVLGQAKQEVEHKK-----KKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGM 1295
Cdd:TIGR04523 278 QNNKkikELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1296 LNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSD 1375
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1376 SKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQ 1455
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1456 LLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKM--LKAEMEDLVSSKDDVGKNVHELEKS 1533
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIeeLKQTQKSLKKKQEEKQELIDQKEKE 597
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 241982718 1534 KRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALK 1573
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
862-1705 |
1.52e-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: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQL 941
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEK 1021
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 AKNLTKLKSKHESMISELEvrlKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDE 1101
Cdd:pfam02463 337 IEELEKELKELEIKREAEE---EEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1102 EIAQKNNALKKIRELEGHISDLQEDLDSERaaRNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKK 1181
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQ--GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1182 ALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQL 1261
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1262 QDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQ-DTQELLQEETRQKLNVSTKLRQ 1340
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIlKDTELTKLKESAKAKESGLRKG 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1341 LEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEK 1420
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1421 TKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKfdQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKE 1500
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKE--EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1501 ELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDL 1580
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1581 QARDEQNEEKRRQLQRQLHEYETELEDERK--QRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQ 1658
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIeeRIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAK 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 241982718 1659 RELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQ 1705
Cdd:pfam02463 970 EELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1040-1566 |
3.66e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.25 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1040 EVRLKKEEKSRQELeklkrklegdasdfHEQIADLQAQIAELKMQLAKKEEELQAALARLDEE---IAQKNNALKKIREL 1116
Cdd:PRK02224 191 QLKAQIEEKEEKDL--------------HERLNGLESELAELDEEIERYEEQREQARETRDEAdevLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1117 EGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTatqqELRAKREQEVTVLKKALDEEtrshEAQVQE 1196
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDR----DEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1197 MRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARA 1276
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1277 ELSDKVHKLQNEVESVTGMLNEAEGKaIKLAKDVASLGSQLQDT-------QEL--------LQEETRQKLNVSTKLRQL 1341
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEAT-LRTARERVEEAEALLEAgkcpecgQPVegsphvetIEEDRERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1342 EDERNSLQDQLDEEMEAKQnLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKT 1421
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1422 KNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETkaLSLARALEEALEAKEE 1501
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRER--LAEKRERKRELEAEFD 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1502 LERTNKmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELE---DELQATEDAKLRLE 1566
Cdd:PRK02224 645 EARIEE-AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEelrERREALENRVEALE 711
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
864-1399 |
7.74e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.51 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 864 IKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQA 943
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 944 ERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEddilvMDDQNSKLSKERKLLEERVSDLTtnlaEEEEKAK 1023
Cdd:PRK03918 271 LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-----IEKRLSRLEEEINGIEERIKELE----EKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1024 NLTKLKSKHESMISELEVRLKKEEKSRQ---ELEKLKRKLEGdasdfhEQIADLQAQIAEL---KMQLAKKEEELQAALA 1097
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYEEAKAkkeELERLKKRLTG------LTPEKLEKELEELekaKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1098 RLDEEIAQKNNALKKIRELEGHISDLQEDLDSE---------RAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQEL 1168
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1169 RakREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELT--------------EQLEQFKRAKANLDKSKQTLEKENA 1234
Cdd:PRK03918 496 I--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklkgeikslkkelEKLEELKKKLAELEKKLDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1235 DLAGELRVLG-QAKQEVEHKKKKLEvQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASL 1313
Cdd:PRK03918 574 ELLKELEELGfESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1314 GSQLqdTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTlniqLSDSKKKLQDFASTIEVMEEG 1393
Cdd:PRK03918 653 EKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEKALERVEEL 726
|
....*.
gi 241982718 1394 KKRLQK 1399
Cdd:PRK03918 727 REKVKK 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
873-1481 |
8.94e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.12 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 873 TELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMaqqm 952
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 953 ldLEEQLEEEEAARQKLQLEKVtaEAKIKKLEDDIlvmddqnsklskerKLLEERVSDLTTNLAEEEEKAKNLTKLKSKH 1032
Cdd:PRK03918 231 --KELEELKEEIEELEKELESL--EGSKRKLEEKI--------------RELEERIEELKKEIEELEEKVKELKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1033 ESMIsELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKmQLAKKEEELQAALARLDEEIAQKNNALKK 1112
Cdd:PRK03918 293 EEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1113 IRELEGH--------ISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTatqQELRaKREQEVTVLKKALD 1184
Cdd:PRK03918 371 KEELERLkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1185 EETRsheaqvQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDL 1264
Cdd:PRK03918 447 EEHR------KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1265 QSKCSDGERARaELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKL-NVSTKLRQLE- 1342
Cdd:PRK03918 521 EKKAEEYEKLK-EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEp 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1343 --DERNSLQD---QLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEvmEEGKKRLQKEMEGLSQQYEEKAAAYDK 1417
Cdd:PRK03918 600 fyNEYLELKDaekELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEEEYEELREEYLELSRELAG 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1418 LEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQK---KFDQLLAEEKNISSKYADERDRAEAEAREK 1481
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEEREKAKKeleKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
840-1697 |
3.19e-17 |
|
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: 88.57 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 840 KVKPLLQVTRQEEEMQAKEEEMQKIKERQQKAETELKELEQ---KHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAK 916
Cdd:TIGR00606 174 KFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQykeKACEIRDQITSKEAQLESSREIVKSYENELDPLKNR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 917 KQELEEIL---HEMEARLEEEEDRGQQLQAERKKMAQQMldleeqLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQ 993
Cdd:TIGR00606 254 LKEIEHNLskiMKLDNEIKALKSRKKQMEKDNSELELKM------EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 994 NSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLK---------KEEKSRQELEKLKRKLEGDA 1064
Cdd:TIGR00606 328 LEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpfSERQIKNFHTLVIERQEDEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1065 -------SDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDL---QEDLDSERAAR 1134
Cdd:TIGR00606 408 ktaaqlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIlelDQELRKAEREL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1135 NKAEKQK--RDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALdEETRSHEAQVQEMRQKHTQAVEELTEQL 1212
Cdd:TIGR00606 488 SKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME-MLTKDKMDKDEQIRKIKSRHSDELTSLL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1213 EQFKRAKA------NLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDkVHKLQ 1286
Cdd:TIGR00606 567 GYFPNKKQledwlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD-LERLK 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1287 NEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHV 1366
Cdd:TIGR00606 646 EEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1367 STLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKaaayDKLEKTKNRLQQELDDLVVDLDNQRQLVSNL 1446
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMEL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1447 EKKQKKFDQLLAEEKNISSKYADERDRAEAEarEKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKN 1526
Cdd:TIGR00606 802 KDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1527 VHEleksKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQ----------- 1595
Cdd:TIGR00606 880 LQR----RQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNdikekvknihg 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1596 --------------RQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAiKGREEAIKQ---LRKLQAQMKDFQ 1658
Cdd:TIGR00606 956 ymkdienkiqdgkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ-KIQERWLQDnltLRKRENELKEVE 1034
|
890 900 910
....*....|....*....|....*....|....*....
gi 241982718 1659 RELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLA 1697
Cdd:TIGR00606 1035 EELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLA 1073
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
886-1600 |
5.00e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.27 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 886 AEEKTLLQEQLQAETelyAEAEEMRVRLAAKK--QELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEE 963
Cdd:PTZ00121 1094 EEAFGKAEEAKKTET---GKAEEARKAEEAKKkaEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 964 AARQKLQLEKVTAEAKIKKLEDdiLVMDDQNSKLSKERKLLEERVSDlTTNLAEEEEKAKNLTKLKskhesmiselEVRL 1043
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEERKAE-EARKAEDAKKAEAVKKAE----------EAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1044 KKEEKSRQELEklkRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHisdl 1123
Cdd:PTZ00121 1238 DAEEAKKAEEE---RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK---- 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1124 QEDLDSERAARNKAEKQKRDlGEELEAlKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQ 1203
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKK-ADAAKK-KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1204 AV----------EELTEQLEQFKRAKANLDKS----KQTLEKENAD----LAGELRVLGQAKQEVEHKKKKLEVQLQDLQ 1265
Cdd:PTZ00121 1389 EKkkadeakkkaEEDKKKADELKKAAAAKKKAdeakKKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1266 SKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKA-IKLAKDVASLGSQLQDTQELLQEETRQKlnvSTKLRQLEDE 1344
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAeAKKKADEAKKAEEAKKADEAKKAEEAKK---ADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1345 RNSlqDQLDEEMEAKQNLERHvstlniQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEE----KAAAYDKLEK 1420
Cdd:PTZ00121 1546 KKA--DELKKAEELKKAEEKK------KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkmKAEEAKKAEE 1617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1421 TKNRlQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKET--KALSLARALEEALEA 1498
Cdd:PTZ00121 1618 AKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakKAEEDEKKAAEALKK 1696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1499 KEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELE-DELQATEDAKLRLEVNMQALKGQFE 1577
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
730 740
....*....|....*....|....*.
gi 241982718 1578 RDL---QARDEQNEEKRRQLQRQLHE 1600
Cdd:PTZ00121 1777 KEAvieEELDEEDEKRRMEVDKKIKD 1802
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1531-1961 |
6.03e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1531 EKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEkRRQLQRQLHEYETELEDERK 1610
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1611 QRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLM 1690
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1691 QLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLS 1770
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1771 NELATERSTAQKNESARQQLERQNKELRSKLqevegavkAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKK 1850
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARL--------LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1851 LKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEAtesnEAMGREVNALKSKLRR 1930
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR----GAIGAAVDLVASDLRE 610
|
410 420 430
....*....|....*....|....*....|.
gi 241982718 1931 GNEASFVPSRRAGGRRVIENTDGSEEEMDAR 1961
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
976-1359 |
1.26e-16 |
|
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: 86.65 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 976 AEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKaknltklkskhesmISELEVRLKKEEKSRQELEK 1055
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ--------------ISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1056 LKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAalarLDEEIAQKNNALKKIRElegHISDLQEDLDSERAARN 1135
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALRE---ALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1136 KAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAqvqemrqkHTQAVEELTEQLEQF 1215
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA--------LLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1216 KRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQskcsdgERARAELSDKVHKLQNEVESVTGM 1295
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDD 966
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1296 LNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQ---DQLDEEMEAK 1359
Cdd:TIGR02168 967 EEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEeaiEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1538-1910 |
2.84e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1538 ETQMEEMKTQLEELEDELQatEdaklrLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQralaaa 1617
Cdd:COG1196 178 ERKLEATEENLERLEDILG--E-----LERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEEL------ 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1618 akkklEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIfatskenEKKAKSLEADLMQLQEDLA 1697
Cdd:COG1196 245 -----EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-------LAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1698 AAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATER 1777
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1778 STAQKNESARQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQ 1857
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1858 VEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEA 1910
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1568 |
4.00e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.19 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEmrVRLAAKKQELEEILHEMEARLEEEEDRgqql 941
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE--LKKAEEKKKADEAKKAEEKKKADEAKK---- 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 QAERKKMAQQMLDL-EEQLEEEEAARQKLQLEKVTAEAKIKKLE--DDILVMDDQNSKLSKERKLLEERVSDLTTNLAEE 1018
Cdd:PTZ00121 1310 KAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEaaADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1019 EEKAKNLTKLKSKHESMISElevrLKKEEKSRQELEKLKRKLEgdasdfheqiADLQAQIAELKMQLAKKEEEL--QAAL 1096
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADE----LKKAAAAKKKADEAKKKAE----------EKKKADEAKKKAEEAKKADEAkkKAEE 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1097 ARLDEEIAQKNNALKKIRELEGHisdlQEDLDSERAARNKAEKQKRDlGEELEAlKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKK----AEEAKKADEAKKKAEEAKKK-ADEAKK-AAEAKKKADEAKKAEEAKKADEAKK 1529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1177 TVLKKALDEETRSHEA-QVQEMRQKHTQAVEELTEQLEQFKRAKAnlDKSKQTLEKENADLAGELRVLGQAKQEVEHKKK 1255
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKkKADELKKAEELKKAEEKKKAEEAKKAEE--DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1256 KLEvqlqdlQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQklnvS 1335
Cdd:PTZ00121 1608 KAE------EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK----A 1677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1336 TKLRQLEDERNSLQDQLDEEMEAKQNLERhvstLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEglsqQYEEKAAAY 1415
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEE----LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE----EDKKKAEEA 1749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1416 DKLEKTKNRLQQElddlvvdldnQRQLVSNLEKKQKKFDQLLAEEknisSKYADERDRAEAEAREKETKAlSLARALEEA 1495
Cdd:PTZ00121 1750 KKDEEEKKKIAHL----------KKEEEKKAEEIRKEKEAVIEEE----LDEEDEKRRMEVDKKIKDIFD-NFANIIEGG 1814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1496 LEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEE-------MKTQLEELEDELQATEDAKLRLEVN 1568
Cdd:PTZ00121 1815 KEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEdgnkeadFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
866-1401 |
4.65e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.71 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAER 945
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 946 kkmaqqmLDLEEQLEEEEAARQKLQLEKVTAEAkikkleddilvMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNL 1025
Cdd:PRK02224 286 -------ERLEELEEERDDLLAEAGLDDADAEA-----------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1026 TKlkskhesMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQ 1105
Cdd:PRK02224 348 RE-------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1106 KNNALKKIRELEGHISDLQEDLDSERAARNK----------AEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQE 1175
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1176 VTVLKKALDEETRSHEAQ--VQEMRQKHTQAVEELTEQLEQFKRAKANLD-------KSKQTLEKENADLAGELRVLGQA 1246
Cdd:PRK02224 501 AEDLVEAEDRIERLEERRedLEELIAERRETIEEKRERAEELRERAAELEaeaeekrEAAAEAEEEAEEAREEVAELNSK 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1247 KQEVEHKKKKLEvQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVAslGSQLQDTQELLQE 1326
Cdd:PRK02224 581 LAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD--EARIEEAREDKER 657
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1327 ETRQKLNVSTKLRQLEDERNSLQDQ---LDEEMEAKQNL-ERHVstlniQLSDSKKKLQDFASTIEVMEEGKKRLQKEM 1401
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELrERRE-----ALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
864-1567 |
4.91e-16 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 84.78 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 864 IKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETElyAEAEEMRVRLAAKKQELEEILHEMEARLeeeedrgqqlQA 943
Cdd:pfam15921 132 IRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEGVLQEIRSILVDFE----------EA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 944 ERKKMAQQMLDLEEQLEEEEAARQKLQLEkvtAEAKIKKLEDDILVMDDQNSKLSKERK-----LLEERVSDLTTNLAEE 1018
Cdd:pfam15921 200 SGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1019 EEKAKNLTKLKSKHESMISELEVRLKK-EEKSRQELEKLKRKLegdaSDFHEQIADLQAQIAELKMQLAKKEEELQAALA 1097
Cdd:pfam15921 277 EVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQL----SDLESTVSQLRSELREAKRMYEDKIEELEKQLV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1098 RLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKA---EKQK------RDLGEE--LEALKTELED------TLD 1160
Cdd:pfam15921 353 LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKElslEKEQnkrlwdRDTGNSitIDHLRRELDDrnmevqRLE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1161 S--TATQQELRAKREQEVTVL--KKALDEETRSHEAQVQEMRQKHTQAVEELTEQ---LEQFKRAKANLDKSKQ----TL 1229
Cdd:pfam15921 433 AllKAMKSECQGQMERQMAAIqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKkmtLESSERTVSDLTASLQekerAI 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1230 EKENADLAGELRVLGQAKQEVEHKKKKLEvQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKD 1309
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGD-HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1310 VASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVstlniqlSDSKKKLQDFASTIEV 1389
Cdd:pfam15921 592 KAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV-------KDIKQERDQLLNEVKT 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1390 MEEGKKRLQKEMEGLSQQYEEKAaayDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQL-LAEEKNISSKya 1468
Cdd:pfam15921 665 SRNELNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK-- 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1469 derdRAEAEAREKETKALSLARALEEALEAKEELERTNkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKT-- 1546
Cdd:pfam15921 740 ----RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNK--LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVal 813
|
730 740
....*....|....*....|....*.
gi 241982718 1547 -----QLEELEDELQATEDAKLRLEV 1567
Cdd:pfam15921 814 dkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1036-1707 |
8.65e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.81 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1036 ISELEVRLKKEEKSRQELEKLK------RKLEGDASDFHEQIADLQAQIAELKMQLAKKE-EELQAALARLDEEI----A 1104
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRelaeryAAARERLAELEYLRAALRLWFAQRRLELLEAElEELRAELARLEAELerleA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1105 QKNNALKKIRELEGHISD--------LQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:COG4913 317 RLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1177 TVLKKALDEETRSHEAQVQEMRQKHtqavEELTEQLEQFKRAKANLDKS--------KQTLEKENADL--AGEL------ 1240
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARllalrdalAEALGLDEAELpfVGELievrpe 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1241 ---------RVLG--------------QAKQEVEHKKKKLEVQLQDLQSKCSDGERARAE---LSDKV------------ 1282
Cdd:COG4913 473 eerwrgaieRVLGgfaltllvppehyaAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDpdsLAGKLdfkphpfrawle 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1283 HKLQNE-----VESVTGMlnEAEGKAIKLAKDVASLGS--QLQDTQELLQE-----ETRQKLNVstklrqLEDERNSLQD 1350
Cdd:COG4913 553 AELGRRfdyvcVDSPEEL--RRHPRAITRAGQVKGNGTrhEKDDRRRIRSRyvlgfDNRAKLAA------LEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1351 QLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEegkkrLQKEMEGLSQQYEEKAAAYDKLEktknRLQQELD 1430
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS-----AEREIAELEAELERLDASSDDLA----ALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1431 DLVVDLDNQRQLVSNLEKKQKKFDQllaeeknisskyadERDRAEAEAREKETKALSLARaleeaLEAKEELERTNKMLK 1510
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEK--------------ELEQAEEELDELQDRLEAAED-----LARLELRALLEERFA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1511 AEMEDLVsskddvgknvheLEKSKRALETQMEEMKTQLEELEDELQATedaklrlevnMQALKGQFE---RDLQARDEQN 1587
Cdd:COG4913 757 AALGDAV------------ERELRENLEERIDALRARLNRAEEELERA----------MRAFNREWPaetADLDADLESL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1588 EEKRRQLQRQ----LHEYETELEDERKQRalaaaakkkLEGDLKDLELQADSAIKGREEAIKQL------------RKLQ 1651
Cdd:COG4913 815 PEYLALLDRLeedgLPEYEERFKELLNEN---------SIEFVADLLSKLRRAIREIKERIDPLndslkripfgpgRYLR 885
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1652 --------AQMKDFQRELDDARASRDEifATSKENEKKakslEADLMQLQEDLAAAERARKQAD 1707
Cdd:COG4913 886 learprpdPEVREFRQELRAVTSGASL--FDEELSEAR----FAALKRLIERLRSEEEESDRRW 943
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
978-1805 |
8.67e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 83.94 E-value: 8.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 978 AKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEeekaknLTKLKSKHESMISELEVRLKKEEKSRQELEKLK 1057
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1058 RKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLdeeiaqknnalkkirELEGhisdLQEDLDSERAARNKA 1137
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL---------------ELDG----FERGPFSERQIKNFH 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1138 EKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMR------QKHTQAVEELTEQ 1211
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKfvikelQQLEGSSDRILEL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1212 LEQFKRAKANLDKSKQ------------TLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERAR---- 1275
Cdd:TIGR00606 477 DQELRKAERELSKAEKnsltetlkkevkSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRkiks 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1276 ----------------AELSDKVHKLQNEVesvtgmlNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKL- 1338
Cdd:TIGR00606 557 rhsdeltsllgyfpnkKQLEDWLHSKSKEI-------NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLf 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1339 -----RQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAA 1413
Cdd:TIGR00606 630 dvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1414 AYDKLEKTKNRLQQELDDLVVDLDNQRqlvSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKET--KALSLARA 1491
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQ---SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKV 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1492 LEEALEAKEELERTNKMLKAEMEDLVSSKD--DVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNM 1569
Cdd:TIGR00606 787 CLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1570 QALKGQferdlQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKqlrK 1649
Cdd:TIGR00606 867 NELKSE-----KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK---K 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1650 LQAQMKDFQRELDDARASRDEIFATSKEN-EKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQ 1728
Cdd:TIGR00606 939 AQDKVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1729 DEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVE 1805
Cdd:TIGR00606 1019 DNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1192-1933 |
1.50e-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: 83.19 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1192 AQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEK--ENADLAGELRVLGQAKQEVE-----HKKKKLEVQLQDL 1264
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlrREREKAERYQALLKEKREYEgyellKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1265 QSKCSDGERARAELSDKVHKLQNEVESVTGMLNEaegkaikLAKDVASLGSQLQdtqellqeetrqkLNVSTKLRQLEDE 1344
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEE-------LNKKIKDLGEEEQ-------------LRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1345 RNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNR 1424
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1425 LQQELDDLVVDLDnqrQLVSNLEKKQKKFDQLLAEEKNISSKYADerdrAEAEAREKETKALSLARALEEALEAKEELER 1504
Cdd:TIGR02169 383 TRDELKDYREKLE---KLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1505 TNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQF-------- 1576
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVaqlgsvge 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1577 -------------------ERDLQARDEQNEEKRRQLQRQlheyeTELEDERKQRALAAAAKKKLEG------DLKDLEL 1631
Cdd:TIGR02169 536 ryataievaagnrlnnvvvEDDAVAKEAIELLKRRKAGRA-----TFLPLNKMRDERRDLSILSEDGvigfavDLVEFDP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1632 QADSAIK------GREEAIKQLRKL--QAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERAR 1703
Cdd:TIGR02169 611 KYEPAFKyvfgdtLVVEDIEAARRLmgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1704 kqadlekeelaeelasslsgrNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKN 1783
Cdd:TIGR02169 691 ---------------------SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1784 ESARQQLERQNKELRSKLQEVEgAVKAKLKSTVAALEAKIAQLE--------EQVEQEAREKQAATKSLKQKDKKLKEVL 1855
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1856 LQVEDERKMAEQY----KEQAEKGNTKVKQLKRQLEEAEEESQRINANRR-------KLQRELDEATESNEAMGREVNAL 1924
Cdd:TIGR02169 829 EYLEKEIQELQEQridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRdlesrlgDLKKERDELEAQLRELERKIEEL 908
|
....*....
gi 241982718 1925 KSKLRRGNE 1933
Cdd:TIGR02169 909 EAQIEKKRK 917
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1315-1933 |
1.95e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1315 SQLQDT-QELLQ----EETRQKL-NVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVstlniQLSDSKKKLQDFASTIE 1388
Cdd:PRK02224 149 SDRQDMiDDLLQlgklEEYRERAsDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHE-----RLNGLESELAELDEEIE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1389 VMEEGKKRLQkemeglsqqyEEKAAAYDKLEKTKNRlQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYA 1468
Cdd:PRK02224 224 RYEEQREQAR----------ETRDEADEVLEEHEER-REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1469 DERD--RAEAEAREKETKALSLARALEEALEAKeelertnkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKT 1546
Cdd:PRK02224 293 EERDdlLAEAGLDDADAEAVEARREELEDRDEE---------LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1547 QLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERkqralaaaakkkleGDL 1626
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIE-ELRERFGDAPVDLGNAEDFLEELREERDELR--------------ERE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1627 KDLElqadSAIKGREEAIKQLRKLQAQMK--DFQRELDDArasrdEIFATSKENEKKAKSLEADLMQLQEDLAAAERARK 1704
Cdd:PRK02224 429 AELE----ATLRTARERVEEAEALLEAGKcpECGQPVEGS-----PHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1705 QADLEKEELaeelasslSGRNTLQDEKRRLEARIAQLEEEleeeqgnMEAMSDRVRKATLQAEQLSNELATERSTAQKNE 1784
Cdd:PRK02224 500 RAEDLVEAE--------DRIERLEERREDLEELIAERRET-------IEEKRERAEELRERAAELEAEAEEKREAAAEAE 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1785 SARQQLERQNKELRSKLQEVEGAVKAKlkSTVAALEAKIAQLEEQVEqEAREKQAAtkslkqkdkklkevLLQVEDERKm 1864
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIE-RLREKREA--------------LAELNDERR- 626
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1865 aEQYKEQAEKgntkVKQLKRQ-----LEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNE 1933
Cdd:PRK02224 627 -ERLAEKRER----KRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1185-1707 |
2.18e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1185 EETRSHEAqVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENadlagelrvlgQAKQEVEhkkkKLEVQLQDL 1264
Cdd:PRK02224 200 EEKDLHER-LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE-----------ERREELE----TLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1265 QSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLgSQLQDTQELLQEETRQKL-NVSTKLRQLED 1343
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV-EARREELEDRDEELRDRLeECRVAAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1344 ERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKN 1423
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1424 RLQQELDDLVVDLdnqrqlvSNLEKKQKKFDQLLAEEKNIS-------SKYADERDRAEaEAREKETKALSLARALEEAL 1496
Cdd:PRK02224 423 ELREREAELEATL-------RTARERVEEAEALLEAGKCPEcgqpvegSPHVETIEEDR-ERVEELEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1497 EAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALK--- 1573
Cdd:PRK02224 495 EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReev 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1574 GQFERDLQARDEQNE--EKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDL-ELQADSAIKGREEAIKQLRKL 1650
Cdd:PRK02224 575 AELNSKLAELKERIEslERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKrERKRELEAEFDEARIEEARED 654
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1651 QAQMKDFQR----ELDDARASRDEIFAT--SKENE-KKAKSLEADLMQLQEDLAAAERARKQAD 1707
Cdd:PRK02224 655 KERAEEYLEqveeKLDELREERDDLQAEigAVENElEELEELRERREALENRVEALEALYDEAE 718
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1054-1908 |
5.56e-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: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1054 EKLKRKLEgdasDFHEQIADLQAQIAELKMQLAKKEEELQAALARLD---EEIAQKNNALKKIRELEghiSDLQEDLdse 1130
Cdd:pfam15921 74 EHIERVLE----EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQtklQEMQMERDAMADIRRRE---SQSQEDL--- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1131 raarnkaEKQKRDLGEELEALKTELEDTLDSTATQQElrakreqevtvlkkALDEETRSHEAQVQEMRQkhtqaveeLTE 1210
Cdd:pfam15921 144 -------RNQLQNTVHELEAAKCLKEDMLEDSNTQIE--------------QLRKMMLSHEGVLQEIRS--------ILV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1211 QLEQFKRAKANLDKSKQTLEKENADLAGElRVLGQAKQEVEHKKKKL---EVQLQDLQSKCSDG-ERARAELSDKVHKLQ 1286
Cdd:pfam15921 195 DFEEASGKKIYEHDSMSTMHFRSLGSAIS-KILRELDTEISYLKGRIfpvEDQLEALKSESQNKiELLLQQHQDRIEQLI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1287 NEVE-SVTGMLNEAEgkaiklakDVASLGSQLQDTQELLQEETRQKlnVSTKLRQLEDernslqdqldeemeakqnLERH 1365
Cdd:pfam15921 274 SEHEvEITGLTEKAS--------SARSQANSIQSQLEIIQEQARNQ--NSMYMRQLSD------------------LEST 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1366 VSTLNIQLSDSKKKLQDfastieVMEEGKKRLQKEMEGLSQQYEEKaaayDKLEKTKNRLQQELDDLVVDLDNQRQLVSn 1445
Cdd:pfam15921 326 VSQLRSELREAKRMYED------KIEELEKQLVLANSELTEARTER----DQFSQESGNLDDQLQKLLADLHKREKELS- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1446 LEKKQKK--FDQLLAEEKNISSKYADERDR-AEAEAREKETKALSLARALEEALEAKEELERTNKMLKAE--MEDLVSSK 1520
Cdd:pfam15921 395 LEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSslTAQLESTK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1521 DDVGKNVHELEKSKRALETQ---MEEMKTQLEELEDELQAT--EDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQ 1595
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1596 RQLHEYETELEDERKQRAlaaaakkklegDLKDLELQadsaiKGREEAIKQLRK--LQAQMKDFQRELDDARASRDEIFA 1673
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIE-----------NMTQLVGQ-----HGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1674 TSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIaqleeeleeeQGNME 1753
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF----------RNKSE 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1754 AMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKaklkstvaALEAKIAQLEEQVEQE 1833
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID--------ALQSKIQFLEEAMTNA 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1834 AREKQAatksLKQKDKKLKEVLLQVEDER-KMA---EQYKEQAEKGNTKVKQLKRQLEEAEE---------ESQRINANR 1900
Cdd:pfam15921 761 NKEKHF----LKEEKNKLSQELSTVATEKnKMAgelEVLRSQERRLKEKVANMEVALDKASLqfaecqdiiQRQEQESVR 836
|
....*...
gi 241982718 1901 RKLQRELD 1908
Cdd:pfam15921 837 LKLQHTLD 844
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1482 |
6.87e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.34 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 849 RQEEEMQAKEEEmqKIKERQQKAETELKELEQKHtqlAEEKTLLQEQLQAETELYAE----AEEMRVRLAAKKQE----L 920
Cdd:PTZ00121 1140 RKAEEARKAEDA--KRVEIARKAEDARKAEEARK---AEDAKKAEAARKAEEVRKAEelrkAEDARKAEAARKAEeerkA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 921 EEILHEMEARLEEEEDRGQQLQ--AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDiLVMDDQNSKLS 998
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKkdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE-LKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 999 KERKLLEERVSDLTTNLAEEEEKAKNLTK-----------LKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDF 1067
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKkaeeakkkadaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1068 HEqiADLQAQIAELKMQLAKKEEELQaalaRLDEEIAQKNNALKKIRELEGHISDLQEDLDSERaarnKAEKQKRDLGEE 1147
Cdd:PTZ00121 1374 EE--AKKKADAAKKKAEEKKKADEAK----KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK----KADEAKKKAEEA 1443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1148 LEAlkTELEDTLDSTATQQELRAKREQEvtvlKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQ 1227
Cdd:PTZ00121 1444 KKA--DEAKKKAEEAKKAEEAKKKAEEA----KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1228 TLEKENADlagELRVLGQAKQEVEHKK---KKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAI 1304
Cdd:PTZ00121 1518 AEEAKKAD---EAKKAEEAKKADEAKKaeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1305 KLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFA 1384
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1385 STIEVMEEGKKRLQKEMEGLSQQYEEKAAAYD---KLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEE- 1460
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEe 1754
|
650 660
....*....|....*....|....
gi 241982718 1461 --KNISSKYADERDRAEAEAREKE 1482
Cdd:PTZ00121 1755 ekKKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1074-1910 |
7.50e-15 |
|
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: 80.79 E-value: 7.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1074 LQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKT 1153
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1154 ELEDTLDSTATQQELRAKREQEVTVLKKALDEETRS--HEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEK 1231
Cdd:pfam02463 220 ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESskQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1232 ENADLAGELRV-LGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDV 1310
Cdd:pfam02463 300 SELLKLERRKVdDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1311 ASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLErhvstlniqlsDSKKKLQDFASTIEVM 1390
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL-----------EEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1391 EEGKKRLQKEMEGLSQQYEEK-AAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYAD 1469
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKsEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1470 ERDRAEAEAREKETKALSLARALEEALEAKEELERTNKM------------LKAEMEDLVSSKDDVGKNVHELEKSK--- 1534
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVraltelplgarkLRLLIPKLKLPLKSIAVLEIDPILNLaql 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1535 -RALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRR--QLQRQLHEYETELEDERKQ 1611
Cdd:pfam02463 609 dKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASlsELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1612 RALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLM- 1690
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSe 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1691 -QLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKaTLQAEQL 1769
Cdd:pfam02463 769 lSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL-ELKEEQK 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1770 SNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSL-KQKD 1848
Cdd:pfam02463 848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERiKEEA 927
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1849 KKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEA 1910
Cdd:pfam02463 928 EILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
862-1482 |
8.26e-15 |
|
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: 80.54 E-value: 8.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKeleQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARL---------- 931
Cdd:pfam05483 88 EKIKKWKVSIEAELK---QKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnllketc 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 932 EEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIK-KLEDDILVMDDQNSKLSKERKLLEERVSD 1010
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1011 LTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHeqiADLQAQIAELKMQlakkEE 1090
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIK---MSLQRSMSTQKAL----EE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1091 ELQAA---LARLDEEIAQKNNALKKIR--------ELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTL 1159
Cdd:pfam05483 318 DLQIAtktICQLTEEKEAQMEELNKAKaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1160 DSTATQ----------------------------QELRAKrEQEVTVLKKALDEETRSHEAQVQEMR---QKHTQAVEEL 1208
Cdd:pfam05483 398 KFKNNKeveleelkkilaedeklldekkqfekiaEELKGK-EQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1209 TEQLEQFKRAKANLDKSKQTLEKENADLAGELR----VLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHK 1284
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1285 LQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLER 1364
Cdd:pfam05483 557 FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1365 HVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQ---------------EL 1429
Cdd:pfam05483 637 KVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvalmekhkhQY 716
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1430 DDLVVDLDNQRQLVSNLEKKQKKFDQLLAEE-KNISSKYADERDRAEAEAREKE 1482
Cdd:pfam05483 717 DKIIEERDSELGLYKNKEQEQSSAKAALEIElSNIKAELLSLKKQLEIEKEEKE 770
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
828-1396 |
1.18e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 828 KLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEEEMQKIK--ERQQKAEtELKELEQKHT-----QLAEEKtllqeqlQAET 900
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKkaEEKKKAD-EAKKAEEKKKadeakKKAEEA-------KKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 901 ELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKi 980
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK- 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 981 KKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEE----EEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKL 1056
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEakkkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1057 KRKLEGDASDFHEQIADLQAQIAELKM--QLAKKEEELQAALARLDEEIAQKNNALKKIRELEGhisdlQEDLDSERAAR 1134
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK-----AEEKKKADELK 1552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1135 NKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQA-----VEELT 1209
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkkAEEEK 1632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1210 EQLEQFKRAKANLDKSKQTLEKENADlaGELRVLGQAKQEVEHKKKKLEVQlqdlqsKCSDGERARAELSDKVHKLQNEV 1289
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEE--NKIKAAEEAKKAEEDKKKAEEAK------KAEEDEKKAAEALKKEAEEAKKA 1704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1290 ESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQklnvSTKLRQLEDERNSLQdQLDEEMEAKQNLERHVSTL 1369
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIA-HLKKEEEKKAEEIRKEKEA 1779
|
570 580 590
....*....|....*....|....*....|....*..
gi 241982718 1370 NIQ----------LSDSKKKLQDFASTIEVMEEGKKR 1396
Cdd:PTZ00121 1780 VIEeeldeedekrRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
990-1664 |
2.40e-14 |
|
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: 79.01 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 990 MDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHEsmiselevrlKKEEKSRQELEKLKRKLEGDASDFHE 1069
Cdd:pfam15921 94 LNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRES----------QSQEDLRNQLQNTVHELEAAKCLKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1070 QIADLQAQIAELKMQLAKKE---EELQAALARLDEEIAQK---------------NNALKKI-RELEGHISDLQ------ 1124
Cdd:pfam15921 164 MLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyehdsmstmhfrslGSAISKIlRELDTEISYLKgrifpv 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1125 ----EDLDSEraARNKAE---KQKRDLGEEL----------------------EALKTELEDTLDSTATQQELRAKR--- 1172
Cdd:pfam15921 244 edqlEALKSE--SQNKIElllQQHQDRIEQLiseheveitgltekassarsqaNSIQSQLEIIQEQARNQNSMYMRQlsd 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1173 -EQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTE---QLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQ 1248
Cdd:pfam15921 322 lESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEartERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNK 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1249 EVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVE-SVTGMLNEAEGKAIKLAKdVASLGSQLQDTQELL--- 1324
Cdd:pfam15921 402 RLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEK-VSSLTAQLESTKEMLrkv 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1325 -QEETRQKLNVSTKLRQLEDERNSLQDQldeemeakqnlERHVSTLNIQLSDSKK----KLQDFAStIEVMEEGKKRLQK 1399
Cdd:pfam15921 481 vEELTAKKMTLESSERTVSDLTASLQEK-----------ERAIEATNAEITKLRSrvdlKLQELQH-LKNEGDHLRNVQT 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1400 EMEGLSQQYEEKaaaydklEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAR 1479
Cdd:pfam15921 549 ECEALKLQMAEK-------DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1480 EKETKALSLARALEEALEAKEELERTNKMLKAEMEDLV----SSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDEL 1555
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1556 QAtedAKLRLEVNMQALKGQFERDLQA------RDEQNEEKRRQ---LQRQLHEYETELEDERKQRALAAAAKKKLEGDL 1626
Cdd:pfam15921 702 KS---AQSELEQTRNTLKSMEGSDGHAmkvamgMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL 778
|
730 740 750
....*....|....*....|....*....|....*...
gi 241982718 1627 KDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDA 1664
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
942-1854 |
2.71e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 78.86 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEK 1021
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 AKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLK-------RKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQA 1094
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELkllakeeEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1095 ALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLdstatqqELRAKREQ 1174
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL-------ELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1175 EVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKK 1254
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1255 KKLEVQLQDLQskcSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNV 1334
Cdd:pfam02463 486 LELLLSRQKLE---ERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1335 STKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSkkKLQDFASTIEVMEEGKKRLQKEMeglsqqyeekaaa 1414
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN--LAQLDKATLEADEDDKRAKVVEG------------- 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1415 ydklektKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEE 1494
Cdd:pfam02463 628 -------ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1495 ALEAKEELERTNKMLKAEMEDLvsskddvgknvhELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKG 1574
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEEL------------LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1575 QFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKqralAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQM 1654
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR----ALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1655 KDFQRELDDARASRDEIFATSKENEKKAKSleadlmQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRL 1734
Cdd:pfam02463 845 EQKLEKLAEEELERLEEEITKEELLQELLL------KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1735 EARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERStaQKNESARQQLERQNKELRSKLQEVEGAVKAKLKS 1814
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN--KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 241982718 1815 TVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEV 1854
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKV 1036
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
4.63e-14 |
|
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: 67.84 E-value: 4.63e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 241982718 32 AKKLVWVPSEKQGFEAASIKEEKGDEVVVELvENGKKVTVGKDDI 76
Cdd:pfam02736 2 AKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
979-1451 |
6.39e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 77.37 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 979 KIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKR 1058
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1059 KLEGDASDFHEQIAdlQAQIAELKMQLAKKEEELQAALARLDEE---IAQKNNALKKIR----ELEGHISDLQEDLDSER 1131
Cdd:TIGR04523 292 QLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNnkiISQLNEQISQLKkeltNSESENSEKQRELEEKQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1132 AARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEaQVQEMRQKHTQAVEELTEQ 1211
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE-RLKETIIKNNSEIKDLTNQ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1212 LEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVES 1291
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1292 VTGMLNEAEGKAIKLAKDVASLGSQLqdtqellqeetrqklnvstKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNI 1371
Cdd:TIGR04523 529 LESEKKEKESKISDLEDELNKDDFEL-------------------KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1372 QLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQK 1451
Cdd:TIGR04523 590 LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1085-1911 |
8.41e-14 |
|
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: 77.57 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1085 LAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERA---ARNKAEKQKRDLgEELEALKTELEDTLDS 1161
Cdd:pfam12128 188 MHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGimkIRPEFTKLQQEF-NTLESAELRLSHLHFG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1162 TATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADlagelr 1241
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIE------ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1242 vlgQAKQEVEhkkkklevQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEaegkaiKLAKDVASLGSQLQDTQ 1321
Cdd:pfam12128 341 ---TAAADQE--------QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIR 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1322 EllqEETRQKLNVSTKLRQLEDE-RNSLQDQLDEEMEAKQNLERHVSTLNIQL------SDSKKKLQDFASTIEVMEE-- 1392
Cdd:pfam12128 404 E---ARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLnqatatPELLLQLENFDERIERAREeq 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1393 -----GKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQR-QLVSNLEKKQKKFDQLLAeeKNISSK 1466
Cdd:pfam12128 481 eaanaEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIG--KVISPE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1467 YADERDRAEAEAREKETKALSL-ARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMK 1545
Cdd:pfam12128 559 LLHRTDLDPEVWDGSVGGELNLyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1546 TQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETEL--------EDERKQRALAAA 1617
Cdd:pfam12128 639 REETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHqawleeqkEQKREARTEKQA 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1618 AKKKLEGDLKDLELQADSAIKGREEAIKqlrklqAQMKDFQRELDDARASRDEifatskeNEKKAKSLEADLMQLQEDLA 1697
Cdd:pfam12128 719 YWQVVEGALDAQLALLKAAIAARRSGAK------AELKALETWYKRDLASLGV-------DPDVIAKLKREIRTLERKIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1698 AAERARKQADLEKEELaeelasslsgRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRkatLQAEQLSNELater 1777
Cdd:pfam12128 786 RIAVRRQEVLRYFDWY----------QETWLQRRPRLATQLSNIERAISELQQQLARLIADTK---LRRAKLEMER---- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1778 staqknESARQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQ 1857
Cdd:pfam12128 849 ------KASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1858 ------VEDERKMAEQYKEQAEKG-----------------NTKVKQLKRQLEEA---------------EEESQRINAN 1899
Cdd:pfam12128 923 hsgsglAETWESLREEDHYQNDKGirlldyrklvpyleqwfDVRVPQSIMVLREQvsilgvdltefydvlADFDRRIASF 1002
|
890
....*....|..
gi 241982718 1900 RRKLQRELDEAT 1911
Cdd:pfam12128 1003 SRELQREVGEEA 1014
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1338-1927 |
2.63e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 75.44 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1338 LRQLEDERNSLQDQLDEEMEAKQN-------LERHVSTLNIQLSDSKKKLQD-------FASTIEVMEEGKKRLQKEMEG 1403
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNsnnkikiLEQQIKDLNDKLKKNKDKINKlnsdlskINSEIKNDKEQKNKLEVELNK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1404 LSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKF-DQLLAEEKNIsskyaderDRAEAEAREKE 1482
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLeKEKLNIQKNI--------DKIKNKLLKLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1483 TKALSLaraleealeakEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQateDAK 1562
Cdd:TIGR04523 201 LLLSNL-----------KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN---KIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1563 LRLEVNMQALkgqferdlqardEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAK-----KKLEGDLKDLELQAD--- 1634
Cdd:TIGR04523 267 KQLSEKQKEL------------EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISqnn 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1635 SAIKGREEAIKQLRK-----------LQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERAR 1703
Cdd:TIGR04523 335 KIISQLNEQISQLKKeltnsesenseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1704 KQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEE-------LEEEQGNMEAMSDRVRKATLQAEQLSNELATE 1776
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIiknldntRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1777 RSTAQKNESARQQLERQNKELRSKLQEVEGAVKaKLKSTVAALEAKIAQLE------------EQVEQEAREKQA----- 1839
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEdelnkddfelkkENLEKEIDEKNKeieel 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1840 --ATKSLKQKDKKLKEVLLQVEDERKmaEQYKEQAEKGnTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAM 1917
Cdd:TIGR04523 574 kqTQKSLKKKQEEKQELIDQKEKEKK--DLIKEIEEKE-KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
650
....*....|
gi 241982718 1918 GREVNALKSK 1927
Cdd:TIGR04523 651 KETIKEIRNK 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
894-1475 |
1.62e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 894 EQLQAETELYAEAEEMRVRLAAKKQELEEIlhemearleeeEDRGQQLQAERKKMAQQmlDLEEQLEEEEAARQKLQLek 973
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPI-----------RELAERYAAARERLAEL--EYLRAALRLWFAQRRLEL-- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 974 vtAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEeeKAKNLTKLKSKHESMISELEVRLKKEEKSRQEL 1053
Cdd:COG4913 293 --LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1054 EKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAA 1133
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1134 RNKAEKQKRD----LGEELEALKTELE---------------------------DTLDSTATQQELR-------AKREQE 1175
Cdd:COG4913 449 LAEALGLDEAelpfVGELIEVRPEEERwrgaiervlggfaltllvppehyaaalRWVNRLHLRGRLVyervrtgLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1176 VTVLKKALDE--ETRSHEAQ---VQEMRQKHTQAVEELTEQLEQFKRA--KANLDKSKQTL-EKENADLAGELRVLGqak 1247
Cdd:COG4913 529 PRLDPDSLAGklDFKPHPFRawlEAELGRRFDYVCVDSPEELRRHPRAitRAGQVKGNGTRhEKDDRRRIRSRYVLG--- 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1248 QEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQN----------------EVESVTGMLNEAEGKAIKLAK--- 1308
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVASAEREIAELEAELERLDAssd 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1309 DVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFAstiE 1388
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD---A 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1389 VMEEGKKRLQKEMEGLSqqyEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQ-----------RQLVSN-LEKKQKKFDQL 1456
Cdd:COG4913 763 VERELRENLEERIDALR---ARLNRAEEELERAMRAFNREWPAETADLDADleslpeylallDRLEEDgLPEYEERFKEL 839
|
650 660
....*....|....*....|....
gi 241982718 1457 LAEE-----KNISSKYADERDRAE 1475
Cdd:COG4913 840 LNENsiefvADLLSKLRRAIREIK 863
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
862-1432 |
1.92e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.69 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETEL---KELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRg 938
Cdd:TIGR00618 314 TELQSKMRSRAKLLmkrAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 939 QQLQAERKKMaQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEE 1018
Cdd:TIGR00618 393 QKLQSLCKEL-DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1019 EEKAKNltklkskhesmiseLEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAqiaelKMQLAKKEEELQAALAR 1098
Cdd:TIGR00618 472 EQQLQT--------------KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP-----ARQDIDNPGPLTRRMQR 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1099 LDEEIAQKNNALKKIR----ELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELR----- 1169
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlac 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1170 AKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLA------GELRVL 1243
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLalqkmqSEKEQL 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1244 GQAKQEVEHKKKKLEVQLQDLQSKcsdgERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDV--ASLGSQLQDTQ 1321
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEY----DREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1322 ELLQEETRqklnvSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVST-----LNIQLSDSKKKLQDFASTIEVMEEgKKR 1396
Cdd:TIGR00618 769 EVTAALQT-----GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeipsdEDILNLQCETLVQEEEQFLSRLEE-KSA 842
|
570 580 590
....*....|....*....|....*....|....*.
gi 241982718 1397 LQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDL 1432
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1326-1889 |
2.18e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1326 EETRQKLN-VSTKLRQLEDERNSLQ------DQLDEEMEAKQ----NLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGK 1394
Cdd:PRK03918 203 EEVLREINeISSELPELREELEKLEkevkelEELKEEIEELEkeleSLEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1395 KRLqKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRA 1474
Cdd:PRK03918 283 KEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1475 EAEAREKEtkalslaraleealeakeelertnkmLKAEMEDLvsSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDE 1554
Cdd:PRK03918 362 ELYEEAKA--------------------------KKEELERL--KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1555 LQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLqrqLHEYETELEDERKQRALAAAAKKKLEGDLKDLE--LQ 1632
Cdd:PRK03918 414 IGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEkvLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1633 ADSAIKGREEAIKQLRKLQAQMKDFQRE-LDDARASRDEIFATSKENEKKAKSLEADLMQLQE---DLAAAERARKQADL 1708
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1709 EKEELAEELASslSGRNTLQDEKRRLEA--RIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAqknESA 1786
Cdd:PRK03918 571 ELAELLKELEE--LGFESVEELEERLKElePFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1787 RQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREkqaaTKSLKQKDKKLKEVLLQVEDERKMAE 1866
Cdd:PRK03918 646 RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT----LEKLKEELEEREKAKKELEKLEKALE 721
|
570 580
....*....|....*....|...
gi 241982718 1867 QYKEQAEkgntKVKQLKRQLEEA 1889
Cdd:PRK03918 722 RVEELRE----KVKKYKALLKER 740
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1198-1895 |
2.23e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.69 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1198 RQKHTQAVEELTEQLEQFK-RAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLqskcsdgERARA 1276
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLAlMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL-------REALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1277 ELSDKVHKLQNEVESvtgmLNEAEGKAIKLAKDVASLgsQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEM 1356
Cdd:TIGR00618 237 QTQQSHAYLTQKREA----QEEQLKKQQLLKQLRARI--EELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1357 EAKQNLERHVSTLNIQLSDSKKKLQDFAStIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKN------RLQQELD 1430
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSS-IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqhihTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1431 DLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLK 1510
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1511 AEMEDLVSSKddvgkNVHELEKSKRALETQ----MEEMKTQLEELEDELQATEDAKLRLEVNMQALKG------QFERDL 1580
Cdd:TIGR00618 470 EREQQLQTKE-----QIHLQETRKKAVVLArlleLQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeqtyaQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1581 QARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRE 1660
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1661 LDDARASrdeifATSKENEKKAKSLEADLMQLQEDLAAaERARKQADLEKEELAEELASSLSGRNTLQDEKRRLeariAQ 1740
Cdd:TIGR00618 625 QDLQDVR-----LHLQQCSQELALKLTALHALQLTLTQ-ERVREHALSIRVLPKELLASRQLALQKMQSEKEQL----TY 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1741 LEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKEL-RSKLQEVEGAVKAKLKSTVAAL 1819
Cdd:TIGR00618 695 WKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQaRTVLKARTEAHFNNNEEVTAAL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1820 E--AKIAQLEEQVEQEAREKQAATKSLKQK--------DKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEA 1889
Cdd:TIGR00618 775 QtgAELSHLAAEIQFFNRLREEDTHLLKTLeaeigqeiPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKY 854
|
....*.
gi 241982718 1890 EEESQR 1895
Cdd:TIGR00618 855 EECSKQ 860
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1272-1933 |
2.69e-12 |
|
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: 72.46 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1272 ERARAELSDKVHKLQNEvesvtgmLNEA----EGKAIKLAKDVASLGSQLQDtqelLQEETRQKLNVSTKLRQ-LEDERN 1346
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRR-------LNESnelhEKQKFYLRQSVIDLQTKLQE----MQMERDAMADIRRRESQsQEDLRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1347 SLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKK-------LQDFASTIEVMEEGKKRLQKEMEGLSQQYeekaaaYDKLE 1419
Cdd:pfam15921 146 QLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMmlshegvLQEIRSILVDFEEASGKKIYEHDSMSTMH------FRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1420 KTKNRLQQELDDLVVDLDN-----QRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEE 1494
Cdd:pfam15921 220 SAISKILRELDTEISYLKGrifpvEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1495 ALEAKEELERT-NKMLKAEMEDLVSSkddVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALK 1573
Cdd:pfam15921 300 QLEIIQEQARNqNSMYMRQLSDLEST---VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1574 GQFER---DLQARDEQNEEKRRQLQR----------QLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGR 1640
Cdd:pfam15921 377 DQLQKllaDLHKREKELSLEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1641 EEAIKQLRKLQAQMKDFQRELddaRASRDEIFATSKENEKKAKSLEADLMQLQEDlaaaERARKQADLEKEELAEELASS 1720
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEML---RKVVEELTAKKMTLESSERTVSDLTASLQEK----ERAIEATNAEITKLRSRVDLK 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1721 LSGRNTLQDEKRRLeaRIAQLEEELEEEQgnMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSK 1800
Cdd:pfam15921 530 LQELQHLKNEGDHL--RNVQTECEALKLQ--MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1801 LQEVEgAVKAKLKSTVAALEAKIAQLE-EQVE--QEAREKQAATKSLKQ-KDKKLKEVLLQVEDERKMAEQY-------K 1869
Cdd:pfam15921 606 LQEFK-ILKDKKDAKIRELEARVSDLElEKVKlvNAGSERLRAVKDIKQeRDQLLNEVKTSRNELNSLSEDYevlkrnfR 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1870 EQAEKGNTKVKQLKRQLEEAEEESQRI-----------------------------------------------NANRRK 1902
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTrntlksmegsdghamkvamgmqkqitakrgqidalqskiqfleeamtNANKEK 764
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 241982718 1903 ---------LQRELDEATESNEAMGREVNALKSKLRRGNE 1933
Cdd:pfam15921 765 hflkeeknkLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1135-1878 |
2.81e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.31 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1135 NKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKRE---QEVTVLKKALDEETRSHEA--QVQEMRQKHTQAVEELT 1209
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAElltLRSQLLTLCTPCMPDTYHErkQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1210 EQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLqsKCSDGERARAELSDKVHKLQNEV 1289
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1290 ESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRqklnvstkLRQLEDERNSLQDQLDEEMEakqnLERHVSTL 1369
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQQHT----LTQHIHTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1370 NIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK 1449
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1450 QKKFDQLLAEEKNISSKYAderdraeaeaREKETKALSLARALEEALEAKEELERTNKmLKAEMEDLVSSKDDVGK---- 1525
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQIHL----------QETRKKAVVLARLLELQEEPCPLCGSCIH-PNPARQDIDNPGPLTRRmqrg 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1526 --NVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKgqferdlqardEQNEEKRRQLQRQLHEYET 1603
Cdd:TIGR00618 534 eqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK-----------EDIPNLQNITVRLQDLTEK 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1604 ELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMK-DFQRELDDARASRDEIFATSKENEKKA 1682
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLAL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1683 KSLEADLMQLQEDLAAAErarkQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKA 1762
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLA----QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKA 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1763 -TLQAEQLSNELATERSTAQKNESARQQLERQNKELRSK---LQEVEGAVKAKLKSTVAALEA---KIAQLEEQVEQEAR 1835
Cdd:TIGR00618 759 rTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDthlLKTLEAEIGQEIPSDEDILNLqceTLVQEEEQFLSRLE 838
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 241982718 1836 EKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTK 1878
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGI 881
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1458-1972 |
6.26e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1458 AEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAE----MEDLVSSKDD----VGKNVHE 1529
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkAEEARKAEDAkrveIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1530 ---LEKSKRALETQMEEMKTQLEELE--DELQATEDAKlRLEvnmQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETE 1604
Cdd:PTZ00121 1163 arkAEEARKAEDAKKAEAARKAEEVRkaEELRKAEDAR-KAE---AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1605 LEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIK--QLRKLQAQMK-------DFQRELDDARASRDEIFATS 1675
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKadELKKAEEKKKadeakkaEEKKKADEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1676 ---KENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNM 1752
Cdd:PTZ00121 1319 eakKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1753 EAMSDRVR----KATLQAEQLSNELATERSTAQKNESARQQLERQNK--ELRSKLQEVEGAVKAKLKstvaALEAKIAQL 1826
Cdd:PTZ00121 1399 KAEEDKKKadelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKK----AEEAKKADE 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1827 EEQVEQEAREKQAATKSLKQKDKKLKEvLLQVEDERKMAEQYKEQAEKGNT---KVKQLKRQLEEAEEESQRINANRRKL 1903
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKAdeaKKAEEAKKADEAKKAEEKKKADELKK 1553
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1904 QRELDEATESN--EAMGREVNALKSKLRRGNEASFVPSRRAGGRRVIENTDGSEEEMDARDSDFNGTKASE 1972
Cdd:PTZ00121 1554 AEELKKAEEKKkaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
863-1467 |
7.60e-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: 70.82 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 863 KIKERQQKAET---ELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQ 939
Cdd:TIGR04523 76 KIKILEQQIKDlndKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 940 QLQAERKKMAQQMLDLEEqleeeeaarqklqlekvtaeaKIKKLEDDILVMDDQNSKLSKERKLLEERVSdlttnlaeee 1019
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELEN---------------------ELNLLEKEKLNIQKNIDKIKNKLLKLELLLS---------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1020 ekakNLTKLKSKHESMISELEvrlkkeeksrqELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARL 1099
Cdd:TIGR04523 205 ----NLKKKIQKNKSLESQIS-----------ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1100 DEEIAQKNNALKKIRELEGHISDLQ---EDLDSEraarnKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQLKseiSDLNNQ-----KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1177 TVLKKALDEETRSHEAQVQEMRQKHTQaVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKK 1256
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNE-IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1257 LEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVST 1336
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1337 KLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQ--DFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAA 1414
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1415 YDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK----QKKFDQLLAEEKNISSKY 1467
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKElekaKKENEKLSSIIKNIKSKK 640
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1114-1740 |
9.02e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.71 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1114 RELEGHISDLQEDLDSERAARNKAEK--QKRDLGEELEALKTELEDTLDSTATQQELRAK-----REQEVTVLKKALDEE 1186
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1187 TRSHEAQVQEMRQkHTQAVEELTEQLEQFKRAKANLD-KSKQTLEKEnadlageLRVLGQAKQEVEHKKKKLEVQLQDLQ 1265
Cdd:COG4913 301 RAELARLEAELER-LEARLDALREELDELEAQIRGNGgDRLEQLERE-------IERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1266 SKCSDGERARAELSDKVHKLqnevesvtgmlneaegkaiklakdVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDER 1345
Cdd:COG4913 373 LPLPASAEEFAALRAEAAAL------------------------LEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1346 NSLQDQ---LDEEM-EAKQNLERHvstlniqLSDSKKKLQDFASTIEVMEEGkKRLQKEMEGL-----------SQQYEE 1410
Cdd:COG4913 429 ASLERRksnIPARLlALRDALAEA-------LGLDEAELPFVGELIEVRPEE-ERWRGAIERVlggfaltllvpPEHYAA 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1411 KAAAYDKLeKTKNRLQ-QELDDLVVDLDNQR----QLVSNLEKKQKKFDQLLAEEknisskYADERDRA---EAEAREKE 1482
Cdd:COG4913 501 ALRWVNRL-HLRGRLVyERVRTGLPDPERPRldpdSLAGKLDFKPHPFRAWLEAE------LGRRFDYVcvdSPEELRRH 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1483 TKALSLARaleealeakeelertnkmlkaemedLVSSKDDVG-KNVHELEKSKRAL----ETQMEEMKTQLEELEDELQA 1557
Cdd:COG4913 574 PRAITRAG-------------------------QVKGNGTRHeKDDRRRIRSRYVLgfdnRAKLAALEAELAELEEELAE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1558 TEDAKLRLEVNMQALKGQFERDLQARDEQNEEKR-RQLQRQLHEYETELEDERKqralaaaakkkLEGDLKDLELQADSA 1636
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDA-----------SSDDLAALEEQLEEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1637 IKGREEAIKQLRKLQAQMKDFQRELDDARASRDEifATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLekeelaee 1716
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDE--LQDRLEAAEDLARLELRALLEERFAAALGDAVEREL-------- 767
|
650 660
....*....|....*....|....
gi 241982718 1717 lasslsgRNTLQDEKRRLEARIAQ 1740
Cdd:COG4913 768 -------RENLEERIDALRARLNR 784
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1075-1292 |
1.07e-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: 69.02 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1075 QAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTE 1154
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1155 LEDTLDSTATQ--QELRAKREQEVTVLKKALDeetrshEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKE 1232
Cdd:COG4942 99 LEAQKEELAELlrALYRLGRQPPLALLLSPED------FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1233 NADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESV 1292
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1203-1957 |
1.55e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1203 QAVEELTEQLEQFKRAKA----NLDKSKQTLEKENADL-AGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAE 1277
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEkdiiDEDIDGNHEGKAEAKAhVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1278 LSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDV--ASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEE 1355
Cdd:PTZ00121 1107 ETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEE 1186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1356 MEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYdklEKTKNRLQQELDDLVVD 1435
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE---EERNNEEIRKFEEARMA 1263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1436 LDNQRQLVSNLEKKQKKFDQLLAEEKnissKYADERDRAEAEAREKETKalslaraleealeAKEELERTNKMLKAEMED 1515
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEK----KKADEAKKAEEKKKADEAK-------------KKAEEAKKADEAKKKAEE 1326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1516 LVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQArdEQNEEKRRQLQ 1595
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA--DEAKKKAEEDK 1404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1596 RQLHEYETELEDERKQRALAAAAKKKLEGDlkDLELQADSAIKGREEAIKQLRKLQAQ-MKDFQRELDDARASRDEIFAT 1674
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKKADEAKKKAEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1675 SKENEKKAKSLEADlmQLQEDLAAAERARKQADLEKEELAEELASSLsgrNTLQDEKRRLEARIAQLEEEleeeqgnmea 1754
Cdd:PTZ00121 1483 KKADEAKKKAEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADEA---KKAEEAKKADEAKKAEEKKK---------- 1547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1755 mSDRVRKAtlqaeqlsnELATERSTAQKNESARQQLERQNKELRsKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEA 1834
Cdd:PTZ00121 1548 -ADELKKA---------EELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1835 REKQAAtkslkqkdkklkEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESN 1914
Cdd:PTZ00121 1617 EAKIKA------------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 241982718 1915 EAMGREVNALKSKLRRGNEASFVPSRRAGGRRVIENTDGSEEE 1957
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
964-1707 |
4.03e-11 |
|
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: 68.46 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 964 AARQKLQLEKVTAEAKIKKLEDDILVMD--DQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKL------KSKHESM 1035
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCtpCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKreaqeeQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1036 ISELEVRLKKEEKSRQELEKLKRKLegDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRE 1115
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERI--NRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1116 LEGHISDLQEDLDSERAARNKAEKQKRDLgEELEALKTELEDTLdstaTQQELRAKREQEVTVLKKALDEETRsheaqvq 1195
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIR-EISCQQHTLTQHIH----TLQQQKTTLTQKLQSLCKELDILQR------- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1196 emrQKHTQAVEELTEQLEQFK--RAKANLDKSKQTLEKENADLAGELRVLGQAK---QEVEHKKKKLEVQLQDLQSKCSD 1270
Cdd:TIGR00618 408 ---EQATIDTRTSAFRDLQGQlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKihlQESAQSLKEREQQLQTKEQIHLQ 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1271 GERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLakdvaslgsqlqdtqELLQEETRQKLNVSTKLRQLEDERNSLQD 1350
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI---------------DNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1351 QLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAydkLEKTKNRLQQELD 1430
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE---QHALLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1431 DLvvdldnqrQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRaEAEAREKETKALSLARaleealeakeelertNKMLK 1510
Cdd:TIGR00618 627 LQ--------DVRLHLQQCSQELALKLTALHALQLTLTQERVR-EHALSIRVLPKELLAS---------------RQLAL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1511 AEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEdaklrlevnmqalkgqfeRDLQARDEQNEEK 1590
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLG------------------SDLAAREDALNQS 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1591 RRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDE 1670
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
730 740 750
....*....|....*....|....*....|....*...
gi 241982718 1671 IFATSKENEK-KAKSLEADLMQLQEDLAAAERARKQAD 1707
Cdd:TIGR00618 825 TLVQEEEQFLsRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1050-1870 |
4.75e-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: 68.44 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1050 RQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKK-------EEELQAA---LARLDEEIAQKnnalKKIRELEGH 1119
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsaresdlEQDYQAAsdhLNLVQTALRQQ----EKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1120 ISDLQEDLDSERAARNKAEKQKRDLGEELEA-------LKTELED---TLDSTAT-----QQELRAKRE-QEVTVLKKAL 1183
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVQQTraiqyQQAVQALEKaRALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1184 DEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKenadLAGEL---RVLGQAKQEVEH--KKKKLE 1258
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCK----IAGEVersQAWQTARELLRRyrSQQALA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1259 VQLQDLQSKCSDGERARAElsdkvhklQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKL 1338
Cdd:COG3096 512 QRLQQLRAQLAELEQRLRQ--------QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSEL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1339 RQLEDERNSLQDQLDEE----MEAKQNLERhvstLNIQLSdskkklQDFASTIEVMEEGKKRLQKEMEgLSQQYEEKAAA 1414
Cdd:COG3096 584 RQQLEQLRARIKELAARapawLAAQDALER----LREQSG------EALADSQEVTAAMQQLLERERE-ATVERDELAAR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1415 YDKLEKTKNRLQQ-------EL----------------DDLVVD--------LDNQRQ--LVSNLEKKQKKFDQLlaeEK 1461
Cdd:COG3096 653 KQALESQIERLSQpggaedpRLlalaerlggvllseiyDDVTLEdapyfsalYGPARHaiVVPDLSAVKEQLAGL---ED 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1462 NISSKYADERDRAEAEAREKETKALSLAraleealeakeelertnkmlkaemeDLVSSKDdvgknvHELEKSK------- 1534
Cdd:COG3096 730 CPEDLYLIEGDPDSFDDSVFDAEELEDA-------------------------VVVKLSD------RQWRYSRfpevplf 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1535 --RALETQMEEMKTQLEELEDELqatedAKLRLEVN-MQALKGQFERDL-----QARDEQNEEKRRQLQRQLHEYETELE 1606
Cdd:COG3096 779 grAAREKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELERELA 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1607 DERKQralaaaakkklegdlkdlELQADSAIKGREEAIKQLRKLQAQM------------KDFQRELDDARASRDEIF-- 1672
Cdd:COG3096 854 QHRAQ------------------EQQLRQQLDQLKEQLQLLNKLLPQAnlladetladrlEELREELDAAQEAQAFIQqh 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1673 -ATSKENEKKAKSLEADLMQ---LQEDLAAAERARKQADLEKEELaeelaSSLSGRNT---LQDEKRRLeariAQLEEEL 1745
Cdd:COG3096 916 gKALAQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFAL-----SEVVQRRPhfsYEDAVGLL----GENSDLN 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1746 EEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKA-----------KLKS 1814
Cdd:COG3096 987 EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAeaeerarirrdELHE 1066
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 1815 TVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKevllqveDERKMAEQYKE 1870
Cdd:COG3096 1067 ELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAKA 1115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1339-1889 |
4.98e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1339 RQLEDERNSLQDQLDEEMEAKQNLE---RHVSTLnIQLSDSKKKLQDFASTIEVMEEGKKRLQkeMEGLSQQYEEKAAAY 1415
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEdarEQIELL-EPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1416 DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK--QKKFDQLLAEEKnisskyadERDRAEAEAREKETKALSLARALE 1493
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRLEQLER--------EIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1494 EALEAKEELErtnKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALK 1573
Cdd:COG4913 370 ALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1574 GQFERDLQARDEQ------------NEEK-------------------------------RRQLQRQLHEYETELEDERK 1610
Cdd:COG4913 447 DALAEALGLDEAElpfvgelievrpEEERwrgaiervlggfaltllvppehyaaalrwvnRLHLRGRLVYERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1611 QRALAAAAKKKLEGDLKDLELQA--DSAIKGRE-----EAIKQLRK------LQAQMKDFQ--RELDDARASRdEIFATS 1675
Cdd:COG4913 527 ERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFdyvcvDSPEELRRhpraitRAGQVKGNGtrHEKDDRRRIR-SRYVLG 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1676 KENEKKAKSLEADLMQLQEDLAAAERARKQADLEkeelaeelasslsgRNTLQdEKRRLEARIAQLEeeleeeqgnmeam 1755
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAE--------------LDALQ-ERREALQRLAEYS------------- 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1756 SDRVRKATLQAEQLsnELATERSTAQKNESARQQLERQNKELRSKLQEVEGAvKAKLKSTVAALEAKIAQLEEQVEQEAR 1835
Cdd:COG4913 658 WDEIDVASAEREIA--ELEAELERLDASSDDLAALEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1836 EKQAATKSLKQK-----DKKLKEVLLQvEDERKMAEQYKEQAEKGNTKVKQLKRQLEEA 1889
Cdd:COG4913 735 RLEAAEDLARLElrallEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
862-1598 |
5.34e-11 |
|
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: 68.07 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhemearleeeedrgqql 941
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL----------------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 qaERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILvmDDQNSKLSKERKLLEERVSDLTTNLAEEEEK 1021
Cdd:pfam02463 377 --AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL--KEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 AKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDasdfheQIADLQAQIAELKMqLAKKEEELQAALARLDE 1101
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK------LEERSQKESKARSG-LKVLLALIKDGVGGRII 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1102 EIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKK 1181
Cdd:pfam02463 526 SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL-VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1182 ALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQL 1261
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1262 QDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQL 1341
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1342 EDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKT 1421
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1422 KNRLQQELDDLV-VDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKE 1500
Cdd:pfam02463 845 EQKLEKLAEEELeRLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1501 ELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvnmQALKGQFERDL 1580
Cdd:pfam02463 925 EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERY---NKDELEKERLE 1001
|
730
....*....|....*...
gi 241982718 1581 QARDEQNEEKRRQLQRQL 1598
Cdd:pfam02463 1002 EEKKKLIRAIIEETCQRL 1019
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1425-1929 |
6.38e-11 |
|
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: 67.89 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1425 LQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLlAEEKNISSkyadERDRAEAE--AREKETKALSLARaleealeakeel 1502
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKELEKKHQQL-CEEKNALQ----EQLQAETElcAEAEEMRARLAAR------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1503 ertnkmlKAEMEDLVSskdDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDA--KLRLE-VNMQALKGQFERD 1579
Cdd:pfam01576 70 -------KQELEEILH---ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAArqKLQLEkVTTEAKIKKLEED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1580 LQARDEQN---EEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKD 1656
Cdd:pfam01576 140 ILLLEDQNsklSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1657 FQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEA 1736
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1737 RIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATE-RSTAQKNESARQQLERQNKELRSKLqEVEGAVKAKLKST 1815
Cdd:pfam01576 300 ELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQL-EQAKRNKANLEKA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1816 VAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQR 1895
Cdd:pfam01576 379 KQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
490 500 510
....*....|....*....|....*....|....
gi 241982718 1896 INANRRKLQRELDEATESNEAMGREVNALKSKLR 1929
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELLQEETRQKLNLSTRLR 492
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
864-1409 |
7.29e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.94 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 864 IKERQQKAETELKELEQKHTQLAEEKTLLQEQ----LQAETELYAEAEEMRVRLAAKKQELEEILhemEARLEEEEDRGQ 939
Cdd:pfam12128 299 WKEKRDELNGELSAADAAVAKDRSELEALEDQhgafLDADIETAAADQEQLPSWQSELENLEERL---KALTGKHQDVTA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 940 QLQAERKKMAQQMLDLEEQLEEEEAA-RQKLQLEKVTAEAKIKKLEDDI-LVMDDQNSKLSKERKLLEERVSDLTTNLAE 1017
Cdd:pfam12128 376 KYNRRRSKIKEQNNRDIAGIKDKLAKiREARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1018 ---EEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLkRKLEGDASDFHEQIA----DLQAQIAELKMQLAKKEE 1090
Cdd:pfam12128 456 ataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA-RKRRDQASEALRQASrrleERQSALDELELQLFPQAG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1091 ELQAALA------------------------------------------RLDEEIAQKNNALKKIRELEGHISDLQEDLD 1128
Cdd:pfam12128 535 TLLHFLRkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAASEEELRERLDKAEEALQ 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1129 SERAARNKAEKQKRDLGEELEALKTELEDTL----DSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQA 1204
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARtalkNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQL 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1205 VEELTEQLEQFKRAKANLDKSKQTLEKEnadLAGELRV-LGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVH 1283
Cdd:pfam12128 695 DKKHQAWLEEQKEQKREARTEKQAYWQV---VEGALDAqLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIA 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1284 KLQNEVESVTGMLNEAEGKAIKLA---------------KDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSL 1348
Cdd:pfam12128 772 KLKREIRTLERKIERIAVRRQEVLryfdwyqetwlqrrpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKAS 851
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1349 QDQ---LDEEMEAKQNLERHVSTLNIQLSDSKKKLQdFASTIEVMEEGKKRLQKEMEGLSQQYE 1409
Cdd:pfam12128 852 EKQqvrLSENLRGLRCEMSKLATLKEDANSEQAQGS-IGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1011-1241 |
1.40e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1011 LTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLA---K 1087
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAeleK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1088 KEEELQAALARLDEEIAQKNNALKKIreleGHISDLQEDLDSERAARnkAEKQKRDLGEELEALKTELEDTLDSTATQQE 1167
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRL----GRQPPLALLLSPEDFLD--AVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1168 LRAKREQEVTVLKKALDEETRSHeAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELR 1241
Cdd:COG4942 165 LRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1036-1431 |
1.46e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1036 ISELEVRLKKEEKSRQELEKLKRKLEgdasDFHEQIADLQAQIAELKMQLAKKEEELQA--ALARLDEEIAQKNNALKKI 1113
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1114 RELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQ 1193
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1194 VQEMRQKH-TQAVEELTEQLEQFKRAKA-------NLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQ 1265
Cdd:COG4717 229 LEQLENELeAAALEERLKEARLLLLIAAallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1266 SKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQ---------LQDTQELLQ-------EETR 1329
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeeelqleelEQEIAALLAeagvedeEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1330 QKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVS--TLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQ 1407
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
410 420
....*....|....*....|....
gi 241982718 1408 yEEKAAAYDKLEKTKNRLQQELDD 1431
Cdd:COG4717 469 -GELAELLQELEELKAELRELAEE 491
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1186-1971 |
1.48e-10 |
|
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: 66.61 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1186 ETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQ 1265
Cdd:TIGR00606 196 QTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1266 SKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKlakdvaSLGSQLQDTQELLQEETRQKLNVSTKLRQLEDE- 1344
Cdd:TIGR00606 276 SRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR------EKERELVDCQRELEKLNKERRLLNQEKTELLVEq 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1345 -RNSLQDQLDEEMEAKQNLERHVSTLNIQL------SDSKKKLQDFAS-TIEVMEEGKKRLQKEMEGLSQQYEEKAAAYD 1416
Cdd:TIGR00606 350 gRLQLQADRHQEHIRARDSLIQSLATRLELdgfergPFSERQIKNFHTlVIERQEDEAKTAAQLCADLQSKERLKQEQAD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1417 KLEKTKNRLQQELDDLVVDLDNQrqlVSNLEKKQKKFDQLLAEEKNISSKyADERDRAEAEAREKETKALSLARALEEal 1496
Cdd:TIGR00606 430 EIRDEKKGLGRTIELKKEILEKK---QEELKFVIKELQQLEGSSDRILEL-DQELRKAERELSKAEKNSLTETLKKEV-- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1497 eakeelertnKMLKAEMEDLVSSKDDVGKNVHELEKSKRALeTQMEEMKtqlEELEDELQATEDAKLRLEVNMQALKGQF 1576
Cdd:TIGR00606 504 ----------KSLQNEKADLDRKLRKLDQEMEQLNHHTTTR-TQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1577 ERDLQARD---------EQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDL------KDLELQADSAIKGRE 1641
Cdd:TIGR00606 570 PNKKQLEDwlhskskeiNQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1642 EAIKQLRKLQAQM---KDFQRELDDARASR----DEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELA 1714
Cdd:TIGR00606 650 KSSKQRAMLAGATavySQFITQLTDENQSCcpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEML 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1715 EELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAmSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQN 1794
Cdd:TIGR00606 730 GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1795 KELRSKLQEVEGA-----VKAKLKSTVAALEaKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYK 1869
Cdd:TIGR00606 809 AQQAAKLQGSDLDrtvqqVNQEKQEKQHELD-TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1870 EQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEAT----ESNEAMGREVNALKSKLRrgneasfvpsRRAGGR 1945
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIsskeTSNKKAQDKVNDIKEKVK----------NIHGYM 957
|
810 820
....*....|....*....|....*...
gi 241982718 1946 RVIEN--TDGSEEEMDARDSDFNGTKAS 1971
Cdd:TIGR00606 958 KDIENkiQDGKDDYLKQKETELNTVNAQ 985
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1036-1221 |
1.56e-10 |
|
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: 63.41 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1036 ISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNAlKKIRE 1115
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1116 LEghisDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTldstatqQELRAKREQEVTVLKKALDEETRSHEAQVQ 1195
Cdd:COG1579 91 YE----ALQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|....*..
gi 241982718 1196 EMRQKHTQAVEELTEQL-EQFKRAKAN 1221
Cdd:COG1579 160 ELEAEREELAAKIPPELlALYERIRKR 186
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
868-1170 |
1.86e-10 |
|
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: 66.30 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 868 QQKAETELKELEQKHtQLAEEKTLLQEQLQAETELYAEAEEM---------RVRLAAKKQELEEILHEMEARLEEEEDRG 938
Cdd:pfam17380 302 RQEKEEKAREVERRR-KLEEAEKARQAEMDRQAAIYAEQERMamerereleRIRQEERKRELERIRQEEIAMEISRMREL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 939 QQLQAERKKMAQQMldleeQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEE 1018
Cdd:pfam17380 381 ERLQMERQQKNERV-----RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1019 EEKAKNLTKLKSKHESMISElEVRLKKEEKSRQELEKLKRKLegdasdfheqiadLQAQIAELKMQLAKKEEELQAalar 1098
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRK-KLELEKEKRDRKRAEEQRRKI-------------LEKELEERKQAMIEEERKRKL---- 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1099 LDEEIAQKNNALKKirELEGHISDLQEDLDSERAARNKAEKQKRDLGEE---LEALKTELE---DTLDSTATQQELRA 1170
Cdd:pfam17380 518 LEKEMEERQKAIYE--EERRREAEEERRKQQEMEERRRIQEQMRKATEErsrLEAMEREREmmrQIVESEKARAEYEA 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1671-1931 |
2.86e-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: 64.40 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1671 IFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEkeelaeelasslsgRNTLQDEKRRLEARIAQLEEELEEEQG 1750
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE--------------EKALLKQLAALERRIAALARRIRALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1751 NMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNK-ELRSKLQEVEGAVK--AKLKSTVAALEAKIAQLE 1827
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRrlQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1828 EQVEQEAREKQAatksLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKgntKVKQLKRQLEEAEEESQRINANRRKLQREL 1907
Cdd:COG4942 157 ADLAELAALRAE----LEAERAELEALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALI 229
|
250 260
....*....|....*....|....
gi 241982718 1908 DEATESNEAMGREVNALKSKLRRG 1931
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFAALKG 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1274-1487 |
3.76e-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: 64.01 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1274 ARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLD 1353
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1354 EEMEAKQNLERHVSTLNIQ-----------LSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTK 1422
Cdd:COG4942 101 AQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 1423 NRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALS 1487
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
769-1354 |
5.87e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 769 FFRTGVLahleEERDL--KITDVIMAFQAMCRgylARKAFTKRQQQLTAMKVIQRNCAAYLKLRNWQwwRLFTKVKPLLQ 846
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARERL--AELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 847 VTRQEEEMQAKEEEMQKIKERQQKAETELKELEQKHTQLAEEKTLLQEQL-----QAETELYAEAEEMRVRLAAKKQELE 921
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 922 EILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKE- 1000
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARl 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1001 ---RKLLEERVSDLTTNL---------AEEEEKAKN----------LTKL-KSKHESMISE-------------LEVRLK 1044
Cdd:COG4913 443 lalRDALAEALGLDEAELpfvgelievRPEEERWRGaiervlggfaLTLLvPPEHYAAALRwvnrlhlrgrlvyERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1045 KEEKSRQELEK--LKRKLEGDASDFHeqiadlqaqiAELKMQLAKK--------EEELQ--------AALARLDEEIAQK 1106
Cdd:COG4913 523 LPDPERPRLDPdsLAGKLDFKPHPFR----------AWLEAELGRRfdyvcvdsPEELRrhpraitrAGQVKGNGTRHEK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1107 N-------------NALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELE---DTLDSTATQQELRA 1170
Cdd:COG4913 593 DdrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1171 KREQevtvlKKALDEEtrsheaqvqemrqkhTQAVEELTEQLEQfkrakanLDKSKQTLEKENADLAGELRVLGQAKQEV 1250
Cdd:COG4913 673 LEAE-----LERLDAS---------------SDDLAALEEQLEE-------LEAELEELEEELDELKGEIGRLEKELEQA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1251 EHKKKKLEVQLQDLQSKCSDGERARAE-----------LSDKVHKLQNEVESVTGMLNEAEGKAIKLAK----------- 1308
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLELRALLEerfaaalgdavERELRENLEERIDALRARLNRAEEELERAMRafnrewpaeta 805
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 1309 ----DVASLGS------QLQDT---------QELLQEETRQklNVSTKLRQLEDERNSLQDQLDE 1354
Cdd:COG4913 806 dldaDLESLPEylalldRLEEDglpeyeerfKELLNENSIE--FVADLLSKLRRAIREIKERIDP 868
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
941-1602 |
6.17e-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: 64.36 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 941 LQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKvtaEAKIKKLEDDIlvmdDQNSKLSKERKLLEERVSDLTTNLAEEEE 1020
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFEN---EKVSLKLEEEI----QENKDLIKENNATRHLCNLLKETCARSAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1021 KAKNLTKLKSKHESMISELEVRLkkeEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLD 1100
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNI---EKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1101 EEIAQKNNALKKIRELeghisdLQEDLDSERAARNKAEKQKRDLGEELEA---LKTELEDTLDSTATQQELRAKREQEVT 1177
Cdd:pfam05483 247 IQITEKENKMKDLTFL------LEESRDKANQLEEKTKLQDENLKELIEKkdhLTKELEDIKMSLQRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1178 VLKKALDEETRSHEAQVQEMRQKHTQAVEELTEqleqfkrakanLDKSKQTLEKenadlagelrVLGQAKQEVEHKKKKL 1257
Cdd:pfam05483 321 IATKTICQLTEEKEAQMEELNKAKAAHSFVVTE-----------FEATTCSLEE----------LLRTEQQRLEKNEDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1258 EVQLQDLQSKCSdgeraraelsdkvhklqnEVESVTGMLNEAEgkaiklaKDVASLGSQLQDTQELLQEEtrqklnvstk 1337
Cdd:pfam05483 380 KIITMELQKKSS------------------ELEEMTKFKNNKE-------VELEELKKILAEDEKLLDEK---------- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1338 lRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEvmeegkkRLQKEMEGLSQQYEEKAAAYDK 1417
Cdd:pfam05483 425 -KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVE-------DLKTELEKEKLKNIELTAHCDK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1418 LEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQ----KKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALE 1493
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1494 EALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQatedaklRLEVNMQALK 1573
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN-------KLELELASAK 649
|
650 660
....*....|....*....|....*....
gi 241982718 1574 GQFERDLQARDEQNEEKRRQLQRQLHEYE 1602
Cdd:pfam05483 650 QKFEEIIDNYQKEIEDKKISEEKLLEEVE 678
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1631-1902 |
6.80e-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: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1631 LQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQadlek 1710
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1711 eelaeelasslsgrntLQDEKRRLEARIAQLEeeleeeqgnmEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQL 1790
Cdd:COG4942 88 ----------------LEKEIAELRAELEAQK----------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1791 ERQNKELRSKLQEVEgAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKE 1870
Cdd:COG4942 142 KYLAPARREQAEELR-ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250 260 270
....*....|....*....|....*....|..
gi 241982718 1871 QAEKGNTKVKQLKRQLEEAEEESQRINANRRK 1902
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1000-1889 |
8.63e-10 |
|
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: 64.20 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1000 ERKLLEERVSDLTTNLAEEEEKaknLTKLKSKHESMISELEvrlkkeeksrqELEKLKRKLEGD---ASDF--------- 1067
Cdd:COG3096 279 ERRELSERALELRRELFGARRQ---LAEEQYRLVEMARELE-----------ELSARESDLEQDyqaASDHlnlvqtalr 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1068 -HEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDseraarnkaEKQKRDLge 1146
Cdd:COG3096 345 qQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALD---------VQQTRAI-- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1147 elealkteledtldstATQQELRAKRE-QEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKS 1225
Cdd:COG3096 414 ----------------QYQQAVQALEKaRALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1226 KQTLEKenadLAGEL---RVLGQAKQEVEH--KKKKLEVQLQDLQSKCSDGERARAElsdkvhklQNEVESVTGMLNEAE 1300
Cdd:COG3096 478 YELVCK----IAGEVersQAWQTARELLRRyrSQQALAQRLQQLRAQLAELEQRLRQ--------QQNAERLLEEFCQRI 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1301 GKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEE----MEAKQNLERhvstLNIQLSds 1376
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawLAAQDALER----LREQSG-- 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1377 kkklQDFASTIEVMEEGKKRLQKEMEgLSQQYEEKAAAYDKLEKTKNRLQQ-------EL----------------DDLV 1433
Cdd:COG3096 620 ----EALADSQEVTAAMQQLLERERE-ATVERDELAARKQALESQIERLSQpggaedpRLlalaerlggvllseiyDDVT 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1434 VD--------LDNQRQ--LVSNLEKKQKKFDQLlaeEKNISSKYADERDRAEAEAREKETKALSLAraleealeakeele 1503
Cdd:COG3096 695 LEdapyfsalYGPARHaiVVPDLSAVKEQLAGL---EDCPEDLYLIEGDPDSFDDSVFDAEELEDA-------------- 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1504 rtnkmlkaemeDLVSSKDdvgknvHELEKSK---------RALETQMEEMKTQLEELEDELqatedAKLRLEVN-MQALK 1573
Cdd:COG3096 758 -----------VVVKLSD------RQWRYSRfpevplfgrAAREKRLEELRAERDELAEQY-----AKASFDVQkLQRLH 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1574 GQFERDL-----QARDEQNEEKRRQLQRQLHEYETELEDERKQralaaaakkklegdlkdlELQADSAIKGREEAIKQLR 1648
Cdd:COG3096 816 QAFSQFVgghlaVAFAPDPEAELAALRQRRSELERELAQHRAQ------------------EQQLRQQLDQLKEQLQLLN 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1649 KLQAQM------------KDFQRELDDARASRDEIfatsKENEKKAKSLEADLMQLQEDLAAAERARKQADlekeelaee 1716
Cdd:COG3096 878 KLLPQAnlladetladrlEELREELDAAQEAQAFI----QQHGKALAQLEPLVAVLQSDPEQFEQLQADYL--------- 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1717 lasslsgrnTLQDEKRRLEARIaqleeeleeeqgnmEAMSDRVRKATLQAEQLSNELATERSTAqkNESARQQL---ERQ 1793
Cdd:COG3096 945 ---------QAKEQQRRLKQQI--------------FALSEVVQRRPHFSYEDAVGLLGENSDL--NEKLRARLeqaEEA 999
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1794 NKELRSKLQEVEG------AVKAKLKS-------TVAALEAKIAQLEEQVEQEAREKQAATKS-----LKQKDKKLKEVL 1855
Cdd:COG3096 1000 RREAREQLRQAQAqysqynQVLASLKSsrdakqqTLQELEQELEELGVQADAEAEERARIRRDelheeLSQNRSRRSQLE 1079
|
970 980 990
....*....|....*....|....*....|....*..
gi 241982718 1856 LQV---EDERKMAEQYKEQAEKgntKVKQLKRQLEEA 1889
Cdd:COG3096 1080 KQLtrcEAEMDSLQKRLRKAER---DYKQEREQVVQA 1113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
866-1308 |
9.41e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAEtELKELEQKHTqlAEEKTLLQEQLQAETELYAE----AEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQL 941
Cdd:PTZ00121 1531 EEAKKAD-EAKKAEEKKK--ADELKKAEELKKAEEKKKAEeakkAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEK 1021
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 AKNLTKLKSKHESMISELEVRlKKEEKSRQELEKLKRKLEgdasdfheqiadlqaqIAELKMQLAKKEEELQAALArldE 1101
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKAEE----------------ENKIKAEEAKKEAEEDKKKA---E 1747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1102 EIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTeLEDTLDSTATQQELRAKREQEVTVLKK 1181
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK-IKDIFDNFANIIEGGKEGNLVINDSKE 1826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1182 ALDEETRSHEAQVQEMRqkhtqaveeltEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQL 1261
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQL-----------EEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK 1895
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 241982718 1262 QDLQSKCSDGERARAELSDKVHKLQNEvESVTGMLNEAEGKAIKLAK 1308
Cdd:PTZ00121 1896 DDIEREIPNNNMAGKNNDIIDDKLDKD-EYIKRDAEETREEIIKISK 1941
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1203-1941 |
1.21e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1203 QAVEELTEQLEQFKRAKANLDKskqtlEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKcsDGERARAELSDKV 1282
Cdd:COG4913 225 EAADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1283 HKLQNEVEsvtgmlneaegkaiKLAKDVASLGSQLQDTQELLQEETRQKLNVST-KLRQLEDERNSLQDQLDEEMEAKQN 1361
Cdd:COG4913 298 EELRAELA--------------RLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1362 LERHVSTLNIQLSDSKKKLqdfastievmEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQ 1441
Cdd:COG4913 364 LEALLAALGLPLPASAEEF----------AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1442 LVSNLEKKQKKFDQLLAEEKNISS------------KYADERDRAEAEA------------REKETKALSLARaleeaLE 1497
Cdd:COG4913 434 RKSNIPARLLALRDALAEALGLDEaelpfvgelievRPEEERWRGAIERvlggfaltllvpPEHYAAALRWVN-----RL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1498 AKEELERTNKmLKAEMEDLVSSKDDVGKNVHELE-KSKRALETQMEEMKTQLE----ELEDELQATEDAkLRLEVNMQAL 1572
Cdd:COG4913 509 HLRGRLVYER-VRTGLPDPERPRLDPDSLAGKLDfKPHPFRAWLEAELGRRFDyvcvDSPEELRRHPRA-ITRAGQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1573 KGQFERDLQARDEQ-------NEEKRRQLQRQLHEYETELEDERKQralaaaakkklegdLKDLELQADsAIKGREEAIK 1645
Cdd:COG4913 587 GTRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEER--------------LEALEAELD-ALQERREALQ 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1646 QLRKLQAQMKDF---QRELDDARASRDEIFATSkenekkaksleADLMQLQEDLAAAERARKQADLEkeelaeelassls 1722
Cdd:COG4913 652 RLAEYSWDEIDVasaEREIAELEAELERLDASS-----------DDLAALEEQLEELEAELEELEEE------------- 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1723 gRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKA-TLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKL 1801
Cdd:COG4913 708 -LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1802 QEVEGAVKAKLKS----------TVAALEAKIAQLEEQVEQEAREKQAATKSLKQK--DKKLKEVLLQVEDERKMAEQyk 1869
Cdd:COG4913 787 EELERAMRAFNREwpaetadldaDLESLPEYLALLDRLEEDGLPEYEERFKELLNEnsIEFVADLLSKLRRAIREIKE-- 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1870 eqaekgntKVKQLKRQLEEAE---------EESQRINANRRKLQRELDEATESNEAMGRE--------VNALKSKLRRGN 1932
Cdd:COG4913 865 --------RIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEElsearfaaLKRLIERLRSEE 936
|
....*....
gi 241982718 1933 EASFVPSRR 1941
Cdd:COG4913 937 EESDRRWRA 945
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1192-1414 |
1.42e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1192 AQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCsdg 1271
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1272 ERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQ 1351
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1352 LDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAA 1414
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
862-1230 |
2.30e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEE----------ILHEMEARL 931
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdelrereaELEATLRTA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 932 EEEEDRGQQLQAERK--KMAQQMLDL--EEQLEEEEAARQKLQLEKVTAEAKIKKLEDDIlvmdDQNSKLSKerklLEER 1007
Cdd:PRK02224 439 RERVEEAEALLEAGKcpECGQPVEGSphVETIEEDRERVEELEAELEDLEEEVEEVEERL----ERAEDLVE----AEDR 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1008 VSDLttnlaeeEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAK 1087
Cdd:PRK02224 511 IERL-------EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1088 KEEELQaalarldeeiaqknnALKKIRELEGHISDLQEDLDS---ERAARNKAEKQKRDLGEELEALKTELEDTLDSTAT 1164
Cdd:PRK02224 584 LKERIE---------------SLERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERKRELEAEFDEARI 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 1165 qQELRAKREQEVTVLKKAlDEETRSHEAQVQEMrQKHTQAVEELTEQLEQFKRAKANLDKSKQTLE 1230
Cdd:PRK02224 649 -EEAREDKERAEEYLEQV-EEKLDELREERDDL-QAEIGAVENELEELEELRERREALENRVEALE 711
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1172-1874 |
2.75e-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: 62.35 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1172 REQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKAN-------LDKSKQTLEKENADLageLRVLG 1244
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQikdlndkLKKNKDKINKLNSDL---SKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1245 QAKQEVEHKKKKlEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELL 1324
Cdd:TIGR04523 111 EIKNDKEQKNKL-EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1325 QEETRQKLNVSTKLRQLE---DERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEM 1401
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1402 EGLSQQYEEKAAAYDKLEKTKNRLQQELDDL--VVDLDNQRQLVSNLEKKQKKFDQL---LAEEKNISSKYADERDRAEA 1476
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQISQLKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1477 EAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ 1556
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1557 ATEDAKLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKqralaaaakkklegDLKDLELQADSA 1636
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQ-DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ--------------NLEQKQKELKSK 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1637 IKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDL--AAAERARKQADLEKEELA 1714
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELK 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1715 EELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQN 1794
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1795 KELRSKLQEVEGAVKAkLKSTVaaleAKIAQLEEQVEQE--AREKQAATKSLKQKD-KKLKEVLLQVEDERKMAEQYKEQ 1871
Cdd:TIGR04523 655 KEIRNKWPEIIKKIKE-SKTKI----DDIIELMKDWLKElsLHYKKYITRMIRIKDlPKLEEKYKEIEKELKKLDEFSKE 729
|
...
gi 241982718 1872 AEK 1874
Cdd:TIGR04523 730 LEN 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1267 |
2.94e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEI--LHEMEARLEEEEDRGQ 939
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeeRHELYEEAKAKKEELE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 940 QLQAERK-----KMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQN-------------------- 994
Cdd:PRK03918 376 RLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkelle 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 995 ------SKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHE--SMISELEVRLK-----KEEKSRQELEKLKRKLE 1061
Cdd:PRK03918 456 eytaelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKkynleELEKKAEEYEKLKEKLI 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1062 GDASDFH------EQIADLQAQIAELKMQLAKKEEELQAALARLDEEiaqknnALKKIRELEGHISDLQEDLDSERAARN 1135
Cdd:PRK03918 536 KLKGEIKslkkelEKLEELKKKLAELEKKLDELEEELAELLKELEEL------GFESVEELEERLKELEPFYNEYLELKD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1136 kAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRsheaqvQEMRQKHTQAVEELTEQLEQF 1215
Cdd:PRK03918 610 -AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY------EELREEYLELSRELAGLRAEL 682
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1216 KRAKANLDKSKQTLEKenadLAGELRVLGQAKQEVEHKKKKLEvQLQDLQSK 1267
Cdd:PRK03918 683 EELEKRREEIKKTLEK----LKEELEEREKAKKELEKLEKALE-RVEELREK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1528-1915 |
3.12e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1528 HELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNmqalkgQFERDLQARDEQNEEKRRQLQRQLHEYETELED 1607
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY------QELEALEAELAELPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1608 ERKQRALAAAAKKKLEGDLKDLELQADSAIkgrEEAIKQLRKLQAQMKDFQRELDDARAsrdeifatskenekKAKSLEA 1687
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQE--------------ELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1688 DLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQ------------LEEELEEEQGNMEAM 1755
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFlvlgllallfllLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1756 SDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEgavKAKLKSTVAALEAKIAQLEEQV----E 1831
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE---ELEEELQLEELEQEIAALLAEAgvedE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1832 QEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVK--QLKRQLEEAEEESQRINANRRKLQRELDE 1909
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEleELEEELEELEEELEELREELAELEAELEQ 464
|
....*.
gi 241982718 1910 ATESNE 1915
Cdd:COG4717 465 LEEDGE 470
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
806-1464 |
3.14e-09 |
|
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: 62.29 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 806 FTKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEeemqkikerqQKAETELKELE--QKHT 883
Cdd:TIGR00618 217 YHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARI----------EELRAQEAVLEetQERI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 884 QLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEE 963
Cdd:TIGR00618 287 NRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 964 AARQKLQleKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRL 1043
Cdd:TIGR00618 367 IREISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1044 KKEEKSRQELEKLKRKLEGDASDFHEQIADLQ------AQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELE 1117
Cdd:TIGR00618 445 AAITCTAQCEKLEKIHLQESAQSLKEREQQLQtkeqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1118 GHISDLQEDLDSERAARNKAEKQKRDLGEELE---ALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQV 1194
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKqraSLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1195 QEMRQKhtqaVEELTEQLEQFKRAKANLDKS------KQTLEKENADLAGELRVLGQAKQEvEHKKKKLEVQLQDLQSKc 1268
Cdd:TIGR00618 605 EAEDML----ACEQHALLRKLQPEQDLQDVRlhlqqcSQELALKLTALHALQLTLTQERVR-EHALSIRVLPKELLASR- 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1269 sdgeraraelSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSL 1348
Cdd:TIGR00618 679 ----------QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKEL 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1349 QDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAY-DKLEKTKNRLQQ 1427
Cdd:TIGR00618 749 MHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDeDILNLQCETLVQ 828
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 241982718 1428 ELDDLVVDLDNQ-------RQLVSNLEKKQKKFDQLLAEEKNIS 1464
Cdd:TIGR00618 829 EEEQFLSRLEEKsatlgeiTHQLLKYEECSKQLAQLTQEQAKII 872
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1527-1961 |
3.64e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1527 VHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETEL- 1605
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLa 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1606 ----------EDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQR-------ELDDARasr 1668
Cdd:COG4913 370 alglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnipaRLLALR--- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1669 DEIFATSKENEKKAKSLeADLMQLQEDLA----AAERA----------------------------------RKQADLEK 1710
Cdd:COG4913 447 DALAEALGLDEAELPFV-GELIEVRPEEErwrgAIERVlggfaltllvppehyaaalrwvnrlhlrgrlvyeRVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1711 EELAEELASSLSGRNTLQDEKRR--LEARIAQLEEELEEEqgNMEAMsDRVRKATLQAEQLSN-----ELATERSTAQKN 1783
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHPFRawLEAELGRRFDYVCVD--SPEEL-RRHPRAITRAGQVKGngtrhEKDDRRRIRSRY 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1784 ---ESARQQLERQNKELrsklqevegavkAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKevLLQVED 1860
Cdd:COG4913 603 vlgFDNRAKLAALEAEL------------AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAER 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1861 ERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNEASFVPSR 1940
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
490 500
....*....|....*....|..
gi 241982718 1941 -RAGGRRVIENTDGSEEEMDAR 1961
Cdd:COG4913 749 aLLEERFAAALGDAVERELREN 770
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1046-1489 |
3.70e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1046 EEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKmqlaKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDL-- 1123
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELREELEKLek 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1124 QEDLDSERAARNKAEKQKRDLGEELEALKTELEDTldstATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQ 1203
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1204 AVEELTEQLEQFKRAKANLDKSKQTLEKENADLagelrvlgQAKQEVEHKKKKLEVQLQDLQskcsdGERARAELSDKVH 1283
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQL--------ENELEAAALEERLKEARLLLL-----IAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1284 KLQNEVESVTGMLNEAEGKAI----KLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQL---EDERNSLQDQLDEEM 1356
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLAllflLLAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1357 EAKQNLERHVSTLN--IQLSDSKKKLQ------------DFASTIEVMEEgKKRLQKEMEGLSQQYEEKAAAYDKLEK-- 1420
Cdd:COG4717 347 EELQELLREAEELEeeLQLEELEQEIAallaeagvedeeELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEal 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1421 TKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLL--AEEKNISSKYADERDRAEAEAREKETKALSLA 1489
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1534-1950 |
4.57e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1534 KRALETQMEEMKTQLEELEDELQATEDAKLRLEVNmqALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRA 1613
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLN--GLESE-LAELDEEIERYEEQREQARETRDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1614 LAAAAkkklEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQ 1693
Cdd:PRK02224 252 ELETL----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1694 EDL----AAAERARKQADLEKEELAEelassLSGRNT-LQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQ 1768
Cdd:PRK02224 328 DRLeecrVAAQAHNEEAESLREDADD-----LEERAEeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1769 LSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVK--------------------AKLKSTVAALEAKIAQLEE 1828
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaealleagkcpecgqpvegSPHVETIEEDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1829 QVEqEAREKQAATKSLKQKDKKLKEVLLQVEDER-------KMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRR 1901
Cdd:PRK02224 483 ELE-DLEEEVEEVEERLERAEDLVEAEDRIERLEerredleELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA 561
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 241982718 1902 KLQRELDEATESNEAMGREVNALKSKLRRGNEASFVPSRRAGGRRVIEN 1950
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIER 610
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
936-1165 |
5.18e-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: 60.55 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 936 DRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNL 1015
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1016 AEEEEKAKNLTKLKSKHeSMISELEVRLKKEekSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAA 1095
Cdd:COG4942 100 EAQKEELAELLRALYRL-GRQPPLALLLSPE--DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1096 LARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQ 1165
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
967-1428 |
2.11e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 967 QKLQLEKVTAEAKIKKLEDDIlvmdDQNSKLSKERKLLEERVSDLTTNLA--EEEEKAKNLTKLKSKHESMISELEVRLK 1044
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1045 KEEKSRQELEKLKRKLEgdasDFHEQIADLQAQIAELKMQL-AKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDL 1123
Cdd:COG4717 150 ELEERLEELRELEEELE----ELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1124 QEDLDSERAARNKAEKQKRDLGEE--------LEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQ 1195
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1196 EMRQKHTQ---AVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHK--KKKLEVQLQDLQSKCSD 1270
Cdd:COG4717 306 ELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1271 GERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAkdvaslgsqlqdtqellqeETRQKLNVSTKLRQLEDERNSLQD 1350
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-------------------EALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1351 QLDEEMEAKQNLERHVStlniQLSDSKkklqdfasTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQE 1428
Cdd:COG4717 447 ELEELREELAELEAELE----QLEEDG--------ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
942-1598 |
2.37e-08 |
|
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: 59.45 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 QAERKKMAQQMLDLEEQLEEEEAARQKLQLekvtaeaKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEk 1021
Cdd:pfam10174 45 RALRKEEAARISVLKEQYRVTQEENQHLQL-------TIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEE- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 akNLTKLKSKHESMISELEVRLKKEEK-------SRQEL----EKLKRKLE---------GDASDFHE---QIADLQAQI 1078
Cdd:pfam10174 117 --NFRRLQSEHERQAKELFLLRKTLEEmelrietQKQTLgardESIKKLLEmlqskglpkKSGEEDWErtrRIAEAEMQL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1079 AELKMQLAKKEEELQAalarLDEEIAQKNNALKKIREleghISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdt 1158
Cdd:pfam10174 195 GHLEVLLDQKEKENIH----LREELHRRNQLQPDPAK----TKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGL-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1159 LDSTATQQELRakreqEVTVLKKALDEETRSHEAQVQEMRQKHTQAV------EELTEQLEQFKRAKANLDKSKQTLEKE 1232
Cdd:pfam10174 265 LHTEDREEEIK-----QMEVYKSHSKFMKNKIDQLKQELSKKESELLalqtklETLTNQNSDCKQHIEVLKESLTAKEQR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1233 NADLAGE---LRVLGQAKQEVEHKKKKlevQLQDLQSKCSDGERARAELSD-------KVHKLQNEVESVTGMLNEAEGK 1302
Cdd:pfam10174 340 AAILQTEvdaLRLRLEEKESFLNKKTK---QLQDLTEEKSTLAGEIRDLKDmldvkerKINVLQKKIENLQEQLRDKDKQ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1303 AIKLAKDVASLGSQLQDTQELL---QEETRQKLNVSTKLR-QLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSD--- 1375
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNTDTALttlEEALSEKERIIERLKeQREREDRERLEELESLKKENKDLKEKVSALQPELTEkes 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1376 SKKKLQDFASTIEVMEEGKKRLQKEMEG-LSQQYEEKAAAYDKLEKTKN-----RLQQELDDLVVDLDNQRQL-VSNLEK 1448
Cdd:pfam10174 497 SLIDLKEHASSLASSGLKKDSKLKSLEIaVEQKKEECSKLENQLKKAHNaeeavRTNPEINDRIRLLEQEVARyKEESGK 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1449 KQKKFDQLLAEEKNisskyaderdrAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVH 1528
Cdd:pfam10174 577 AQAEVERLLGILRE-----------VENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRE 645
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1529 ELEKSKrALETQMEEMKTQLEELEDELQATedaKLRLEVNMQALKgqfERDLQARDEQnEEKRRQLQRQL 1598
Cdd:pfam10174 646 DNLADN-SQQLQLEELMGALEKTRQELDAT---KARLSSTQQSLA---EKDGHLTNLR-AERRKQLEEIL 707
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1037-1344 |
2.93e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 57.62 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1037 SELEVRLK-KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKnnalkkiRE 1115
Cdd:pfam00038 28 KLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR-------TS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1116 LEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKT-------ELEDTLDSTATQQELRAKREQEVTVLkkaldeetr 1188
Cdd:pfam00038 101 AENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnheeevrELQAQVSDTQVNVEMDAARKLDLTSA--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1189 sheaqVQEMRQKHTQAVEELTEQLEQFKRAKanLDKSKQTLEKENADlagelrvLGQAKQEV---EHKKKKLEVQLQDLQ 1265
Cdd:pfam00038 172 -----LAEIRAQYEEIAAKNREEAEEWYQSK--LEELQQAAARNGDA-------LRSAKEEItelRRTIQSLEIELQSLK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1266 SKCSDGERARAELSDkvhKLQNEVESVTGMLNEAEGkaiKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDE 1344
Cdd:pfam00038 238 KQKASLERQLAETEE---RYELQLADYQELISELEA---ELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGE 310
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1591 |
3.28e-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: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 845 LQVTRQEEEMQAKEEEMQKIKERQQKAETELKELEqkhtqlaEEKTLLQEQLQAETELyaeaeemrvrLAAKKQELEEIL 924
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR-------DEKKGLGRTIELKKEI----------LEKKQEELKFVI 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 925 HEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQK-LQLEKVTAEAKIKKLEDDILVMD------DQNSKL 997
Cdd:TIGR00606 461 KELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKsLQNEKADLDRKLRKLDQEMEQLNhhtttrTQMEML 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 998 SKERKLLEERV-------SDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQ 1070
Cdd:TIGR00606 541 TKDKMDKDEQIrkiksrhSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1071 IADLQAQIAElkmqlAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAA-------RNKAEKQKRD 1143
Cdd:TIGR00606 621 LSSYEDKLFD-----VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrVFQTEAELQE 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1144 LGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELteqleqfKRAKANLD 1223
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI-------QRLKNDIE 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1224 KSKQTLEKENA------DLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSkcSDGERARAELSDKVHKLQNEVESVTgmln 1297
Cdd:TIGR00606 769 EQETLLGTIMPeeesakVCLTDVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQHELDTVV---- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1298 eaegkaiklakdvaslgSQLQDTQELLQEETRQKLNVSTKLRQLEDERNslqdQLDEEMEAKQNLERHVSTLNIQLSDSK 1377
Cdd:TIGR00606 843 -----------------SKIELNRKLIQDQQEQIQHLKSKTNELKSEKL----QIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1378 KKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEkaaaydklekTKNRLQQELDDLVVDLDNQRQLVSNLEKK--QKKFDQ 1455
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQEKEELISSKET----------SNKKAQDKVNDIKEKVKNIHGYMKDIENKiqDGKDDY 971
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1456 LLAEEKNISSKYADERDraEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEkskr 1535
Cdd:TIGR00606 972 LKQKETELNTVNAQLEE--CEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMG---- 1045
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1536 alETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQ---FERDLQARDEQNEEKR 1591
Cdd:TIGR00606 1046 --QMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEikhFKKELREPQFRDAEEK 1102
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1629-1873 |
4.08e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1629 LELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDeIFATSKEnekkAKSLEADLMQLQEDLAAAERARKQAdl 1708
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEE----AKLLLQQLSELESQLAEARAELAEA-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1709 ekeelaeelasslsgrntlQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEqlsneLATERSTAQKNESARQ 1788
Cdd:COG3206 239 -------------------EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE-----LAELSARYTPNHPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1789 QLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEarekQAATKSLKQKDKKLKEVLLQVEDERKMAEQY 1868
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL----EARLAELPELEAELRRLEREVEVARELYESL 370
|
....*
gi 241982718 1869 KEQAE 1873
Cdd:COG3206 371 LQRLE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1070-1277 |
4.59e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1070 QIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDserAARNKAEKQKRDLGEELE 1149
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1150 ALKTE------LEDTLDSTATQQELrakreQEVTVLKKALDEETRSHEaQVQEMRQKHTQAVEELTEQLEQFKRAKANLD 1223
Cdd:COG3883 94 ALYRSggsvsyLDVLLGSESFSDFL-----DRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1224 KSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAE 1277
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1070-1240 |
5.41e-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: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1070 QIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKrdlgeELE 1149
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1150 ALKTELEdtldstaTQQELRAKREQEVTVLKKALDEetrsHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTL 1229
Cdd:COG1579 93 ALQKEIE-------SLKRRISDLEDEILELMERIEE----LEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|.
gi 241982718 1230 EKENADLAGEL 1240
Cdd:COG1579 162 EAEREELAAKI 172
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1206-1808 |
6.96e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1206 EELTEQLEQFKRAKANLDKSKQTLEkenaDLAGELRVLGQAKQEVEHKKKKLE---VQLQDLQSKCSDGERARAELSDKV 1282
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVID----MLRAEISNIDYLEEKLKSSNLELEnikKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1283 HKLQNEVEsvtgMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEEtrqkLNVSTKLRQLEDERNSLQDqldEEMEAKQNL 1362
Cdd:PRK01156 228 NNAMDDYN----NLKSALNELSSLEDMKNRYESEIKTAESDLSME----LEKNNYYKELEERHMKIIN---DPVYKNRNY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1363 ERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQkEMEGLSQQYEEKAAAYDKLEKtknrlqqELDDLVVDLDNQRQL 1442
Cdd:PRK01156 297 INDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNN-------QILELEGYEMDYNSY 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1443 VSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREketkalslaraleealeakeelertnkmLKAEMEDLVSSKDD 1522
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA----------------------------IKKELNEINVKLQD 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1523 VGKNVHELEKSKRALETQMEEMKTQLEEL------------------EDELQATEDAKLRLEVNMQALkgqfERDLQARD 1584
Cdd:PRK01156 421 ISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeeksNHIINHYNEKKSRLEEKIREI----EIEVKDID 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1585 EQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAikgrEEAIKQLRKLQAQMKDFQR-ELDD 1663
Cdd:PRK01156 497 EKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKY----EEIKNRYKSLKLEDLDSKRtSWLN 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1664 ARASRD--EIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEaRIAQL 1741
Cdd:PRK01156 573 ALAVISliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIE-KLRGK 651
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1742 EEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAV 1808
Cdd:PRK01156 652 IDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1529-1764 |
6.98e-08 |
|
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: 57.08 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1529 ELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDE 1608
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1609 RKQ-RALAAAAKKKLEGDLKDLELQADSAikgrEEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEA 1687
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1688 DLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATL 1764
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1450-1912 |
8.15e-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: 57.75 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1450 QKKFDQLLAEEKNISskyADERDRAEAEAREKETKALSLARALEEALEAKEELERTNkmLKAEMEDLVSSKDDVGKNVHE 1529
Cdd:TIGR00606 172 KQKFDEIFSATRYIK---ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQ--ITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1530 LEKSKRALEtQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYE------- 1602
Cdd:TIGR00606 247 LDPLKNRLK-EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKErelvdcq 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1603 TELEDERKQRALAAAAKKKLEGDLKDLELQAD---SAIKGREEAIKQLrKLQAQMKDFQRELDDARASRDEIFATSKENE 1679
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADrhqEHIRARDSLIQSL-ATRLELDGFERGPFSERQIKNFHTLVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1680 KKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEelasslsgrnTLQDEKRRLEARIAQLEEELEEEQgNMEAMSDRV 1759
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR----------TIELKKEILEKKQEELKFVIKELQ-QLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1760 rkatLQAEQLSNELATERSTAQKNESARQQLERQnKELRSKlqevegavKAKLKSTVAALEAKIAQLE------EQVEQE 1833
Cdd:TIGR00606 474 ----LELDQELRKAERELSKAEKNSLTETLKKEV-KSLQNE--------KADLDRKLRKLDQEMEQLNhhtttrTQMEML 540
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1834 AREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATE 1912
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1210-1853 |
1.24e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1210 EQLEQFKRAKANLDKSKQTLEKENADLAGELRvlgQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEV 1289
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELK---QKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1290 ESvtgmlNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQ-----------KLNVSTKLR-QLEDERNSLQDQLDEEME 1357
Cdd:pfam05483 148 KE-----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnniekMILAFEELRvQAENARLEMHFKLKEDHE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1358 AKQNLE-----------RHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEkaaaydkLEKTKNRLQ 1426
Cdd:pfam05483 223 KIQHLEeeykkeindkeKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKE-------LIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1427 QELDDLVVDL----DNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEEL 1502
Cdd:pfam05483 296 KELEDIKMSLqrsmSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1503 ERTNKMLKAEMEDLVSSKDDVGKNVH----ELEKSKRAL---ETQMEEMKtQLEELEDELQATEDAKLRLevnMQALKGQ 1575
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKNnkevELEELKKILaedEKLLDEKK-QFEKIAEELKGKEQELIFL---LQAREKE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1576 FErDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAI--------------KGRE 1641
Cdd:pfam05483 452 IH-DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTlelkkhqediinckKQEE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1642 EAIKQLRKLQAQMKDFQRELDDARAS----RDEIFATSKENEKKAKSLEADLMQLQEDLAAAERA----RKQADLEKEEL 1713
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnnlKKQIENKNKNI 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1714 AEELASSLSGRNTLQDEKRRL---EARIAQLEEELEEEQGNMEAMSDRVRK----ATLQAEQLSNELATERSTA------ 1780
Cdd:pfam05483 611 EELHQENKALKKKGSAENKQLnayEIKVNKLELELASAKQKFEEIIDNYQKeiedKKISEEKLLEEVEKAKAIAdeavkl 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1781 QKNESARQQ--------------------LERQNKEL---RSKLQEvEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREK 1837
Cdd:pfam05483 691 QKEIDKRCQhkiaemvalmekhkhqydkiIEERDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEK 769
|
730
....*....|....*.
gi 241982718 1838 QAATKSLKQKDKKLKE 1853
Cdd:pfam05483 770 EKLKMEAKENTAILKD 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1069-1912 |
1.33e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1069 EQIADLQAQIAELKMQLAKKEEelqaALARLDEEIAQKNNALKkirELEGHISDLQEDLDSERAARNKAEKQKRdLGEEL 1148
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQY----RLVEMARELAELNEAES---DLEQDYQAASDHLNLVQTALRQQEKIER-YQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1149 EALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEeTRSHEAQVQemrqkhtQAVEELTEQLEQFKRAKANLDKSKQT 1228
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDE-LKSQLADYQ-------QALDVQQTRAIQYQQAVQALERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1229 LEKENADLAGelrvLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERAR---AELSDKVHKLQNEVESvtgmlNEAEGKAIK 1305
Cdd:PRK04863 430 CGLPDLTADN----AEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfEQAYQLVRKIAGEVSR-----SEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1306 LAKDVASLGSQLQDTQELLQE--ETRQKLNvstKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDF 1383
Cdd:PRK04863 501 LLRRLREQRHLAEQLQQLRMRlsELEQRLR---QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1384 ASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDlVVDLDNQRQlvsnlekkqkkfdQLLAEEKNI 1463
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFED-SQDVTEYMQ-------------QLLEREREL 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1464 SSkyadERDRAEAEAREKETKALSLA-RALEEALEAKEELERTNKMLKAEM----------------------------- 1513
Cdd:PRK04863 644 TV----ERDELAARKQALDEEIERLSqPGGSEDPRLNALAERFGGVLLSEIyddvsledapyfsalygparhaivvpdls 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1514 -------------EDL------VSSKDDVGKNVHELEKS----------------------KRALETQMEEMKTQLEELE 1552
Cdd:PRK04863 720 daaeqlagledcpEDLyliegdPDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELA 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1553 DELqatedAKLRLEVN-MQALKGQFERDLQ-----ARDEQNEEKRRQLQRQLHEYETELEDERKQralaaaakkklegdl 1626
Cdd:PRK04863 800 ERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELRQLNRRRVELERALADHESQ--------------- 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1627 kdlELQADSAIKGREEAIKQLRKLQAQMK-----DFQRELDDARASRDEifatskenekkAKSLEADLMQLQEDLAAAER 1701
Cdd:PRK04863 860 ---EQQQRSQLEQAKEGLSALNRLLPRLNlladeTLADRVEEIREQLDE-----------AEEAKRFVQQHGNALAQLEP 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1702 --ARKQADlekeelaeelasslsgrntlQDEKRRLEARIAQLEEELEEEQGNMEAMSDRV-RKATLQAEQLSNELATErs 1778
Cdd:PRK04863 926 ivSVLQSD--------------------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVqRRAHFSYEDAAEMLAKN-- 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1779 tAQKNESARQQL---ERQNKELRSKLQEVEG------AVKAKLKSTVAALEAKIAQLEEQVEQ------EAREKQAATKS 1843
Cdd:PRK04863 984 -SDLNEKLRQRLeqaEQERTRAREQLRQAQAqlaqynQVLASLKSSYDAKRQMLQELKQELQDlgvpadSGAEERARARR 1062
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1844 lkqkdKKLKEVLLQvederkmAEQYKEQAEKgntkvkqlKRQLEEAEEESQriNANRRKLQRELDEATE 1912
Cdd:PRK04863 1063 -----DELHARLSA-------NRSRRNQLEK--------QLTFCEAEMDNL--TKKLRKLERDYHEMRE 1109
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1589-1840 |
1.42e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1589 EKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADsaikgreEAIKQLRKLQAQMKDFQRELddarasr 1668
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALEAEL------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1669 deifatsKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEE 1748
Cdd:COG4942 86 -------AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1749 QGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQnkeLRSKLQEVEGAVkAKLKSTVAALEAKIAQLEE 1828
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAEL-AELQQEAEELEALIARLEA 234
|
250
....*....|..
gi 241982718 1829 QVEQEAREKQAA 1840
Cdd:COG4942 235 EAAAAAERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
999-1763 |
1.53e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 999 KERKLLEERVSDLTTNLAEEEEKaknLTKLKSKHESMISELEvRLKKEEKS-RQELEKLKRKLE--GDASDFHEQIADLQ 1075
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQ---LAAEQYRLVEMARELA-ELNEAESDlEQDYQAASDHLNlvQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1076 AQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDsERAARNKAEKQKRDLGEELEALKTEL 1155
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALD-VQQTRAIQYQQAVQALERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1156 EDTLDS-TATQQELRAKrEQEVTVLKKALDEETRSHEAqvqeMRQKHTQAVEELTEQLEQFKRAKANlDKSKQTLEKena 1234
Cdd:PRK04863 434 DLTADNaEDWLEEFQAK-EQEATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEVSRSEAW-DVARELLRR--- 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1235 dlAGELRVLGQAKQEVEHKKKKLEVQLQDLQskcsDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLG 1314
Cdd:PRK04863 505 --LREQRHLAEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1315 ---SQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSdskkklqdfASTIEV-- 1389
Cdd:PRK04863 579 errMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERER---------ELTVERde 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1390 MEEGKKRLQKEMEGLSQQyeeKAAAYDKLEKTKNRLQQEL-----DD--------------------LVVDLDN-QRQLV 1443
Cdd:PRK04863 650 LAARKQALDEEIERLSQP---GGSEDPRLNALAERFGGVLlseiyDDvsledapyfsalygparhaiVVPDLSDaAEQLA 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1444 SN---------LEKKQKKFDQ--LLAEE--KNISSKYADERDRAEA---------EAREKETKAL-----SLARALEEAL 1496
Cdd:PRK04863 727 GLedcpedlylIEGDPDSFDDsvFSVEEleKAVVVKIADRQWRYSRfpevplfgrAAREKRIEQLraereELAERYATLS 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1497 EAKEELERTNKMLK----------------AEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQL------------ 1548
Cdd:PRK04863 807 FDVQKLQRLHQAFSrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnl 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1549 ----------EELEDELQATEDAKL----------RLEVNMQALK---GQFERdLQARDEQNEEKRRQLQRQLHEYeTEL 1605
Cdd:PRK04863 887 ladetladrvEEIREQLDEAEEAKRfvqqhgnalaQLEPIVSVLQsdpEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-TEV 964
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1606 ---------EDERKQRALAAAAKKKLEGDLKDLELQadsaikgREEAIKQLRKLQAQMKDFQRELDDARASRDeifatSK 1676
Cdd:PRK04863 965 vqrrahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQE-------RTRAREQLRQAQAQLAQYNQVLASLKSSYD-----AK 1032
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1677 ENEKKAKSLEADLMQLQEDLAAAERARkqadlekeelaeelasslSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMS 1756
Cdd:PRK04863 1033 RQMLQELKQELQDLGVPADSGAEERAR------------------ARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLT 1094
|
....*..
gi 241982718 1757 DRVRKAT 1763
Cdd:PRK04863 1095 KKLRKLE 1101
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
996-1115 |
1.78e-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: 54.16 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 996 KLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKS-------------RQELEKLKRK--- 1059
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyealQKEIESLKRRisd 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 1060 LEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRE 1115
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1504-1936 |
1.87e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1504 RTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvnmqALKGQFE------ 1577
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEelekel 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1578 RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQaDSAIKGREEAIKQLRKLQAQMKDF 1657
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY-EEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1658 QRELDDARASRDEIfatsKENEKKAKSLEADLMQLQEDLAAAERARKqadlekeelaeelasslsgrntLQDEKRRLEAR 1737
Cdd:PRK03918 327 EERIKELEEKEERL----EELKKKLKELEKRLEELEERHELYEEAKA----------------------KKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1738 IAQLEEeleeeqGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKL--------QEVEGAVK 1809
Cdd:PRK03918 381 LTGLTP------EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1810 AKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDK--KLKEVLLQVED-ERKMAEQYKEQAEKGNTKVKQLKRQL 1886
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKElEEKLKKYNLEELEKKAEEYEKLKEKL 534
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 241982718 1887 EEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNEASF 1936
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF 584
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1317-1896 |
2.54e-07 |
|
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: 55.90 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1317 LQDTQELLQEETRQKlnvsTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFAstievmeEGKKR 1396
Cdd:pfam05557 12 SQLQNEKKQMELEHK----RARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA-------ELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1397 LQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEA 1476
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1477 ---EAREKETKALSLARALEEALEAKEELERTNKMLK--AEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEEL 1551
Cdd:pfam05557 161 qqsSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAriPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1552 E---DELQATEDAKLRLEVNMQALKGQFER---------DLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAK 1619
Cdd:pfam05557 241 EkyrEEAATLELEKEKLEQELQSWVKLAQDtglnlrspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1620 KKLEGDLKDLElqadsaiKGREEAIKQLRKLQAQMKDFQRELDDARA---SRDEIFATSKENEKKAKSLE--ADLMQLQE 1694
Cdd:pfam05557 321 AQYLKKIEDLN-------KKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1695 DLAAAERARKQADLEKEELAEELASSLsgrntlqdeKRRLEARIAQLEEELEEEQGNmEAMSDRVRKATLQAEqlsnela 1774
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTL---------ERELQALRQQESLADPSYSKE-EVDSLRRKLETLELE------- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1775 terstaqknesaRQQLERQNKELRSKLQEVEGAVKAKLKSTvaaleaKIAQLEEQVEQEAREKQAAT-KSLKQKDKKLKE 1853
Cdd:pfam05557 457 ------------RQRLREQKNELEMELERRCLQGDYDPKKT------KVLHLSMNPAAEAYQQRKNQlEKLQAEIERLKR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 241982718 1854 VLLQVEDERKMAEQYKEQAEKGNTK-VKQLKRQLEEAEEESQRI 1896
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTMNFKeVLDLRKELESAELKNQRL 562
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1392-1611 |
2.60e-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: 55.16 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1392 EGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK-----------QKKFDQLLAEE 1460
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaaleaelaelEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1461 KNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQ 1540
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1541 MEEMKTQLEELEDELQATEDAKLRLEVNMQAlkgqferdLQARDEQNEEKRRQLQRQLHEYETELEDERKQ 1611
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
965-1288 |
2.62e-07 |
|
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: 55.07 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 965 ARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSK-------HESMIS 1037
Cdd:pfam19220 42 ELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEElrielrdKTAQAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1038 ELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELE 1117
Cdd:pfam19220 122 ALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1118 G-------HISDLQEDLDSERAARNKAEKQkrdLGEELEALKTEL-----------------EDTLDSTATQQELRAKRE 1173
Cdd:pfam19220 202 TqldatraRLRALEGQLAAEQAERERAEAQ---LEEAVEAHRAERaslrmklealtaraaatEQLLAEARNQLRDRDEAI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1174 QEVTVLKKALDEETRSHEAQVQEMRQKHTQaveeLTEQLEQFKRAKANLDKSKQTLEKEnadLAGELRVLGQAKQEVEHK 1253
Cdd:pfam19220 279 RAAERRLKEASIERDTLERRLAGLEADLER----RTQQFQEMQRARAELEERAEMLTKA---LAAKDAALERAEERIASL 351
|
330 340 350
....*....|....*....|....*....|....*
gi 241982718 1254 KKKLEVQLQDLQSKCSDGERARAELSDkvhKLQNE 1288
Cdd:pfam19220 352 SDRIAELTKRFEVERAALEQANRRLKE---ELQRE 383
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
887-1706 |
2.63e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 887 EEKTLLQEQLQAETELYaeaeEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLdleeqleeeeAAR 966
Cdd:PRK04863 280 ERRVHLEEALELRRELY----TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT----------ALR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 967 QKLQLEKVTA--EAKIKKLEDDILVMDDQNSKL--SKERK-LLEERVSDLTTNLAEEE--------------------EK 1021
Cdd:PRK04863 346 QQEKIERYQAdlEELEERLEEQNEVVEEADEQQeeNEARAeAAEEEVDELKSQLADYQqaldvqqtraiqyqqavqalER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 AKNLTKLKSKHESMISELEVRLKKEEKSR-QELEKLKRKLE--GDASDFHEQIADLQAQIA-ELKMQLAKkeEELQAALA 1097
Cdd:PRK04863 426 AKQLCGLPDLTADNAEDWLEEFQAKEQEAtEELLSLEQKLSvaQAAHSQFEQAYQLVRKIAgEVSRSEAW--DVARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1098 RLDEEIAQKNNAlkkiRELEGHISDLQEDLDSERAAR------NKAEKQKRDLGEELEALKTELEDTLDS-TATQQELRA 1170
Cdd:PRK04863 504 RLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAErllaefCKRLGKNLDDEDELEQLQEELEARLESlSESVSEARE 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1171 KREQEVTVLKKaLDEETRSHEAQVQEMRQKHtQAVEELTEQL-EQFKRAKANLDKSKQTLEKEnadlagelRVLGQAKQE 1249
Cdd:PRK04863 580 RRMALRQQLEQ-LQARIQRLAARAPAWLAAQ-DALARLREQSgEEFEDSQDVTEYMQQLLERE--------RELTVERDE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1250 VEHKKKKLEVQLQDLQSkcsdgeRARAELSdkvhKLQNEVESVTGMLnEAEGKAiklakDVAslgsqLQDTQ--ELLQEE 1327
Cdd:PRK04863 650 LAARKQALDEEIERLSQ------PGGSEDP----RLNALAERFGGVL-LSEIYD-----DVS-----LEDAPyfSALYGP 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1328 TRQKLNVS------TKLRQLEDERNSLQ------DQLDEEMEAKQNLERHVStlnIQLSDSKKKLQDFAstiEVMEEGKK 1395
Cdd:PRK04863 709 ARHAIVVPdlsdaaEQLAGLEDCPEDLYliegdpDSFDDSVFSVEELEKAVV---VKIADRQWRYSRFP---EVPLFGRA 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1396 RLQKEMEGLSQQYEEKAAAYDKLE---------------------------------KTKNRLQQELDDLVVDLDNQRQL 1442
Cdd:PRK04863 783 AREKRIEQLRAEREELAERYATLSfdvqklqrlhqafsrfigshlavafeadpeaelRQLNRRRVELERALADHESQEQQ 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1443 VSNLEKKQKKFDQLLAEEKNISSKYADER--DRAEaEAREKETKALSLARaleealeakeeLERTNKMLKAEMEDLVSSK 1520
Cdd:PRK04863 863 QRSQLEQAKEGLSALNRLLPRLNLLADETlaDRVE-EIREQLDEAEEAKR-----------FVQQHGNALAQLEPIVSVL 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1521 DDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAKLRLEVNMQ---ALKGQFERDLQARDEQNEEkRR 1592
Cdd:PRK04863 931 QSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfSYEDAAEMLAKNSDlneKLRQRLEQAEQERTRAREQ-LR 1009
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1593 QLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSaikGREEaikqlrKLQAQMKDFQRELDDARASRDEIF 1672
Cdd:PRK04863 1010 QAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS---GAEE------RARARRDELHARLSANRSRRNQLE 1080
|
890 900 910
....*....|....*....|....*....|....
gi 241982718 1673 ATSKENEKKAKSLEADLMQLQEDLAAAERARKQA 1706
Cdd:PRK04863 1081 KQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1282 |
2.90e-07 |
|
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: 55.80 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAET-----------ELYAEAEEMRVRLAA-KKQELEEILHEMEA 929
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleqnnkkikELEKQLNQLKSEISDlNNQKEQDWNKELKS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 930 RLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVS 1009
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1010 DLTTNLAEEEEKAKNL----TKLKSKHESMISELEVRLKKEEKSRQELEKLKRK----------LEGDASDFHEQIADLQ 1075
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKdeqiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknLDNTRESLETQLKVLS 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1076 AQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTEL 1155
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1156 EDTLDSTATQQelrakREQEVTVLKKALDEETRSHEaQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENAD 1235
Cdd:TIGR04523 555 KKENLEKEIDE-----KNKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 241982718 1236 LAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKV 1282
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1656-1934 |
3.38e-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: 55.84 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1656 DFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKqadlekeelaeelasslsgrntLQDEKRRLE 1735
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA----------------------LLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1736 ARIaqleeeleeeqgnmeaMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAK---- 1811
Cdd:TIGR02169 225 GYE----------------LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeee 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1812 ---LKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLE- 1887
Cdd:TIGR02169 289 qlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEd 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1888 ---EAEEESQRINANRRKL---QRELDEATESNEAMGREVNALKSKLRRGNEA 1934
Cdd:TIGR02169 369 lraELEEVDKEFAETRDELkdyREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1153-1481 |
3.40e-07 |
|
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: 55.25 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1153 TELEDTLDSTatqqelrakrEQEVTVLKKALDEETRSHE---AQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTL 1229
Cdd:pfam06160 89 DEIEELLDDI----------EEDIKQILEELDELLESEEknrEEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1230 EK---------ENADLAGELRVLGQAKQEVEHKKKKLEvQLQDLQSKCSDgeraraELSDKVHKLQNEVESVtgmlnEAE 1300
Cdd:pfam06160 159 EEefsqfeeltESGDYLEAREVLEKLEEETDALEELME-DIPPLYEELKT------ELPDQLEELKEGYREM-----EEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1301 G---KAIKLAKDVASLGSQLQDTQELLqEETRQKlNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSK 1377
Cdd:pfam06160 227 GyalEHLNVDKEIQQLEEQLEENLALL-ENLELD-EAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1378 KKLQDfastievmeegkkrLQKEMEGLSQQY---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQ----LVSNLEKKQ 1450
Cdd:pfam06160 305 EQNKE--------------LKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVayseLQEELEEIL 370
|
330 340 350
....*....|....*....|....*....|.
gi 241982718 1451 KKFDQLLAEEKNISSKYADERDrAEAEAREK 1481
Cdd:pfam06160 371 EQLEEIEEEQEEFKESLQSLRK-DELEAREK 400
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1262-1458 |
3.54e-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: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1262 QDLQSKCSDGERARAELSDKVHKLQNEVESVtgmlnEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQL 1341
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1342 EDERNSLQDQLDEEMEAK---------QNLERHVSTLNIQLSDSKKKLQDFASTI--------EVMEEGKKRLQKEMEGL 1404
Cdd:COG3206 239 EARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPNHPDVialraqiaALRAQLQQEAQRILASL 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1405 SQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLA 1458
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
865-1630 |
3.56e-07 |
|
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: 55.75 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 865 KERQQKAETELkELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAE 944
Cdd:TIGR00618 186 FAKKKSLHGKA-ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 945 rkkmaqqmldleeqleeeeaarqklqlekvtAEAKIKKLEDDILVMDDQNSKLSKERKLleERVSDLTTNLAEEEEKAKN 1024
Cdd:TIGR00618 265 -------------------------------LRARIEELRAQEAVLEETQERINRARKA--APLAAHIKAVTQIEQQAQR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1025 -LTKLKSKHESMISELEVRlKKEEKSRQELEKLKRKLEGDASDfHEQIADLQAQIAELKMQLAKKEEELQ--AALARLDE 1101
Cdd:TIGR00618 312 iHTELQSKMRSRAKLLMKR-AAHVKQQSSIEEQRRLLQTLHSQ-EIHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1102 EIAQKNNALKKIRELEGHISDLQEDLDSERaarnkaekqkRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKK 1181
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAF----------RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1182 ALDEETRSHEAQVQEMRQKHT--QAVEELTEQLEQFKRAKANLDK--SKQTLEKE-NADLAGELRVLGQAKQEVEHKKKK 1256
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQihLQETRKKAVVLARLLELQEEPCplCGSCIHPNpARQDIDNPGPLTRRMQRGEQTYAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1257 LEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLgsqLQDTQELLQEETRQKLNVST 1336
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHA 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1337 KLRQLEDERNSLQDQLDEEMEAK--QNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEglsQQYEEKAAA 1414
Cdd:TIGR00618 617 LLRKLQPEQDLQDVRLHLQQCSQelALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK---MQSEKEQLT 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1415 YDKLE-KTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALE 1493
Cdd:TIGR00618 694 YWKEMlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1494 EaleakeelertnkMLKAEMEDLVSskddvgknvhELEKSKRALETQMEEMKTQLEELEDELQATEDAKLrlevnmqALK 1573
Cdd:TIGR00618 774 L-------------QTGAELSHLAA----------EIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILN-------LQC 823
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1574 GQFERDLQARDEQNEEKRRQLQRQLHEYEtELEDERKQRALAAAAKKKLEGDLKDLE 1630
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEKSATLGEITHQLL-KYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1350-1913 |
3.68e-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: 55.61 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1350 DQLDEEMEAKQNLERHVSTLNIQLSDSKKKLqdfASTIEVMEEGKKRLQKEMEGLSQQYEEKAAaydklektknRLQQEL 1429
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLI---ASRQEERQETSAELNQLLRTLDDQWKEKRD----------ELNGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1430 DDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERdRAEAEAREKETKALSlaraleeaLEAKEELERTNKML 1509
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSW-QSELENLEERLKALT--------GKHQDVTAKYNRRR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1510 KAEMEDLvssKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAT--------EDAKLRLEVNMQALKGQFErDLQ 1581
Cdd:pfam12128 382 SKIKEQN---NRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQleagklefNEEEYRLKSRLGELKLRLN-QAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1582 ARDEQNEEKRrQLQRQLHEYETELEDERKQRAlaaaakkklegDLKDLELQADSAikgREEAIKQLRKLQAQMKDFQREL 1661
Cdd:pfam12128 458 ATPELLLQLE-NFDERIERAREEQEAANAEVE-----------RLQSELRQARKR---RDQASEALRQASRRLEERQSAL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1662 DDARASRD-------------------------------------EIFATSKENEKKAKSLEADLMQLQ--EDLAAAERA 1702
Cdd:pfam12128 523 DELELQLFpqagtllhflrkeapdweqsigkvispellhrtdldpEVWDGSVGGELNLYGVKLDLKRIDvpEWAASEEEL 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1703 RKQADLEKE------ELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGN----MEAMSDRVRKATLQAEQLSNE 1772
Cdd:pfam12128 603 RERLDKAEEalqsarEKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRlfdeKQSEKDKKNKALAERKDSANE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1773 LATERSTAQK-----NESARQQLERQNKELRS----KLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKS 1843
Cdd:pfam12128 683 RLNSLEAQLKqldkkHQAWLEEQKEQKREARTekqaYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAS 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1844 ----------LKQKDKKLKEVLLQVEDERKMAEQY---------------KEQAEKGNTKVK----QLKRQLEEAEEESQ 1894
Cdd:pfam12128 763 lgvdpdviakLKREIRTLERKIERIAVRRQEVLRYfdwyqetwlqrrprlATQLSNIERAISelqqQLARLIADTKLRRA 842
|
650
....*....|....*....
gi 241982718 1895 RINANRRKLQRELDEATES 1913
Cdd:pfam12128 843 KLEMERKASEKQQVRLSEN 861
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
863-1235 |
3.79e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 863 KIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhemEARLEEEEDRGQQLQ 942
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL---EQLSLATEEELQDLA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 943 AERKKMAQQMLDLeeqleeeEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEE-RVSDLTTNLAEEEEK 1021
Cdd:COG4717 199 EELEELQQRLAEL-------EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaALLALLGLGGSLLSL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 AKN------------------LTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKM 1083
Cdd:COG4717 272 ILTiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1084 QLAKKEEE----------------LQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNK--AEKQKRDLG 1145
Cdd:COG4717 352 LLREAEELeeelqleeleqeiaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1146 EELEALKTELEDTLDSTATQQELRAKREQEVTVLKKaldeetrshEAQVQEMRQKHTQAVEELTEQLEQFKR---AKANL 1222
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEE---------DGELAELLQELEELKAELRELAEEWAAlklALELL 502
|
410
....*....|...
gi 241982718 1223 DKSKQTLEKENAD 1235
Cdd:COG4717 503 EEAREEYREERLP 515
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1193-1706 |
4.44e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.29 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1193 QVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGE 1272
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1273 RARAELSDKVHKLQ------NEVESVTGMLNEAEGKA-----------IKLAKDVASLGSQLQDTQELLQ--EETRQKLN 1333
Cdd:PRK01156 253 RYESEIKTAESDLSmeleknNYYKELEERHMKIINDPvyknrnyindyFKYKNDIENKKQILSNIDAEINkyHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1334 VSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVM----EEGKKRLQKEMEGLSQQYE 1409
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiSEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1410 EKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQK--KFDQLLAEEK--NISSKYADERDRAEAEAREKETKA 1485
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpVCGTTLGEEKsnHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1486 LSLaraleeALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETqMEEMKTQLEELEDELQAT--EDAKL 1563
Cdd:PRK01156 493 KDI------DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINE-LKDKHDKYEEIKNRYKSLklEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1564 RLEVNMQALKGQFERDLQARDEQNEEKRRQL---QRQLHEYETELEDERKqralaaaakkKLEGDLKDLELQADSAikgr 1640
Cdd:PRK01156 566 KRTSWLNALAVISLIDIETNRSRSNEIKKQLndlESRLQEIEIGFPDDKS----------YIDKSIREIENEANNL---- 631
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1641 EEAIKQLRKLQAQMKDFQRELDDAR---ASRDEIFATSKENEKKAKSLEADLMQL--QEDLAAAERARKQA 1706
Cdd:PRK01156 632 NNKYNEIQENKILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNLKKSrkALDDAKANRARLES 702
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1509-1707 |
4.92e-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: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1509 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNE 1588
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1589 EKR----------RQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQ 1658
Cdd:COG4942 119 QPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 241982718 1659 RELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQAD 1707
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1450-1867 |
5.31e-07 |
|
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: 54.52 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1450 QKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHE 1529
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1530 LEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQnEEKRRQLQRQLHEYETELEDER 1609
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-EAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1610 KQRALaaaakkklegdLKDLELQADSAIKGREEAIKQLRKL--QAQMKDFQRE--LDDARASRdEIFATSkenEKKAKSL 1685
Cdd:pfam07888 192 KEFQE-----------LRNSLAQRDTQVLQLQDTITTLTQKltTAHRKEAENEalLEELRSLQ-ERLNAS---ERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1686 EADL--MQLQEDLAAAE--RARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRK 1761
Cdd:pfam07888 257 GEELssMAAQRDRTQAElhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1762 ATLQAEQLSNELATERSTaqkNESARQQLERQNKELRSKLQeVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAAT 1841
Cdd:pfam07888 337 ERMEREKLEVELGREKDC---NRVQLSESRRELQELKASLR-VAQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEA 412
|
410 420
....*....|....*....|....*.
gi 241982718 1842 KSLkqKDKKLKEVLLQVEDERKMAEQ 1867
Cdd:pfam07888 413 ALT--STERPDSPLSDSEDENPEALQ 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
862-1080 |
5.96e-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: 54.00 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELE-EILHEMEARLEEEEDRGQQ 940
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 941 LQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDdilvMDDQNSKLSKERKLLEERVSDLTTNLAEEEE 1020
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1021 KAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEgdasdfhEQIADLQAQIAE 1080
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAA 238
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1072-1455 |
6.29e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.92 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1072 ADLQAQIAELKMQLAKKEEE------LQAALARLD--EEIAQKNNALKK-IRELEGHISDLQEDLDSERAArNKAEKQKR 1142
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDklvqqdLEQTLALLDkiDRQKEETEQLKQqLAQAPAKLRQAQAELEALKDD-NDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1143 DLGEELEALKTELEDTLDSTAT-QQELRAKREQEVTVlkkaldeETRSHEAQVQEMR-QKHTQaveELTEQLEQFKRAKA 1220
Cdd:PRK11281 118 LSTLSLRQLESRLAQTLDQLQNaQNDLAEYNSQLVSL-------QTQPERAQAALYAnSQRLQ---QIRNLLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1221 NLDKSKQTLekenadLAGELRVLGQakqEVEHKKKKLEV--QLQDLqskcsdGERARAELSDKVHKLQNEVESVTGMLNE 1298
Cdd:PRK11281 188 ALRPSQRVL------LQAEQALLNA---QNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQLQLLQEAINS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1299 aegKAIKLAKDVASLGSQLQDTQE-----LLQEETRQKLNVSTKLRQLEDERNSL-QD------QLDEEMEAKQNLERHV 1366
Cdd:PRK11281 253 ---KRLTLSEKTVQEAQSQDEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLtQQnlrvknWLDRLTQSERNIKEQI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1367 STLNIQLSDSK---KKLQDFASTIEVMEEGKK----RL-QKEmegLSQQYEE--KAAAY-DKLEKT---------KNRLQ 1426
Cdd:PRK11281 330 SVLKGSLLLSRilyQQQQALPSADLIEGLADRiadlRLeQFE---INQQRDAlfQPDAYiDKLEAGhksevtdevRDALL 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 241982718 1427 QELD---DLVVDLD---------------NQRQLVSNLEKKQKKFDQ 1455
Cdd:PRK11281 407 QLLDerrELLDQLNkqlnnqlnlainlqlNQQQLLSVSDSLQSTLTQ 453
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1057-1277 |
7.88e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1057 KRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLdserAARNK 1136
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----GERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1137 AEKQKRDLGEELEALK--TELEDTLDSTATQQELRAKREQEVTVLKKALdEETRSHEAQVQEMRQKHTQAVEELTEQLEQ 1214
Cdd:COG3883 94 ALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1215 FKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAE 1277
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
999-1410 |
8.94e-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: 54.28 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 999 KERKLLEERVSDLTTNL----AEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADL 1074
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLrlapDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1075 QAQIAELKMQLAKKE--EELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQkrdlgEELEALK 1152
Cdd:TIGR00606 768 EEQETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ-----HELDTVV 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1153 TELEDTldstatqQELRAKREQEVTVLKKALDeETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQtlekE 1232
Cdd:TIGR00606 843 SKIELN-------RKLIQDQQEQIQHLKSKTN-ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKE----Q 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1233 NADLAGELRVLGQAKQEVEHKK----KKLEVQLQDLQSKCSDGERARAELSDKVH--------KLQNEVESVTGMLNEAE 1300
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKetsnKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgkddylkQKETELNTVNAQLEECE 990
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1301 GKAIKLAKDVASLGSQL--QDTQELLQEETRQKLNVSTKLRQLEDERNSL-----QDQLDEEMEAKQNLERHVSTLNIQL 1373
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHlkemgQMQVLQMKQEHQKLEENIDLIKRNH 1070
|
410 420 430
....*....|....*....|....*....|....*..
gi 241982718 1374 SDSKKKLQDFASTIEVMEegKKRLQKEMEGLSQQYEE 1410
Cdd:TIGR00606 1071 VLALGRQKGYEKEIKHFK--KELREPQFRDAEEKYRE 1105
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1280-1489 |
1.06e-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: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1280 DKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAK 1359
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1360 QNLERHVSTLNIQLSDskKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLvvdldnq 1439
Cdd:COG3883 96 YRSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL------- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 241982718 1440 RQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLA 1489
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1765-1912 |
1.12e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1765 QAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAKLKS-TVAALEAKIAQLEEQVEQEAREKQAATKS 1843
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpVIQQLRAQLAELEAELAELSARYTPNHPD 292
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1844 LKQKDKKLKEVLLQVEDE-RKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRK---LQRELDEATE 1912
Cdd:COG3206 293 VIALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARE 365
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
990-1262 |
1.33e-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: 53.59 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 990 MDDQNSKLSKERKLLEERVSDLttNLAEEEEKAKNLTKLKSKHESM----ISELE----VRLKKEEKSRQELEKL-KRKL 1060
Cdd:pfam17380 329 MDRQAAIYAEQERMAMEREREL--ERIRQEERKRELERIRQEEIAMeisrMRELErlqmERQQKNERVRQELEAArKVKI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1061 EGDasdfhEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKnnaLKKIRELE----GHISDLQEDLDSERAARNK 1136
Cdd:pfam17380 407 LEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARE---MERVRLEEqerqQQVERLRQQEEERKRKKLE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1137 AEKQKRD--LGEEL--EALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQL 1212
Cdd:pfam17380 479 LEKEKRDrkRAEEQrrKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM 558
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 241982718 1213 EQFKRAKANLDkskqTLEKEnadlagelRVLGQAKQEVEHKKKKLEVQLQ 1262
Cdd:pfam17380 559 RKATEERSRLE----AMERE--------REMMRQIVESEKARAEYEATTP 596
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1316-1735 |
1.34e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1316 QLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLD--EEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEg 1393
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1394 kkrLQKEMEGLSQQYEE-KAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERD 1472
Cdd:COG4717 161 ---LEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1473 RAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELE 1552
Cdd:COG4717 238 AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1553 DELQATEDAKLRLEVNMQA--LKGQFERDLQARDEQNEEKRRQLQRQLHEYETEL-----------EDERKQRALAAAAK 1619
Cdd:COG4717 318 EEELEELLAALGLPPDLSPeeLLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagvedEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1620 KKLEGDLKDLELQADSAIKGREEAIKQLRK--LQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADlmqlqEDLA 1697
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELA 472
|
410 420 430
....*....|....*....|....*....|....*...
gi 241982718 1698 AAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLE 1735
Cdd:COG4717 473 ELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1107-1481 |
1.63e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.92 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1107 NNALKKIRElegHISDLQEDLDSERAarNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEE 1186
Cdd:PRK04778 78 TNSLPDIEE---QLFEAEELNDKFRF--RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYREL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1187 TRSHEAQvqemRQKHTQAVEELTEQLEQFKRakanlDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEV------- 1259
Cdd:PRK04778 153 RKSLLAN----RFSFGPALDELEKQLENLEE-----EFSQFVELTESGDYVEAREILDQLEEELAALEQIMEEipellke 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1260 -------QLQDLQSKCsdgerarAELSDKVHKLQNevesvtgmlneaegkaIKLAKDVASLGSQLQDTQELLqEETRQKl 1332
Cdd:PRK04778 224 lqtelpdQLQELKAGY-------RELVEEGYHLDH----------------LDIEKEIQDLKEQIDENLALL-EELDLD- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1333 NVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLniqlsdskkklqdfASTIEVMEEGKKRLQKEMEGLSQQY---E 1409
Cdd:PRK04778 279 EAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTL--------------PDFLEHAKEQNKELKEEIDRVKQSYtlnE 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 1410 EKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQ----LVSNLEKKQKKFDQLLAEEKNISSKYADERDrAEAEAREK 1481
Cdd:PRK04778 345 SELESVRQLEKQLESLEKQYDEITERIAEQEIayseLQEELEEILKQLEEIEKEQEKLSEMLQGLRK-DELEAREK 419
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
939-1117 |
1.99e-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: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 939 QQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDIlvmDDQNSKLSKERKLLEERVSDL------- 1011
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGERARALyrsggsv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1012 --------TTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKM 1083
Cdd:COG3883 103 syldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|....
gi 241982718 1084 QLAKKEEELQAALARLDEEIAQKNNALKKIRELE 1117
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
866-1333 |
2.06e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKK---------QELEEILHEMEARLEEEED 936
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 937 RGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLA 1016
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1017 EEEEKAKNLTKLKSKHESMISELEVRLkkeeksRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAAL 1096
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAA------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1097 ARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtldstatQQELRAKREQEV 1176
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--------LEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1177 TVLKKALDEETRSHEAQVQEmRQKHTQAVEELTEQLEQFKRAKANL--DKSKQTLEKENADLAGELRVLGQAKQEVEHKK 1254
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1255 KKLEVQLQDLQSkcsdgERARAELSDKVHKLQNEVESVtgmlnEAEGKAIKLAKDVaslgsqLQDTQELLQEETRQKLN 1333
Cdd:COG4717 456 AELEAELEQLEE-----DGELAELLQELEELKAELREL-----AEEWAALKLALEL------LEEAREEYREERLPPVL 518
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
889-1349 |
2.34e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 889 KTLLQEQLQAEteLYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEeeaarqk 968
Cdd:COG4717 36 KSTLLAFIRAM--LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 969 LQLEKVTAEAKIKKLEDDIlvmddQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEvrlKKEEK 1048
Cdd:COG4717 107 LEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA---ELQEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1049 SRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLD--EEIAQKNNALKKIRELEGHISDLQED 1126
Cdd:COG4717 179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARLLLLIAAAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1127 LDSERAARNKAEKQKRDLG-------------EELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQ 1193
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1194 VQEMRQKHTQAVEELTEQLEQFKRAK--ANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDG 1271
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEELQleELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1272 ERARAELSDKvhKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQD--TQELLQEETRQKLNVSTKLRQLEDERNSLQ 1349
Cdd:COG4717 419 EELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1548-1962 |
2.85e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1548 LEELEdELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYeTELEDERKQRALAAAAKKKLEGDlK 1627
Cdd:PTZ00121 1029 IEELT-EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDF-DAKEDNRADEATEEAFGKAEEAK-K 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1628 DLELQADSAIKgREEAIKQL----RKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEadLMQLQEDLAAAERAR 1703
Cdd:PTZ00121 1106 TETGKAEEARK-AEEAKKKAedarKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE--EARKAEDAKKAEAAR 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1704 K--QADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRvRKATLQAEQLSNELATERSTAQ 1781
Cdd:PTZ00121 1183 KaeEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA-EEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1782 KNESARQQLERQNKELRsKLQEVEGAVKAKlkstvAALEAKIAQLEEQVEqEAREKQAATKSLKQKDKKLKEVLLQVEDE 1861
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEAR-KADELKKAEEKK-----KADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1862 RKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNEASFVPSRR 1941
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
410 420
....*....|....*....|.
gi 241982718 1942 AGGRRVIENTDGSEEEMDARD 1962
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADE 1435
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
965-1177 |
2.94e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 965 ARQKLQlekvTAEAKIK--KLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISEL--E 1040
Cdd:COG3206 187 LRKELE----EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1041 VRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAkkeEELQAALARLDEEIAQknnALKKIRELEGHI 1120
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1121 SDLQEDLDSEraarNKAEKQKRDLGEELEALKTELEDTLdstATQQELRAKREQEVT 1177
Cdd:COG3206 337 AQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVG 386
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
867-1363 |
3.31e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.50 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 867 RQQKAETELKELEQKHTQLAEEKTLLQEQLQA----ETELYAEAEEMRVRLAAKKQELEEIlhemeARLEEEEDRGQQLQ 942
Cdd:PRK10246 420 EQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNvtqeQTQRNAALNEMRQRYKEKTQQLADV-----KTICEQEARIKDLE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 943 AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDIlvmddqnSKLSKERKLLEERVSDLTTNLAEEEEKA 1022
Cdd:PRK10246 495 AQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEV-------KKLGEEGAALRGQLDALTKQLQRDESEA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1023 KNLTK----LKSKHESMISELEVR----------LKKEEKSRQELEKLKRKLEGDAsdfheQIADLQAQIAELKMQLAKK 1088
Cdd:PRK10246 568 QSLRQeeqaLTQQWQAVCASLNITlqpqddiqpwLDAQEEHERQLRLLSQRHELQG-----QIAAHNQQIIQYQQQIEQR 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1089 EEELQAALARLDEEIAQKNNalkkireleghisdlQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQEL 1168
Cdd:PRK10246 643 QQQLLTALAGYALTLPQEDE---------------EASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1169 RAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANldkskqtleKENADLAGELRVL--GQA 1246
Cdd:PRK10246 708 PHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQA---------SVFDDQQAFLAALldEET 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1247 KQEVEHKKKKLEVQLQDLQSKCSDGERARAElsdkvHKLQNEvesvtgmlneaegKAIKLAKDVASLGSQLQDTQELLQE 1326
Cdd:PRK10246 779 LTQLEQLKQNLENQRQQAQTLVTQTAQALAQ-----HQQHRP-------------DGLDLTVTVEQIQQELAQLAQQLRE 840
|
490 500 510
....*....|....*....|....*....|....*..
gi 241982718 1327 ETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLE 1363
Cdd:PRK10246 841 NTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1101-1466 |
4.17e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1101 EEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKrdlgEELEALKTELEDtldstATQQELRAKReqEVTVLK 1180
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQ-----APAKLRQAQA--ELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1181 KALDEETRSH---------EAQVQEMRQKHTQAVEELTE-------QLEQFKRAKANLDKSKQTLEKENADLAG------ 1238
Cdd:PRK11281 108 DDNDEETRETlstlslrqlESRLAQTLDQLQNAQNDLAEynsqlvsLQTQPERAQAALYANSQRLQQIRNLLKGgkvggk 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1239 ----ELRVLGQAKQ-----EVEHKKKKLEV--QLQDLqskcsdGERARAELSDKVHKLQNEVESVTGMLNEaegKAIKLA 1307
Cdd:PRK11281 188 alrpSQRVLLQAEQallnaQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQLQLLQEAINS---KRLTLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1308 KDVASLGSQLQDTQE-----LLQEETRQKLNVSTKLRQLEDERNSL-QD------QLDEEMEAKQNLERHVSTLNIQLSD 1375
Cdd:PRK11281 259 EKTVQEAQSQDEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLtQQnlrvknWLDRLTQSERNIKEQISVLKGSLLL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1376 SK------------KKLQDFASTI-----EVMEEGKKR---------LQKEMEGLSQQY-EEKAAAYDKLEKTKNRLqqe 1428
Cdd:PRK11281 339 SRilyqqqqalpsaDLIEGLADRIadlrlEQFEINQQRdalfqpdayIDKLEAGHKSEVtDEVRDALLQLLDERREL--- 415
|
410 420 430
....*....|....*....|....*....|....*...
gi 241982718 1429 LDDLVVDLDNQRQLVSNLEKKQKkfdQLLAEEKNISSK 1466
Cdd:PRK11281 416 LDQLNKQLNNQLNLAINLQLNQQ---QLLSVSDSLQST 450
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
965-1356 |
4.31e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 965 ARQKLQLEKV-----TAEAKIKKLEDDILVMDDQNSKLSKER------KLLEERVSDLTTNLAEEEEKAKN----LTKLK 1029
Cdd:PRK11281 76 DRQKEETEQLkqqlaQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTLDQLQNAQNDLAEynsqLVSLQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1030 SKHE---SMISELEVRLkkeeksrQELEK-LKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQ 1105
Cdd:PRK11281 156 TQPEraqAALYANSQRL-------QQIRNlLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1106 KNNALKKIRELEGHISDLQEDLDSERaarnkaekqkrdlgeelealKTELEDTLDSTATQQElrAKREQEVTVLKKALDE 1185
Cdd:PRK11281 229 RDYLTARIQRLEHQLQLLQEAINSKR--------------------LTLSEKTVQEAQSQDE--AARIQANPLVAQELEI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1186 ETRSHEAQVQEmrqkhTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGEL---RVLGQAKQEVEHKK--KKLEVQ 1260
Cdd:PRK11281 287 NLQLSQRLLKA-----TEKLNTLTQQNLRVKNWLDRLTQSERNIKEQISVLKGSLllsRILYQQQQALPSADliEGLADR 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1261 LQDLQSKCSDGERARAELSDK---VHKL-QNEVESVTGMLNEAegkaiklakdvasLGSQLQDTQELLQEETRQ---KLN 1333
Cdd:PRK11281 362 IADLRLEQFEINQQRDALFQPdayIDKLeAGHKSEVTDEVRDA-------------LLQLLDERRELLDQLNKQlnnQLN 428
|
410 420
....*....|....*....|....*..
gi 241982718 1334 VSTKL----RQLEDERNSLQDQLDEEM 1356
Cdd:PRK11281 429 LAINLqlnqQQLLSVSDSLQSTLTQQI 455
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
862-1377 |
4.72e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEmrvrlaAKKQELEEILHEMEARLEEEEDRGQQL 941
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE------EKEAQMEELNKAKAAHSFVVTEFEATT 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSdlTTNLAEE-EE 1020
Cdd:pfam05483 359 CSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ--FEKIAEElKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1021 KAKNLTKLKSKHESMISELEVRL----KKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKmQLAKKEEELQAAL 1096
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLtaikTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENK-ELTQEASDMTLEL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1097 ARLDEEIaqkNNALKKIRELEGHISDLQEdldSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:pfam05483 516 KKHQEDI---INCKKQEERMLKQIENLEE---KEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1177 TVLKKALDeetrsheaQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEV-EHKKK 1255
Cdd:pfam05483 590 KILENKCN--------NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIiDNYQK 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1256 KLEVQLQDLQSKCSDGERARAeLSDKVHKLQNEVE-----SVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQ 1330
Cdd:pfam05483 662 EIEDKKISEEKLLEEVEKAKA-IADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSA 740
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 241982718 1331 KLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSK 1377
Cdd:pfam05483 741 KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
972-1459 |
4.74e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 972 EKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKS-- 1049
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVis 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1050 --RQELEKLKRKLEGDASDFHEQIADLQ-------------AQIAELKMQLAKKEEELQAALARLDE---EIAQKNN--- 1108
Cdd:pfam05557 108 clKNELSELRRQIQRAELELQSTNSELEelqerldllkakaSEAEQLRQNLEKQQSSLAEAEQRIKElefEIQSQEQdse 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1109 ALKKIRELEGHISDLQEDLDSERAARNKAEKQKRD---LGEELEALKTELEDTLDSTATQQELRAKREQevtvLKKALDE 1185
Cdd:pfam05557 188 IVKNSKSELARIPELEKELERLREHNKHLNENIENkllLKEEVEDLKRKLEREEKYREEAATLELEKEK----LEQELQS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1186 ETRSHEAQVQEMRQKhtqavEELTEQLEQfkrakanLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQ 1265
Cdd:pfam05557 264 WVKLAQDTGLNLRSP-----EDLSRRIEQ-------LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1266 SKCSDGERARAELSDKVHKLQNEVESVTGMLnEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDER 1345
Cdd:pfam05557 332 KKLKRHKALVRRLQRRVLLLTKERDGYRAIL-ESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEEL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1346 NSLQDQ---LDEEMEAK--QNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGL---------------- 1404
Cdd:pfam05557 411 GGYKQQaqtLERELQALrqQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRclqgdydpkktkvlhl 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1405 -----SQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQL-VSNLEKKQKKFDQLLAE 1459
Cdd:pfam05557 491 smnpaAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLpETTSTMNFKEVLDLRKE 551
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1321-1536 |
5.32e-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: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1321 QELLQEETRQKLN-VSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQK 1399
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1400 EMEGLSQQYEEKAAAYDKLEKTKNRL----QQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAE 1475
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1476 AEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRA 1536
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1033-1249 |
5.65e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1033 ESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKK 1112
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1113 IRELEGHISDLQEDLDSE----------------RAARNKAEKQKRDLgEELEALKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldrlsalskiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1177 TVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQE 1249
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1025-1449 |
7.02e-06 |
|
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: 51.01 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1025 LTKLKSKHESMISELEVRLKKEEKSRQELEKLKrklegdasdfhEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIA 1104
Cdd:pfam06160 95 LDDIEEDIKQILEELDELLESEEKNREEVEELK-----------DKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1105 QKNN---------ALKKIRELEGHISDLQEDLDseraarnkaekqkrDLGEELEALKTELEDTLDS-TATQQELrakREQ 1174
Cdd:pfam06160 164 QFEEltesgdyleAREVLEKLEEETDALEELME--------------DIPPLYEELKTELPDQLEElKEGYREM---EEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1175 EVTVLKKALDEETRSHEAQVQEmrqkhtqaVEELTEQLEqFKRAKANLDKSKQTLEKENADLAGELrvlgQAKQEVEHKK 1254
Cdd:pfam06160 227 GYALEHLNVDKEIQQLEEQLEE--------NLALLENLE-LDEAEEALEEIEERIDQLYDLLEKEV----DAKKYVEKNL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1255 KKLEVQLQDLQskcsdgeraraelsDKVHKLQNEVESVT---GMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEET--- 1328
Cdd:pfam06160 294 PEIEDYLEHAE--------------EQNKELKEELERVQqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEvay 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1329 ---RQKLNVSTK-LRQLEDERNSLQDQL----DEEMEAKQNLERhvstLNIQLSDSKKKLQdfastievmeegKKRLqke 1400
Cdd:pfam06160 360 selQEELEEILEqLEEIEEEQEEFKESLqslrKDELEAREKLDE----FKLELREIKRLVE------------KSNL--- 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1401 mEGLSQQYEE-KAAAYDKLEKTKNRLQQ---ELDDLVVDLDNQRQLVSNLEKK 1449
Cdd:pfam06160 421 -PGLPESYLDyFFDVSDEIEDLADELNEvplNMDEVNRLLDEAQDDVDTLYEK 472
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1538-1788 |
8.14e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1538 ETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAA 1617
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1618 AKKKLEGDLKDLE--LQADSAikgrEEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQED 1695
Cdd:COG3883 94 ALYRSGGSVSYLDvlLGSESF----SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1696 LAAAERARKQADLEKeelaeelasslsgrNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELAT 1775
Cdd:COG3883 170 KAELEAQQAEQEALL--------------AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
250
....*....|...
gi 241982718 1776 ERSTAQKNESARQ 1788
Cdd:COG3883 236 AAAAAAAAASAAG 248
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1175-1448 |
1.10e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1175 EVTVLKKALDEETRShEAQVQEMRQKHTQAVEELTE--QLEQFKRAKANLDKsKQTLEKENADLAGELrvlgqaKQEVEh 1252
Cdd:PHA02562 167 EMDKLNKDKIRELNQ-QIQTLDMKIDHIQQQIKTYNknIEEQRKKNGENIAR-KQNKYDELVEEAKTI------KAEIE- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1253 kkkKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTgmlneaegKAIKLAKD---VASLGSQLQDTQELLQEETR 1329
Cdd:PHA02562 238 ---ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ--------KVIKMYEKggvCPTCTQQISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1330 QKLNVSTKLRQLEDERNSLQDQLDEEMEakqnLERHVSTLNIQLSDSKKKLQDFASTIevmeegkKRLQKEMEGLSQQYE 1409
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEEIMDEFNE----QSKKLLELKNKISTNKQSLITLVDKA-------KKVKAAIEELQAEFV 375
|
250 260 270
....*....|....*....|....*....|....*....
gi 241982718 1410 EKAAAYDKLEKTKNRLQQELDDLVVDLDnQRQLVSNLEK 1448
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKY-HRGIVTDLLK 413
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1069-1298 |
1.30e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1069 EQIADLQAQIAE--LKMQLAKKEEELQAALARLDEEIAQknnALKKIRELEGHISDLQE-----DLDSERAArnkAEKQK 1141
Cdd:COG3206 148 ELAAAVANALAEayLEQNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQknglvDLSEEAKL---LLQQL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1142 RDLGEELEALKTELEDTldsTATQQELRAKREQEVTVLKKAL-DEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKA 1220
Cdd:COG3206 222 SELESQLAEARAELAEA---EARLAALRAQLGSGPDALPELLqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1221 NLDKSKQTLEKENADLAGELRVlgqAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDkvhkLQNEVESVTGMLNE 1298
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYES 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
862-1061 |
1.32e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKH--TQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEED--R 937
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 938 GQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVmddqnsKLSKERKLLEERVSDLTTNLAE 1017
Cdd:COG3206 265 IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA------SLEAELEALQAREASLQAQLAQ 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 241982718 1018 EEEKAKNLTKLKSKHESMISELEVrlkkeekSRQELEKLKRKLE 1061
Cdd:COG3206 339 LEARLAELPELEAELRRLEREVEV-------ARELYESLLQRLE 375
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1025-1447 |
1.45e-05 |
|
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: 50.12 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1025 LTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIA 1104
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1105 QKNNALKKIRELEGHISDLQEDLDSeraarnkaekqkrdLGEELEALKTELEDtldstaTQQELRAKReQEVTVLKKALD 1184
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISC--------------LKNELSELRRQIQR------AELELQSTN-SELEELQERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1185 EETR----------SHEAQVQEmRQKHTQAVEELTEQLEQFKRAKANLDKSKQ------TLEKENADLAGELRVLGQAKQ 1248
Cdd:pfam05557 143 LLKAkaseaeqlrqNLEKQQSS-LAEAEQRIKELEFEIQSQEQDSEIVKNSKSelaripELEKELERLREHNKHLNENIE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1249 EVEhkkkKLEVQLQDLQSKCSDGERARAELSDkvhkLQNEVESVTGMLNEAE------GKAIKLAKDVASLGSQLQDTQE 1322
Cdd:pfam05557 222 NKL----LLKEEVEDLKRKLEREEKYREEAAT----LELEKEKLEQELQSWVklaqdtGLNLRSPEDLSRRIEQLQQREI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1323 LLQEE----TRQKLNVSTKLRQLEDERNSLQDQLDEEM-------EAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVME 1391
Cdd:pfam05557 294 VLKEEnsslTSSARQLEKARRELEQELAQYLKKIEDLNkklkrhkALVRRLQRRVLLLTKERDGYRAILESYDKELTMSN 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1392 EGKKRLQ--KEMEGLSQQY----EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLE 1447
Cdd:pfam05557 374 YSPQLLEriEEAEDMTQKMqahnEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLAD 435
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
866-1611 |
1.62e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAETELKELEqkhTQLAEEKTLLQEQlQAETELYAEAeemrvrlaakKQELEEI---LHEMEARLEEEEDRGQQLQ 942
Cdd:PRK04863 383 ARAEAAEEEVDELK---SQLADYQQALDVQ-QTRAIQYQQA----------VQALERAkqlCGLPDLTADNAEDWLEEFQ 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 943 AERKKMAQQMLDLEEQLEEEEAARQklQLEKvtAEAKIKKLEDDILVMDDQNSKLSKERKLLEER------------VSD 1010
Cdd:PRK04863 449 AKEQEATEELLSLEQKLSVAQAAHS--QFEQ--AYQLVRKIAGEVSRSEAWDVARELLRRLREQRhlaeqlqqlrmrLSE 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1011 LTTNLAEEEEKAKNLTKLKSKHESMI---SELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKmQLAK 1087
Cdd:PRK04863 525 LEQRLRQQQRAERLLAEFCKRLGKNLddeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA-ARAP 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1088 KEEELQAALARLDEeiaQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALkteledTLDSTATQQE 1167
Cdd:PRK04863 604 AWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL------SQPGGSEDPR 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1168 LRAKREQEVTVLKKALDEETRSHEAQVQEMR---QKHTQAVEELTeqleqfkRAKANLDKSKQTLEkenaDL---AGELR 1241
Cdd:PRK04863 675 LNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLS-------DAAEQLAGLEDCPE----DLyliEGDPD 743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1242 VLGQAKQEVEHKKKKLEVQLQDLQSKCSD-------GERARAELsdkVHKLQNEVESVTGMLNEAEGKAIKLAKDVASL- 1313
Cdd:PRK04863 744 SFDDSVFSVEELEKAVVVKIADRQWRYSRfpevplfGRAAREKR---IEQLRAEREELAERYATLSFDVQKLQRLHQAFs 820
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1314 ---GSQLQ-----DTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDS-KKKLQDFA 1384
Cdd:PRK04863 821 rfiGSHLAvafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlADRVEEIR 900
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1385 STIEVMEEGKKRLQKEMEGLSQ-------------QYEEKAAAYDKLEKTKNRLQQELDDLvVDLdNQRQLVSNLEKKQk 1451
Cdd:PRK04863 901 EQLDEAEEAKRFVQQHGNALAQlepivsvlqsdpeQFEQLKQDYQQAQQTQRDAKQQAFAL-TEV-VQRRAHFSYEDAA- 977
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1452 kfdQLLAEEKNISSKYADERDRAEAEAREketkalslaraleealeakeelertnkmLKAEMEDLVSSKDDVGKNVHELE 1531
Cdd:PRK04863 978 ---EMLAKNSDLNEKLRQRLEQAEQERTR----------------------------AREQLRQAQAQLAQYNQVLASLK 1026
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1532 KSKRALETQMEEMKTQLEELedELQATEDAKLRLEVNmqalkgqfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQ 1611
Cdd:PRK04863 1027 SSYDAKRQMLQELKQELQDL--GVPADSGAEERARAR--------RDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK 1096
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1002-1553 |
1.96e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.05 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1002 KLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELE-VRLKKEEKSRQELEKLKRKLEGDASDFHEQI-ADLQAQIA 1079
Cdd:TIGR01612 675 ALYNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQnMETATVELHLSNIENKKNELLDIIVEIKKHIhGEINKDLN 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1080 ELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDlQEDLDSeraarNKAEKQKRDLGEELEALKTELEDTL 1159
Cdd:TIGR01612 755 KILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND-QINIDN-----IKDEDAKQNYDKSKEYIKTISIKED 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1160 DSTATQQELRAKREQEVTVLKKALD------EETRSHEAQVQEMRQKHTQAV--EELTEQLEQFKRAKANLDKSKQTLEK 1231
Cdd:TIGR01612 829 EIFKIINEMKFMKDDFLNKVDKFINfennckEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDSKSLINEINKSIEE 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1232 ENADLA------GELRVLGQAKQEVEHKKKKlEVQLQDLQSKCSDGERaRAELSDKVHKLQNEvESVTGMLNEAEgkaiK 1305
Cdd:TIGR01612 909 EYQNINtlkkvdEYIKICENTKESIEKFHNK-QNILKEILNKNIDTIK-ESNLIEKSYKDKFD-NTLIDKINELD----K 981
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1306 LAKDvASLGSQLQDTQELLQEETRQKLNVSTklrqleDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLqdFAS 1385
Cdd:TIGR01612 982 AFKD-ASLNDYEAKNNELIKYFNDLKANLGK------NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAI--HTS 1052
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1386 TIEVMEEGKKRLQKEMEGLSQQYEEKA-AAYDKLEKTKNRLqqelddlvvdldnqrqlvsnlekKQKKFDQLLAEEkNIs 1464
Cdd:TIGR01612 1053 IYNIIDEIEKEIGKNIELLNKEILEEAeINITNFNEIKEKL-----------------------KHYNFDDFGKEE-NI- 1107
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1465 sKYADErdraeaeareketkalslaraleealeakeelerTNKMlkaeMEDLVSSKDDVGKNVHELEKSKRALETQMEEM 1544
Cdd:TIGR01612 1108 -KYADE----------------------------------INKI----KDDIKNLDQKIDHHIKALEEIKKKSENYIDEI 1148
|
....*....
gi 241982718 1545 KTQLEELED 1553
Cdd:TIGR01612 1149 KAQINDLED 1157
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1089-1321 |
2.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1089 EEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLdseraarNKAEKQKRDLGEELEALKTELEdtldstATQQEL 1168
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEY-------NELQAELEALQAEIDKLQAEIA------EAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1169 RAKREQevtvlkkaLDEETRSheAQVQEMRQKHTQAV------EELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRV 1242
Cdd:COG3883 82 EERREE--------LGERARA--LYRSGGSVSYLDVLlgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1243 LGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQ 1321
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1069-1195 |
2.51e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.81 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1069 EQIADLQAQIAELKMQLA---KKEEELQAALARLDEEIAQKnnalkkirelEGHISDLQEDLDSERAARNKAEKQKRDLG 1145
Cdd:PRK09039 53 SALDRLNSQIAELADLLSlerQGNQDLQDSVANLRASLSAA----------EAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1146 EELEALKTELEDTLDSTAT-QQELRAKREQeVTVLKKALD-EETRSHEAQVQ 1195
Cdd:PRK09039 123 QELDSEKQVSARALAQVELlNQQIAALRRQ-LAALEAALDaSEKRDRESQAK 173
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
886-1706 |
2.53e-05 |
|
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: 49.57 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 886 AEEKTLLQEQLQAETELYAEAEEmrvrLAAKKQELEEILHEMEARLEEEEDRGQQLQAE-------RKKMAQQ------- 951
Cdd:COG3096 278 NERRELSERALELRRELFGARRQ----LAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnlvQTALRQQekieryq 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 952 --MLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDI-----------LVMDDQNSK----------LSKERKLLEErv 1008
Cdd:COG3096 354 edLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslksqladyqQALDVQQTRaiqyqqavqaLEKARALCGL-- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1009 SDLT-TNLAEEEEKAKnlTKLKSKHESMIsELEVRLKKEEKSRQELEK---LKRKLEG--DASDFHEQIADLQAQIAELK 1082
Cdd:COG3096 432 PDLTpENAEDYLAAFR--AKEQQATEEVL-ELEQKLSVADAARRQFEKayeLVCKIAGevERSQAWQTARELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1083 MQlAKKEEELQAALARLDEEIAQKNNAlkkIRELEGHISDLQEDLDSEraarnkaekqkRDLGEELEALKTELEDTLDST 1162
Cdd:COG3096 509 AL-AQRLQQLRAQLAELEQRLRQQQNA---ERLLEEFCQRIGQQLDAA-----------EELEELLAELEAQLEELEEQA 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1163 ATQQELRAKREQEvtvlkkaLDEetrsHEAQVQEMRQK----HT--QAVEELTEQL-EQFKRAKANLDKSKQTLEKEnad 1235
Cdd:COG3096 574 AEAVEQRSELRQQ-------LEQ----LRARIKELAARapawLAaqDALERLREQSgEALADSQEVTAAMQQLLERE--- 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1236 lagelRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVH-KLQNEV-ESVTgmLNEA-------------- 1299
Cdd:COG3096 640 -----REATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGgVLLSEIyDDVT--LEDApyfsalygparhai 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1300 -----EGKAIKLAK-------------DVASLGSQLQDTQEL-----LQEETRQkLNVST--------------KLRQLE 1342
Cdd:COG3096 713 vvpdlSAVKEQLAGledcpedlyliegDPDSFDDSVFDAEELedavvVKLSDRQ-WRYSRfpevplfgraarekRLEELR 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1343 DERNSLQDQLDEEMEAKQNLERHVSTLNiqlsdskkklQDFASTIEVMEEGKKrlQKEMEGLSQQYEEKAAAYDKLEKTK 1422
Cdd:COG3096 792 AERDELAEQYAKASFDVQKLQRLHQAFS----------QFVGGHLAVAFAPDP--EAELAALRQRRSELERELAQHRAQE 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1423 NRLQQELDDLVVDLDNQRQLVSNLEkkqkkfdqLLAEEknisskyaDERDRAEaEAREKETKALSLARALEEALEAKeel 1502
Cdd:COG3096 860 QQLRQQLDQLKEQLQLLNKLLPQAN--------LLADE--------TLADRLE-ELREELDAAQEAQAFIQQHGKAL--- 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1503 ertnkmlkAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAKLRLEVN---MQALKG 1574
Cdd:COG3096 920 --------AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLGENsdlNEKLRA 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1575 QFERDLQARDEQNeEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSaikGREEaikqlrKLQAQM 1654
Cdd:COG3096 992 RLEQAEEARREAR-EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA---EAEE------RARIRR 1061
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1655 KDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQA 1706
Cdd:COG3096 1062 DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1004-1923 |
2.63e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 49.83 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1004 LEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQElEKLKRKLEGD-------ASDFHEQIADLQA 1076
Cdd:PTZ00440 510 IKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKD-EKLKRSMKNDiknkikyIEENVDHIKDIIS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1077 QIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIREL--EGHISDLQEDLDS-------------ERAARNKAEKQK 1141
Cdd:PTZ00440 589 LNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYIlnKFYKGDLQELLDElshflddhkylyhEAKSKEDLQTLL 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1142 RDLGEELEALKTELEDTLDSTAtqQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKAN 1221
Cdd:PTZ00440 669 NTSKNEYEKLEFMKSDNIDNII--KNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEK 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1222 LDKSKQTLEKENADLAGELRvlgqakqevEHKKKKLEVQ---LQDLQSKCSDGERARAeLSDKVHKLQNEVESVTGMLNE 1298
Cdd:PTZ00440 747 LEVYKHQIINRKNEFILHLY---------ENDKDLPDGKntyEEFLQYKDTILNKENK-ISNDINILKENKKNNQDLLNS 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1299 AEGKAIKLAKDVASLGSQLQDTQELLQEEtrqklNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVS---TLNIQLSD 1375
Cdd:PTZ00440 817 YNILIQKLEAHTEKNDEELKQLLQKFPTE-----DENLNLKELEKEFNENNQIVDNIIKDIENMNKNINiikTLNIAINR 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1376 SKKKLQDFASTIEVMEEGKKRLQKEMEGLSQ----QYEEKAAAYDKLEKTKNRLQQELDDLVVDldnqrQLVSNLEKKQK 1451
Cdd:PTZ00440 892 SNSNKQLVEHLLNNKIDLKNKLEQHMKIINTdniiQKNEKLNLLNNLNKEKEKIEKQLSDTKIN-----NLKMQIEKTLE 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1452 KFDQLlaeEKNISSKyaDERDRAEAEAREKETKALSlARALEEALEAKEELERTNKMLKAEMEDLV--SSKDDVGKNvHE 1529
Cdd:PTZ00440 967 YYDKS---KENINGN--DGTHLEKLDKEKDEWEHFK-SEIDKLNVNYNILNKKIDDLIKKQHDDIIelIDKLIKEKG-KE 1039
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1530 LEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHEYETELEDER 1609
Cdd:PTZ00440 1040 IEEKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVE-ALLKKIDENKNKLIEIKNKSHEHVVNADKEK 1118
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1610 KQralAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMkdfQRELDDARASRDEIFATSKENEKKAKSLEADL 1689
Cdd:PTZ00440 1119 NK---QTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVN---EIEIEYERILIDHIVEQINNEAKKSKTIMEEI 1192
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1690 MQLQEDLaaaerarKQADLEKEELAEELASSLSgRNTLQDEKRRLEARIAQLEEELEEEQGNMEAmSDRVRKATLQAEQL 1769
Cdd:PTZ00440 1193 ESYKKDI-------DQVKKNMSKERNDHLTTFE-YNAYYDKATASYENIEELTTEAKGLKGEANR-STNVDELKEIKLQV 1263
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1770 SNELATERSTAQKNESARQQLERQNKELRS---------------KLQEVEGAVKAKLKSTVAAL---EAKIAQLEE--- 1828
Cdd:PTZ00440 1264 FSYLQQVIKENNKMENALHEIKNMYEFLISidsekilkeilnstkKAEEFSNDAKKELEKTDNLIkqvEAKIEQAKEhkn 1343
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1829 ---------QVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQleEAEEESQRINAN 1899
Cdd:PTZ00440 1344 kiygsledkQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDKIDFLNKH--EAIEPSNSKEVN 1421
|
970 980
....*....|....*....|....*
gi 241982718 1900 RRKLQRELDEATE-SNEAMGREVNA 1923
Cdd:PTZ00440 1422 IIKITDNINKCKQySNEAMETENKA 1446
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
874-1395 |
2.81e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 874 ELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAA---KKQELEEILHEMEARLEEEEDRGQQLQA--ERKKM 948
Cdd:PRK01156 205 QIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSledMKNRYESEIKTAESDLSMELEKNNYYKEleERHMK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 949 AQQMLDLEEQLEEEEAARQKLQLEKVTA------------EAKIKKLE------DDILVMDDQNSKLSKERKLLEERVSD 1010
Cdd:PRK01156 285 IINDPVYKNRNYINDYFKYKNDIENKKQilsnidaeinkyHAIIKKLSvlqkdyNDYIKKKSRYDDLNNQILELEGYEMD 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1011 LTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEE 1090
Cdd:PRK01156 365 YNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1091 ELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSEraaRNKAEKQKRDLGEELEALKtELEDTLDSTATQQELRA 1170
Cdd:PRK01156 445 NMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEK---IREIEIEVKDIDEKIVDLK-KRKEYLESEEINKSINE 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1171 KReqevtvLKKALDEETRSHEAQVQEMRQKHTQAvEELTEQLEQFKRakANLDKSKQTLEKENADLAG-ELRVLGQAKQE 1249
Cdd:PRK01156 521 YN------KIESARADLEDIKIKINELKDKHDKY-EEIKNRYKSLKL--EDLDSKRTSWLNALAVISLiDIETNRSRSNE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1250 VEHKKKKLEVQLQDLQSKCSDGErarAELSDKVHKLQNEVESVTGMLNEAEGKAI---KLAKDVASLGSQLQDTQELlqe 1326
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEIQENKIlieKLRGKIDNYKKQIAEIDSI--- 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1327 ETRQKlNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKK 1395
Cdd:PRK01156 666 IPDLK-EITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1372-1595 |
2.84e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1372 QLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQK 1451
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1452 K-------FDQLLAeekniSSKYADERDRAEAeareketkalsLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVG 1524
Cdd:COG3883 97 RsggsvsyLDVLLG-----SESFSDFLDRLSA-----------LSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1525 KNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQ 1595
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
965-1915 |
2.95e-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: 49.66 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 965 ARQKLQLEKVTAE-AKIKKLEDDILVMDdqNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRL 1043
Cdd:TIGR01612 775 AKEKDELNKYKSKiSEIKNHYNDQINID--NIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFI 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1044 KKEEKSrqeleklKRKLEGDASDFHEQIADLQAQIAELKMQLAKKE----EELQAALARLDEEIAQKNNALKKIrelEGH 1119
Cdd:TIGR01612 853 NFENNC-------KEKIDSEHEQFAELTNKIKAEISDDKLNDYEKKfndsKSLINEINKSIEEEYQNINTLKKV---DEY 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1120 ISDLQEDLDSERAARNKAEKQKRDLGEELEALKteledtlDSTATQQELRAKREQEVTVLKKALDEETRshEAQVQEMRQ 1199
Cdd:TIGR01612 923 IKICENTKESIEKFHNKQNILKEILNKNIDTIK-------ESNLIEKSYKDKFDNTLIDKINELDKAFK--DASLNDYEA 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1200 KHTqaveeltEQLEQFKRAKANLDKSKQTLekenadlagelrvLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERAraeLS 1279
Cdd:TIGR01612 994 KNN-------ELIKYFNDLKANLGKNKENM-------------LYHQFDEKEKATNDIEQKIEDANKNIPNIEIA---IH 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1280 DKVHKLQNEVESVTG---------MLNEAEGKAIKLAKDVASLgsQLQDTQELLQEETrqkLNVSTKLRQLEDERNSLQD 1350
Cdd:TIGR01612 1051 TSIYNIIDEIEKEIGkniellnkeILEEAEINITNFNEIKEKL--KHYNFDDFGKEEN---IKYADEINKIKDDIKNLDQ 1125
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1351 QLDEEM----EAKQNLERHVSTLNIQLSDskkkLQDFASTiEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRlq 1426
Cdd:TIGR01612 1126 KIDHHIkaleEIKKKSENYIDEIKAQIND----LEDVADK-AISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-- 1198
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1427 qelddlvvdldnqrqlVSNLEKKQKKfdqlLAEEKNISSKYA------------DERDRAE--AEAREKETKALSLARAL 1492
Cdd:TIGR01612 1199 ----------------IAEIEKDKTS----LEEVKGINLSYGknlgklflekidEEKKKSEhmIKAMEAYIEDLDEIKEK 1258
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1493 EEALEAKEELERTnkmLKAEMEDLVSSKDDVgKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNM-QA 1571
Cdd:TIGR01612 1259 SPEIENEMGIEMD---IKAEMETFNISHDDD-KDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLlDA 1334
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1572 LKGQFERDLQARDEQN------EEKRRQLQRQLHEYETELEDERKQ------RALAAAAKKKLEGDLKDLELQADSAIKG 1639
Cdd:TIGR01612 1335 QKHNSDINLYLNEIANiynilkLNKIKKIIDEVKEYTKEIEENNKNikdeldKSEKLIKKIKDDINLEECKSKIESTLDD 1414
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1640 RE--EAIKQLRKLQAQMKDfqrelddARASRDEIFATSKENEKK----------AKSLEADLMQLQEDLAAAERARKQAD 1707
Cdd:TIGR01612 1415 KDidECIKKIKELKNHILS-------EESNIDTYFKNADENNENvlllfkniemADNKSQHILKIKKDNATNDHDFNINE 1487
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1708 LEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNEL--ATERSTAQKNES 1785
Cdd:TIGR01612 1488 LKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIkdAHKKFILEAEKS 1567
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1786 arqqlERQNKELRSKLQEVEGAVKAKLKSTVAALEA------------KIAQLEEQV-----EQEAREKQAATKSLKQKD 1848
Cdd:TIGR01612 1568 -----EQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIqlslenfenkflKISDIKKKIndclkETESIEKKISSFSIDSQD 1642
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1849 KKLKEVLLQVEDERKMAEQYKEQaekgntkvkqlKRQLEEAEEESQRINANRRKLQRELDEATESNE 1915
Cdd:TIGR01612 1643 TELKENGDNLNSLQEFLESLKDQ-----------KKNIEDKKKELDELDSEIEKIEIDVDQHKKNYE 1698
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
972-1284 |
3.26e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 48.90 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 972 EKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEE---EEKAKNLTKLKSKHESMISEL--EVRLKKE 1046
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDEcwkKIKRKKNSALSEALNGFKYEAnfKSRLLRE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1047 EKSRQE-------LEKLKRKLEG-----------------DASDFHEQIADLQ------AQIAELKMQLAKKE------- 1089
Cdd:pfam13166 170 IEKDNFnagvllsDEDRKAALATvfsdnkpeiapltfnviDFDALEKAEILIQkvigksSAIEELIKNPDLADwveqgle 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1090 -----------------EELQAALAR-LDEEIAQKNNALKK-IRELEGHISDLQEDLDSeRAARNKAEKQKRDLGEELEA 1150
Cdd:pfam13166 250 lhkahldtcpfcgqplpAERKAALEAhFDDEFTEFQNRLQKlIEKVESAISSLLAQLPA-VSDLASLLSAFELDVEDIES 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1151 LKTELEDTLDSTatQQELRAKREQEVTV--LKKALDEETRSHEAQVQ---------EMRQKHTQAVEELTEQLEQF--KR 1217
Cdd:pfam13166 329 EAEVLNSQLDGL--RRALEAKRKDPFKSieLDSVDAKIESINDLVASineliakhnEITDNFEEEKNKAKKKLRLHlvEE 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1218 AKANLDKskqtLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHK 1284
Cdd:pfam13166 407 FKSEIDE----YKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKA 469
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1033-1159 |
3.32e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1033 ESMISELEVRLKKEEKSRQELEKLK-----RKLEGDASDFHEQIADLQAQIAELKMQLAKKE---EELQAALARLDEEIA 1104
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHeerelTEEEEEIRRLEEQVERLEAEVEELEAELEEKDeriERLERELSEARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 1105 QKNNALKKIRELEGHISDLQEDLDSEraaRNKAEKQKRDLGEELEALKTELEDTL 1159
Cdd:COG2433 459 REIRKDREISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1234-1612 |
3.35e-05 |
|
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: 48.53 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1234 ADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGkaiklakDVASL 1313
Cdd:pfam19220 16 ADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1314 GSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQ----DFASTIE- 1388
Cdd:pfam19220 89 VARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQraegELATAREr 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1389 --VMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLvvdldnQRQLVSNLEKKQKKFDQLLAEEKNISSK 1466
Cdd:pfam19220 169 laLLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRAL------EGQLAAEQAERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1467 YADERDRAEA-EAREKET-KALSLARALEEAleakeeleRTNKMLKAE--MEDLVSSKDDVGKNVHELEKSKRALETQME 1542
Cdd:pfam19220 243 RASLRMKLEAlTARAAATeQLLAEARNQLRD--------RDEAIRAAErrLKEASIERDTLERRLAGLEADLERRTQQFQ 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1543 EMKTQLEELEDE-------LQATEDAKLRLEVNMQALKGQFErDLQARDEQneeKRRQLQRQLHEYETELEDERKQR 1612
Cdd:pfam19220 315 EMQRARAELEERaemltkaLAAKDAALERAEERIASLSDRIA-ELTKRFEV---ERAALEQANRRLKEELQRERAER 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1757-1934 |
4.85e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1757 DRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKA-KLKSTVAALEAKIAQLEEQVEqEAR 1835
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLE-ELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1836 EKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKgntkvkqlkRQLEEAEEESQRINANRRKLQRELDEATESNE 1915
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATE---------EELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*....
gi 241982718 1916 AMGREVNALKSKLRRGNEA 1934
Cdd:COG4717 224 ELEEELEQLENELEAAALE 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1529-1930 |
5.44e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1529 ELEKSKRALETQMEemktQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRrqlqrqlheYETELEDE 1608
Cdd:PRK04863 294 ELYTSRRQLAAEQY----RLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIER---------YQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1609 RKQRALAAAAKKKLEGDLKDLELQADSAikgrEEAIKQLRKlqaQMKDFQRELDDA--RASRdeiFATSKENEKKAKSLe 1686
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAA----EEEVDELKS---QLADYQQALDVQqtRAIQ---YQQAVQALERAKQL- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1687 ADLMQLQ----EDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSD--RVR 1760
Cdd:PRK04863 430 CGLPDLTadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRlrEQR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1761 KATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEgavkaKLKSTVAALEAKIAQLEEQVEqEAREKQAA 1840
Cdd:PRK04863 510 HLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDED-----ELEQLQEELEARLESLSESVS-EARERRMA 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1841 TKslkqkdKKLKEVLLQVEDERKMAEQYKEqaekGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGRE 1920
Cdd:PRK04863 584 LR------QQLEQLQARIQRLAARAPAWLA----AQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAAR 653
|
410
....*....|
gi 241982718 1921 VNALKSKLRR 1930
Cdd:PRK04863 654 KQALDEEIER 663
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1665-1928 |
5.67e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1665 RASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERAR-----KQADLEKEELAEELASSLSGRNTLQDEKRRLEARIA 1739
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemdRQAAIYAEQERMAMERERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1740 QLEEELEeeqgnMEAMSDrVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAKLKSTVAAL 1819
Cdd:pfam17380 367 QEEIAME-----ISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1820 EAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEK---------------GNTKVKQLKR 1884
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilekeleerkqamieEERKRKLLEK 520
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 241982718 1885 QLEE-----AEEESQRINANRRKLQRELDEATESNEAMgREVNALKSKL 1928
Cdd:pfam17380 521 EMEErqkaiYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1318-1785 |
6.41e-05 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 48.12 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1318 QDTQELLQEETRQKLNVSTKLR------------QLEDERnsLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFAS 1385
Cdd:PTZ00108 900 EDYKEFLESETLKEKDVIVDYRdystantvhftvKLNDGV--LEQWEEEGIEKVFKLKSTISTTNMVLFDENGKIKKYSD 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1386 TIEVMEE-GKKRLQkemeglsqqyeekaaAYdklEKTKNRLQQELDDLVVDLDNQRQLV-----SNLEKKQKKFDQLLAE 1459
Cdd:PTZ00108 978 ALDILKEfYLVRLD---------------LY---KKRKEYLLGKLERELARLSNKVRFIkhvinGELVITNAKKKDLVKE 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1460 -EKNISSKYADERDRAEAE--AREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLvsSKDDVGKNVHELEKSKRA 1536
Cdd:PTZ00108 1040 lKKLGYVRFKDIIKKKSEKitAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSL--TKEKVEKLNAELEKKEKE 1117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1537 LE----TQMEEM-KTQLEELEDELQATE--DAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDER 1609
Cdd:PTZ00108 1118 LEklknTTPKDMwLEDLDKFEEALEEQEevEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGN 1197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1610 KQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKlqAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADL 1689
Cdd:PTZ00108 1198 SKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKK--SSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAP 1275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1690 MQLQEDLAAAERARKQADlekeelAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQL 1769
Cdd:PTZ00108 1276 KRVSAVQYSPPPPSKRPD------GESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQS 1349
|
490
....*....|....*.
gi 241982718 1770 SNELATERSTAQKNES 1785
Cdd:PTZ00108 1350 SRLLRRPRKKKSDSSS 1365
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
872-1142 |
6.83e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 872 ETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQ 951
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 952 MLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEErvsdlTTNLAEEEEKAKNLTKLKSK 1031
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEK-----IKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1032 HESMISELEVRLKKEEKSRQELEKLKRKlegdASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALK 1111
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEE----AQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250 260 270
....*....|....*....|....*....|.
gi 241982718 1112 KIRELEGHISDLQEDLDSERAARNKAEKQKR 1142
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1096-1267 |
7.00e-05 |
|
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: 46.46 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1096 LARLDEEIAQKNnalKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTldstatqQELRAKREQE 1175
Cdd:COG1579 12 LQELDSELDRLE---HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-------EARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1176 VTVLKKALDEETRSHEAQVQEMRQKhtQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKK 1255
Cdd:COG1579 82 LGNVRNNKEYEALQKEIESLKRRIS--DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|..
gi 241982718 1256 KLEVQLQDLQSK 1267
Cdd:COG1579 160 ELEAEREELAAK 171
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1373-1905 |
7.62e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1373 LSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKK 1452
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1453 FDQLLAEEKNISSKYADERDRA------EAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKN 1526
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNnyykelEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1527 VHELEKSKraleTQMEEMKTQLEELE---DELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQlheyET 1603
Cdd:PRK01156 331 LSVLQKDY----NDYIKKKSRYDDLNnqiLELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ----EI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1604 ELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKdfqRELDDARASRDEIFATSKENEKKAK 1683
Cdd:PRK01156 403 DPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSV---CPVCGTTLGEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1684 SLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKAT 1763
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1764 LQAEQLSNE----LATERSTA--QKNESARQQLERQNKELRSKLQEVEGA---VKAKLKSTVAALEAKIAQLEEQVeQEA 1834
Cdd:PRK01156 560 LEDLDSKRTswlnALAVISLIdiETNRSRSNEIKKQLNDLESRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY-NEI 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1835 REKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEA------------------EEESQRI 1896
Cdd:PRK01156 639 QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlestieilrtriNELSDRI 718
|
....*....
gi 241982718 1897 NANRRKLQR 1905
Cdd:PRK01156 719 NDINETLES 727
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1763-1933 |
7.85e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 47.70 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1763 TLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQevegavKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATK 1842
Cdd:PTZ00491 645 TRDSLQKSVQLAIEITTKSQEAAARHQAELLEQEARGRLE------RQKMHDKAKAEEQRTKLLELQAESAAVESSGQSR 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1843 SlkQKDKKLKEVLLQVEDERKMAEqYKEQAEK--GNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEaTESN------ 1914
Cdd:PTZ00491 719 A--EALAEAEARLIEAEAEVEQAE-LRAKALRieAEAELEKLRKRQELELEYEQAQNELEIAKAKELAD-IEATkferiv 794
|
170
....*....|....*....
gi 241982718 1915 EAMGREvnALKSKLRRGNE 1933
Cdd:PTZ00491 795 EALGRE--TLIAIARAGPE 811
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
865-1109 |
7.88e-05 |
|
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: 47.76 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 865 KERQQKAETELKELEQKHTQLAE-----EKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQ 939
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 940 QLQA------ERKKMAQQ--------MLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLE 1005
Cdd:TIGR02169 837 ELQEqridlkEQIKSIEKeienlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1006 ERVSDLTTNLAEEEEKAKNLTKLKSKHESmISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQL 1085
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR 995
|
250 260
....*....|....*....|....
gi 241982718 1086 AKKEEELQAALARLDEEIAQKNNA 1109
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
910-1212 |
7.95e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 910 RVRLAAKKQELEEIlhemEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEK--VTAEAKIKKLE--- 984
Cdd:COG4913 609 RAKLAALEAELAEL----EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiAELEAELERLDass 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 985 DDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEksRQELEKLKRKLEGDA 1064
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1065 SdFHEQIADLQAQIAELKMQLAKKEEELQAALAR-----------LDEEIA-----------QKNNAL----KKIREL-- 1116
Cdd:COG4913 763 V-ERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadLDADLEslpeylalldrLEEDGLpeyeERFKELln 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1117 ---EGHISDLQEDLDSERAArnkAEKQKRDLGEELEALKTELEDTLdstatQQELRAKREQEVTVLKKALDEETRSHEAQ 1193
Cdd:COG4913 842 ensIEFVADLLSKLRRAIRE---IKERIDPLNDSLKRIPFGPGRYL-----RLEARPRPDPEVREFRQELRAVTSGASLF 913
|
330
....*....|....*....
gi 241982718 1194 VQEMRQKHTQAVEELTEQL 1212
Cdd:COG4913 914 DEELSEARFAALKRLIERL 932
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
869-1487 |
7.99e-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: 47.82 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 869 QKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKM 948
Cdd:pfam07111 63 QQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQREL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 949 AQQMLDLEEQLEEEEAARQKlQLEKVTAEAKikKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKL 1028
Cdd:pfam07111 143 EEIQRLHQEQLSSLTQAHEE-ALSSLTSKAE--GLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1029 KSKHESMISEL---EVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDeeiAQ 1105
Cdd:pfam07111 220 VESLRKYVGEQvppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSD---SL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1106 KNNALKKIRELeghISDLQEDLDSERAARNKAEKQKRDLGEELEalkteledtlDSTATQQELRAKREQEVTVLKKALDE 1185
Cdd:pfam07111 297 EPEFPKKCRSL---LNRWREKVFALMVQLKAQDLEHRDSVKQLR----------GQVAELQEQVTSQSQEQAILQRALQD 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1186 ETRshEAQVQEMRQKHTQAveELTEQLEQFKRAKANLDKSKQTLekenadlagelrvlgqakQEVEHKKKKLEVQLQDLQ 1265
Cdd:pfam07111 364 KAA--EVEVERMSAKGLQM--ELSRAQEARRRQQQQTASAEEQL------------------KFVVNAMSSTQIWLETTM 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1266 SKCSDGERARAELSDKVHKLQNEVESVTGMlneaegkaikLAKDVAsLGSQLQDTQELLQEETRQKLNVSTKLRQLEDER 1345
Cdd:pfam07111 422 TRVEQAVARIPSLSNRLSYAVRKVHTIKGL----------MARKVA-LAQLRQESCPPPPPAPPVDADLSLELEQLREER 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1346 NSLQDQLD--------------EEMEA-KQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEE 1410
Cdd:pfam07111 491 NRLDAELQlsahliqqevgrarEQGEAeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQ 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1411 KAAAY-----DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSkyadERDRAEAEAREKETKA 1485
Cdd:pfam07111 571 QQEIYgqalqEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQ----ELRRLQDEARKEEGQR 646
|
..
gi 241982718 1486 LS 1487
Cdd:pfam07111 647 LA 648
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1071-1228 |
7.99e-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: 47.03 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1071 IADLQAQIAELKMQLAKkeeeLQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEA 1150
Cdd:pfam00529 53 PTDYQAALDSAEAQLAK----AQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1151 LKTELEDTL---DSTATQQELRAKREQEVTVLKKALD----EETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLD 1223
Cdd:pfam00529 129 RRVLAPIGGisrESLVTAGALVAQAQANLLATVAQLDqiyvQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
....*
gi 241982718 1224 KSKQT 1228
Cdd:pfam00529 209 RTEIR 213
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1081-1286 |
8.92e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1081 LKMQLAKKEEelqaALARLDEEIAQKNNALKkireLE-GHISDLQEDLDSERAARNKAEkqkrdlgeeleALKTELEDTL 1159
Cdd:PRK09039 44 LSREISGKDS----ALDRLNSQIAELADLLS----LErQGNQDLQDSVANLRASLSAAE-----------AERSRLQALL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1160 DSTATQQELRAKREQEvtvLKKALDEE-TRSHEAQVQemrqkhtqaVEELTEQLEQFKRakanldkskqtlekenadlag 1238
Cdd:PRK09039 105 AELAGAGAAAEGRAGE---LAQELDSEkQVSARALAQ---------VELLNQQIAALRR--------------------- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 241982718 1239 ELRVLGQAKQEVEHKKKKLEVQLQDLqskcsdGERARAELSDKVHKLQ 1286
Cdd:PRK09039 152 QLAALEAALDASEKRDRESQAKIADL------GRRLNVALAQRVQELN 193
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
657-681 |
9.25e-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: 45.03 E-value: 9.25e-05
10 20
....*....|....*....|....*
gi 241982718 657 YKEQLGKLMTTLRNTTPNFVRCIIP 681
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1528-1912 |
9.50e-05 |
|
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: 47.64 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1528 HELEKSKRALETQmeemKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQneEKRRQLQRQLHEYETELED 1607
Cdd:COG3096 292 RELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQ--EKIERYQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1608 ERKQRALAAAAKKKLEGDLKDLELQADSaikgreeaikqlrkLQAQMKDFQRELDdarasrdeifatskENEKKAkslea 1687
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDS--------------LKSQLADYQQALD--------------VQQTRA----- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1688 dlMQLQEDLAAAERARKQADLekeelaeelaSSLSGRNtLQDEKRRLEARIAQLEEELEEEQGNMeAMSDRVRKATLQAE 1767
Cdd:COG3096 413 --IQYQQAVQALEKARALCGL----------PDLTPEN-AEDYLAAFRAKEQQATEEVLELEQKL-SVADAARRQFEKAY 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1768 QLSNELATERSTAQKNESARQQLeRQNKELRSKLQEVEgavkaklkstvaALEAKIAQLEeqveQEAREKQAATKSLKQK 1847
Cdd:COG3096 479 ELVCKIAGEVERSQAWQTARELL-RRYRSQQALAQRLQ------------QLRAQLAELE----QRLRQQQNAERLLEEF 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 1848 DKKLKEVLlqveDERKMAEQYKEQAEKgntkvkqlkrQLEEAEEESQRINANRRKLQRELDEATE 1912
Cdd:COG3096 542 CQRIGQQL----DAAEELEELLAELEA----------QLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1405-1934 |
1.20e-04 |
|
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: 47.27 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1405 SQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEaEAREKETK 1484
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1485 ALSLARALEEALEAKEELERTNKmlKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLR 1564
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQE--RINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1565 LEVNMQALKGQFERDLQARDEQNEEK--RRQLQRQLHEYE--------TELEDERKQRALAAAAKKKLEGDLKDLELQAD 1634
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATsiREISCQQHTLTQhihtlqqqKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1635 SAIKGREEAIKQLRKLQAQMKDFQR--------ELDDARASRDEIFATSKENEKKAKSLEaDLMQLQEDLAAAERARKQA 1706
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAaaitctaqCEKLEKIHLQESAQSLKEREQQLQTKE-QIHLQETRKKAVVLARLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1707 DLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESA 1786
Cdd:TIGR00618 499 LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1787 RQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDE----- 1861
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLtltqe 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1862 ---------RKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGN 1932
Cdd:TIGR00618 659 rvrehalsiRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
..
gi 241982718 1933 EA 1934
Cdd:TIGR00618 739 DA 740
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1141-1310 |
1.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1141 KRDLGEELEALKTELEDTLDstATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKA 1220
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1221 NLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSdgERARAELSDKV-HKLQNEVES-VTGMLNE 1298
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA--EEAKEILLEKVeEEARHEAAVlIKEIEEE 181
|
170
....*....|..
gi 241982718 1299 AEGKAIKLAKDV 1310
Cdd:PRK12704 182 AKEEADKKAKEI 193
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
937-1407 |
1.54e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 937 RGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLA 1016
Cdd:pfam10174 339 RAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1017 EEEEKAKNLTKLKSKHESMISELEVRLKKEEKSrqeLEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQaal 1096
Cdd:pfam10174 419 GLKERVKSLQTDSSNTDTALTTLEEALSEKERI---IERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT--- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1097 arldeeiaqknnalkkirELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTEledtldSTATQQELRAKREQEV 1176
Cdd:pfam10174 493 ------------------EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE------CSKLENQLKKAHNAEE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1177 TVLKKA-LDEETRSHEAQVQEMRQKHTQA---VEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEH 1252
Cdd:pfam10174 549 AVRTNPeINDRIRLLEQEVARYKEESGKAqaeVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQ 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1253 KKKKLEVQLQDlqskcsDGERARAELSDKVHKLQnevesvtgmLNEAEGKAIKLAKDVASLGSQLQDTQELLQEetrqkl 1332
Cdd:pfam10174 629 EMKKKGAQLLE------EARRREDNLADNSQQLQ---------LEELMGALEKTRQELDATKARLSSTQQSLAE------ 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1333 nvstKLRQLEDERNSLQDQLDEEMEAKQNL------ERHVSTLNIQLSDSKKKlqdfASTIEVMEegkkrLQKEMEGLSQ 1406
Cdd:pfam10174 688 ----KDGHLTNLRAERRKQLEEILEMKQEAllaaisEKDANIALLELSSSKKK----KTQEEVMA-----LKREKDRLVH 754
|
.
gi 241982718 1407 Q 1407
Cdd:pfam10174 755 Q 755
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
869-1105 |
1.60e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 869 QKAETELKELEQKHTQLAEEKTLLQEQLQaetELYAeaeemrvrLAAKKQELEEilhemearleeeedrgqqLQAERKKM 948
Cdd:COG0497 168 RALKKELEELRADEAERARELDLLRFQLE---ELEA--------AALQPGEEEE------------------LEEERRRL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 949 AQqmldLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEE---RVSDLTTN----------- 1014
Cdd:COG0497 219 SN----AEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESaliELEEAASElrryldslefd 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1015 ---LAEEEEKAKNLTKLKSKHESMISELevrLKKEEKSRQELEKLkrklegdaSDFHEQIADLQAQIAELKMQLAKKEEE 1091
Cdd:COG0497 295 perLEEVEERLALLRRLARKYGVTVEEL---LAYAEELRAELAEL--------ENSDERLEELEAELAEAEAELLEAAEK 363
|
250
....*....|....*...
gi 241982718 1092 L----QAALARLDEEIAQ 1105
Cdd:COG0497 364 LsaarKKAAKKLEKAVTA 381
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1131-1490 |
1.65e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1131 RAARnkaEKQkrdlgeeLEALKTELedtlDSTATQQELRAKREQEVTVLKKALDEETRSH---------EAQVQEMRQKH 1201
Cdd:PRK04863 781 RAAR---EKR-------IEQLRAER----EELAERYATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRR 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1202 TQAVEELTEQLEQFKRAKANLDKSKQ------------------TLEKENADLAGELRVLGQAKQEVEHKKK---KLEVQ 1260
Cdd:PRK04863 847 VELERALADHESQEQQQRSQLEQAKEglsalnrllprlnlladeTLADRVEEIREQLDEAEEAKRFVQQHGNalaQLEPI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1261 LQDLQSKCSDGERaraelsdkvhkLQNEVESVTGMLNEAEGKAIKLaKDVASLGSQL--QDTQELLQEETRQKLNVSTKL 1338
Cdd:PRK04863 927 VSVLQSDPEQFEQ-----------LKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHFsyEDAAEMLAKNSDLNEKLRQRL 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1339 RQLEDERnslqDQLDEEMEAKQNlerhvstlniQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAydkl 1418
Cdd:PRK04863 995 EQAEQER----TRAREQLRQAQA----------QLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEE---- 1056
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 1419 ektknRLQQELDDLVVDLDNQRQLVSNLEKKQKKF----DQLLAEEKNISSKYADERDRAEAeAREKETKALSLAR 1490
Cdd:PRK04863 1057 -----RARARRDELHARLSANRSRRNQLEKQLTFCeaemDNLTKKLRKLERDYHEMREQVVN-AKAGWCAVLRLVK 1126
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1105-1331 |
1.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1105 QKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtldstATQQELrAKREQEVTVLKKALD 1184
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID------KLQAEI-AEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1185 EETRSheAQVQEMRQKHTQAV---EELTEQLEQFkrakanldkskQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQL 1261
Cdd:COG3883 90 ERARA--LYRSGGSVSYLDVLlgsESFSDFLDRL-----------SALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1262 QDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQK 1331
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1520-1706 |
1.76e-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: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1520 KDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAtedakLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLH 1599
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEE-AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1600 EYETELEDERKQRALAAAAKKKLEGD--LKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARAS-RDEIFATSK 1676
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILA 316
|
170 180 190
....*....|....*....|....*....|
gi 241982718 1677 ENEKKAKSLEADLMQLQEDLAAAERARKQA 1706
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1800-1929 |
1.85e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1800 KLQEVEGAVkAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNT-- 1877
Cdd:COG1579 11 DLQELDSEL-DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnk 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1878 -------KVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLR 1929
Cdd:COG1579 90 eyealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
997-1678 |
2.42e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 997 LSKERKLLEErvSDLT-TNLAEEEEKAKnlTKLKSKHESMIsELEVRLKKEEKSRQELEK---LKRKLEG--DASDFHEQ 1070
Cdd:COG3096 422 LEKARALCGL--PDLTpENAEDYLAAFR--AKEQQATEEVL-ELEQKLSVADAARRQFEKayeLVCKIAGevERSQAWQT 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1071 IADLQAQIAELKMQlAKKEEELQAALARLDEEIAQKNNAlkkIRELEGHISDLQEDLDSERaarnkaekqkrDLGEELEA 1150
Cdd:COG3096 497 ARELLRRYRSQQAL-AQRLQQLRAQLAELEQRLRQQQNA---ERLLEEFCQRIGQQLDAAE-----------ELEELLAE 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1151 LKTELEDTLDSTATQQELRAKREQEvtvlkkaLDEetrsHEAQVQEMRQK----HT--QAVEELTEQL-EQFKRAKANLD 1223
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQ-------LEQ----LRARIKELAARapawLAaqDALERLREQSgEALADSQEVTA 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1224 KSKQTLEKEnadlagelRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVH-KLQNEV-ESVTgmLNEA-- 1299
Cdd:COG3096 631 AMQQLLERE--------REATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGgVLLSEIyDDVT--LEDApy 700
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1300 -----------------EGKAIKLAK-------------DVASLGSQLQDTQEL-----LQEETRQkLNVST-------- 1336
Cdd:COG3096 701 fsalygparhaivvpdlSAVKEQLAGledcpedlyliegDPDSFDDSVFDAEELedavvVKLSDRQ-WRYSRfpevplfg 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1337 ------KLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNiqlsdskkklQDFASTIEVMEEGKKrlQKEMEGLSQQYEE 1410
Cdd:COG3096 780 raarekRLEELRAERDELAEQYAKASFDVQKLQRLHQAFS----------QFVGGHLAVAFAPDP--EAELAALRQRRSE 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1411 KAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEkkqkkfdqLLAEEknisskyaDERDRAEaEAREKETKALSLAR 1490
Cdd:COG3096 848 LERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN--------LLADE--------TLADRLE-ELREELDAAQEAQA 910
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1491 ALEEALEAKeelertnkmlkAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAKLRL 1565
Cdd:COG3096 911 FIQQHGKAL-----------AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLL 979
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1566 EVN---MQALKGQFERDLQARDEQNEeKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGR-- 1640
Cdd:COG3096 980 GENsdlNEKLRARLEQAEEARREARE-QLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERar 1058
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1641 -------------------------------EEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKEN 1678
Cdd:COG3096 1059 irrdelheelsqnrsrrsqlekqltrceaemDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDN 1127
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1260-1482 |
2.59e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.84 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1260 QLQDLQSKCSDGERAraelsdkVHKLQNEVESVTGMLNEAEgkaiklaKDVASLGSQLQDTQELLQEETRQKLNVSTKLR 1339
Cdd:PRK11637 48 QLKSIQQDIAAKEKS-------VRQQQQQRASLLAQLKKQE-------EAISQASRKLRETQNTLNQLNKQIDELNASIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1340 QLEDERNSLQD----QLD-----------------EEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEV---MEEGKK 1395
Cdd:PRK11637 114 KLEQQQAAQERllaaQLDaafrqgehtglqlilsgEESQRGERILAYFGYLNQARQETIAELKQTREELAAqkaELEEKQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1396 RLQKEMegLSQQYEEKAaaydKLEKTKNRLQQELDdlvvdldnqrQLVSNLEKKQKKFDQLLAEEKNISSKYAD-ERD-- 1472
Cdd:PRK11637 194 SQQKTL--LYEQQAQQQ----KLEQARNERKKTLT----------GLESSLQKDQQQLSELRANESRLRDSIARaEREak 257
|
250
....*....|.
gi 241982718 1473 -RAEAEAREKE 1482
Cdd:PRK11637 258 aRAEREAREAA 268
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1761-1934 |
2.63e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 46.05 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1761 KATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEgavKAKLKSTVAALEAKIAQLEEQVEQEAREKQAA 1840
Cdd:pfam15964 353 KALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKE---REELGATMLALSQNVAQLEAQVEKVTREKNSL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1841 TKSLKQKDKKLKEvllQVEDERKMAEQYKEQaekgntkVKQLKRQLEEAEEESQRInanRRKLQRELDEATESNEAMGRE 1920
Cdd:pfam15964 430 VSQLEEAQKQLAS---QEMDVTKVCGEMRYQ-------LNQTKMKKDEAEKEHREY---RTKTGRQLEIKDQEIEKLGLE 496
|
170
....*....|....
gi 241982718 1921 VNALKSKLRRGNEA 1934
Cdd:pfam15964 497 LSESKQRLEQAQQD 510
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1006-1273 |
2.82e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1006 ERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKmql 1085
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1086 aKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSER----------AARNKAEKQKRDLGEELEALKTEL 1155
Cdd:COG1340 78 -EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspEEEKELVEKIKELEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1156 EDTLDSTATQQELRAKREQ--EVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQT---LE 1230
Cdd:COG1340 157 EKNEKLKELRAELKELRKEaeEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEiieLQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 241982718 1231 KENADLAGELRVL--GQAKQEVEHKKKKLEVQLQDLQSKCSDGER 1273
Cdd:COG1340 237 KELRELRKELKKLrkKQRALKREKEKEELEEKAEEIFEKLKKGEK 281
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
862-1055 |
2.86e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQaetELYAEAE-EMRVRLAAKKQELEEILHE--MEARLEEEEDRG 938
Cdd:PRK00409 530 RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED---KLLEEAEkEAQQAIKEAKKEADEIIKElrQLQKGGYASVKA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 939 QQLQAERKKMAQQMLDLEEQLEEEEAARQKLqleKVTAEAKIKKLED--DILVMDDQNS--------KLSKERKLLEerv 1008
Cdd:PRK00409 607 HELIEARKRLNKANEKKEKKKKKQKEKQEEL---KVGDEVKYLSLGQkgEVLSIPDDKEaivqagimKMKVPLSDLE--- 680
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 241982718 1009 sdLTTNLAEEEEKAKNLTKLKSKHESMisELEVRLKKEEKSRQELEK 1055
Cdd:PRK00409 681 --KIQKPKKKKKKKPKTVKPKPRTVSL--ELDLRGMRYEEALERLDK 723
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
866-1352 |
2.89e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAETELKELEQKHTQ---LAEEKTLLQEQLQAETE-LYAEAEEMRVRLAAKKQELEEI------LHEMEARLEEEE 935
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQqldAAEELEELLAELEAQLEeLEEQAAEAVEQRSELRQQLEQLrarikeLAARAPAWLAAQ 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 936 DRGQQLQ-------AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLE------------------------ 984
Cdd:COG3096 609 DALERLReqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSqpggaedprllalaerlggvllse 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 985 --DDI------------------LVMDDqnskLSKERKLLEERvSDLTTNL----------------AEEEEKA------ 1022
Cdd:COG3096 689 iyDDVtledapyfsalygparhaIVVPD----LSAVKEQLAGL-EDCPEDLyliegdpdsfddsvfdAEELEDAvvvkls 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1023 ---------------------KNLTKLKSKHEsmisELEVRLKKEEKSRQELEklkrKLEGDASDF---HEQIA---DLQ 1075
Cdd:COG3096 764 drqwrysrfpevplfgraareKRLEELRAERD----ELAEQYAKASFDVQKLQ----RLHQAFSQFvggHLAVAfapDPE 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1076 AQIAELKMQLAKKEEEL---QAALARLDEEIAQKNNALKKIRELEGHIS-----DLQEDLDSERAARNKAEKQKRDL--- 1144
Cdd:COG3096 836 AELAALRQRRSELERELaqhRAQEQQLRQQLDQLKEQLQLLNKLLPQANlladeTLADRLEELREELDAAQEAQAFIqqh 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1145 GEELEALKTELeDTLDSTATQQElrakreqevtvlkkALDEETRSHEAQVQEMRQKhTQAVEELTEQLEQFkrakaNLDK 1224
Cdd:COG3096 916 GKALAQLEPLV-AVLQSDPEQFE--------------QLQADYLQAKEQQRRLKQQ-IFALSEVVQRRPHF-----SYED 974
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1225 SKQTLEkENADLAGELRvlgQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELsDKVHKLQNEvesvtgMLNEAEgkai 1304
Cdd:COG3096 975 AVGLLG-ENSDLNEKLR---ARLEQAEEARREAREQLRQAQAQYSQYNQVLASL-KSSRDAKQQ------TLQELE---- 1039
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 241982718 1305 klaKDVASLGSQLQDTQELLQEETRQKLNvsTKLRQLEDERNSLQDQL 1352
Cdd:COG3096 1040 ---QELEELGVQADAEAEERARIRRDELH--EELSQNRSRRSQLEKQL 1082
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1378-1807 |
3.07e-04 |
|
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: 45.88 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1378 KKLQDFASTIEVMEEGKKRLQKE--MEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnQRQLVSNLEKKQKKFDq 1455
Cdd:pfam17380 221 KEVQGMPHTLAPYEKMERRKESFnlAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIV-----QHQKAVSERQQQEKFE- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1456 llaeeknissKYADERDRAEAEAREKEtkaLSLARALEEALEAKEELERTNKMLKAEMEDLVsskddvgknvheLEKSKR 1535
Cdd:pfam17380 295 ----------KMEQERLRQEKEEKARE---VERRRKLEEAEKARQAEMDRQAAIYAEQERMA------------MERERE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1536 ALETQMEEMKTQLEELEDELQATEDAKLRlevnmqalkgQFERdLQARDEQNEEKRRQlqrqlheyetELEDERKQRALA 1615
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEISRMR----------ELER-LQMERQQKNERVRQ----------ELEAARKVKILE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1616 AAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFaTSKENEKKAKSLEADLMQLQED 1695
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRDRK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1696 LAAAER---------ARKQADLEKEELAEELASSLSGR-NTLQDEKRRleaRIAQLEEELEEEQGNMEAMSDRVRKATlq 1765
Cdd:pfam17380 488 RAEEQRrkilekeleERKQAMIEEERKRKLLEKEMEERqKAIYEEERR---REAEEERRKQQEMEERRRIQEQMRKAT-- 562
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 241982718 1766 aeqlsnelaTERSTAQKNESARQQLeRQNKELRSKLQEVEGA 1807
Cdd:pfam17380 563 ---------EERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1059-1213 |
3.08e-04 |
|
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: 43.41 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1059 KLEGDASDFHEQIADLQAQIAELKMQLAKK-EEELQAALARLDEEIAQKNNALKKIRE-----LEGHISDLQEDLDSE-R 1131
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRlEKETEALRERLQKDLEEVRAKLEPYLEelqakLGQNVEELRQRLEPYtE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1132 AARNKAEKQKRDLGEELEALKTELEDTLDSTATQ---------QELRAKREQEVTVLKKALDEETRSHEAQ----VQEMR 1198
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDAlrarlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQELR 160
|
170
....*....|....*
gi 241982718 1199 QKHTQAVEELTEQLE 1213
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1025-1434 |
3.10e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1025 LTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEgdasdfheqiaDLQAQIAELKMQLAKKEEELQAALARLDEEIA 1104
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYR-----------ELRKSLLANRFSFGPALDELEKQLENLEEEFS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1105 QKNN---------ALKKIRELEGHISDLQEDLDseraarnkaekqkrDLGEELEALKTELEDTLdstatqQELRAKREQe 1175
Cdd:PRK04778 183 QFVEltesgdyveAREILDQLEEELAALEQIME--------------EIPELLKELQTELPDQL------QELKAGYRE- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1176 vtVLKKALDEETRSHEAQVQEMRQKHTQAVEELtEQLEqFKRAKANLDKSKQTLEKENADLAGELrvlgQAKQEVEHKKK 1255
Cdd:PRK04778 242 --LVEEGYHLDHLDIEKEIQDLKEQIDENLALL-EELD-LDEAEEKNEEIQERIDQLYDILEREV----KARKYVEKNSD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1256 KLEVQLQdlqskcsdgeraraELSDKVHKLQNEVESV--TGMLNEAEGKAIK-LAKDVASLGSQLQDTQELLQE------ 1326
Cdd:PRK04778 314 TLPDFLE--------------HAKEQNKELKEEIDRVkqSYTLNESELESVRqLEKQLESLEKQYDEITERIAEqeiays 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1327 ETRQKLN-VSTKLRQLEDE----RNSLQDQLDEEMEAKQNLERHVStlniQLSDSKKKL---------QDFASTIEVMEE 1392
Cdd:PRK04778 380 ELQEELEeILKQLEEIEKEqeklSEMLQGLRKDELEAREKLERYRN----KLHEIKRYLeksnlpglpEDYLEMFFEVSD 455
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 241982718 1393 GKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVV 1434
Cdd:PRK04778 456 EIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVE 497
|
|
| ASY3-like |
pfam20435 |
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific ... |
1008-1113 |
3.18e-04 |
|
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific proteins, such as AtASY3 from Arabidopsis and PAIR3 from rice. They are coiled-coil domain proteins required for normal meiosis. PAIR3 is an axial element and part of the synaptonemal complex (SC) that forms between homologous chromosomes during meiosis. Members of this family are homologs of SCYP2 from vertebrates and fungal Red1/Rec10.
Pssm-ID: 466584 [Multi-domain] Cd Length: 793 Bit Score: 45.65 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1008 VSDLTTNLAEEEEKAKNLTKLKSKHEsmiselEVRLK-KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLA 1086
Cdd:pfam20435 667 LENIKSHIITEAGKTSNLAKTKRKHA------ETRLQeQEEKMRMIHEKFKDDVSHHLEDFKSTIEELEANQSELKGSIK 740
|
90 100
....*....|....*....|....*...
gi 241982718 1087 KKEEELQAALARLDEEIAQK-NNALKKI 1113
Cdd:pfam20435 741 KQRTSHQKLIAHFEGGIETKlDDATKRI 768
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1788-1929 |
3.19e-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: 44.53 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1788 QQLERQNKELRSKLQEVEGAVKAkLKSTVAALEAKIAQLEEQVEQ---EAREKQAATKSLKQKDKKLKEVLLQVEDERKM 1864
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-LEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1865 A------EQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLR 1929
Cdd:COG1579 92 EalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1527-1924 |
3.33e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.40 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1527 VHELEKSKRAletqMEEMKTQLEELE-DELQATED---AKLRLEvNMQalKGQFERDLQARDEQNEEKRRQLQRQLHEYE 1602
Cdd:pfam05701 69 LEELESTKRL----IEELKLNLERAQtEEAQAKQDselAKLRVE-EME--QGIADEASVAAKAQLEVAKARHAAAVAELK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1603 T---ELEDERKQRAlaaaakkklegdlkDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENE 1679
Cdd:pfam05701 142 SvkeELESLRKEYA--------------SLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1680 KK----AKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAM 1755
Cdd:pfam05701 208 EHrigaALAREQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1756 SDRVRKATLQAEqlsNELATERSTAQKNESARQQLERQNKELRSKLQEvEGAVKAKLKSTVAALEAKIAQLEEQVEQEAR 1835
Cdd:pfam05701 288 STSIQAALASAK---KELEEVKANIEKAKDEVNCLRVAAASLRSELEK-EKAELASLRQREGMASIAVSSLEAELNRTKS 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1836 EKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNE 1915
Cdd:pfam05701 364 EIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEK 443
|
....*....
gi 241982718 1916 AMGREVNAL 1924
Cdd:pfam05701 444 LALAAIKAL 452
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1545-1841 |
4.28e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1545 KTQLEELEDELQATEDAKLRLEVNMQALkgqfERDLQARdeqnEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEG 1624
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFEARQARL----EREKAAR----EARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1625 DLKDLELQADSAIKGREEAikqlRKLQAQmkdfqrelddARASRDEifATSKENEKKAKsleadlmqlqedLAAAeRARK 1704
Cdd:PRK05035 507 VIKAGARPDNSAVIAAREA----RKAQAR----------ARQAEKQ--AAAAADPKKAA------------VAAA-IARA 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1705 QADLEKEELaeelaSSLSGRNTLQDEKRRLEARIAQLEEeleeeqgnmeamsdrvRKATLQAEQLSNELATERSTAQKNE 1784
Cdd:PRK05035 558 KAKKAAQQA-----ANAEAEEEVDPKKAAVAAAIARAKA----------------KKAAQQAASAEPEEQVAEVDPKKAA 616
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1785 ----SARQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQL---EEQVEQEAREKQAAT 1841
Cdd:PRK05035 617 vaaaIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQqqaNAEPEEAEDPKKAAV 680
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1727-1909 |
5.21e-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: 43.76 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1727 LQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNEsARQQLERQNKELRSKLQEVEg 1806
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-EQLGNVRNNKEYEALQKEIE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1807 avkaKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEvllqvederkmaeqykeqaekgntKVKQLKRQL 1886
Cdd:COG1579 100 ----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE------------------------KKAELDEEL 151
|
170 180
....*....|....*....|...
gi 241982718 1887 EEAEEESQRINANRRKLQRELDE 1909
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPP 174
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1058-1357 |
5.23e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.23 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1058 RKLEGDASDfheqIADLQAQIAELKMQLAKKEEE--------LQAALARLDEEIAQK-NNALKKIreleghisDLQEDLD 1128
Cdd:PLN03229 422 KKREAVKTP----VRELEGEVEKLKEQILKAKESsskpselaLNEMIEKLKKEIDLEyTEAVIAM--------GLQERLE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1129 SERAARNKAEKQK----RDLGEELEALKTELEDTLDSTATQQELRAKRE--QEVTVLKKALDEETRSHEAQvQEMRQKHT 1202
Cdd:PLN03229 490 NLREEFSKANSQDqlmhPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKKFK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1203 QAVE--ELTEQLEQFKRAKAN--------LDKS-KQTLEKEN----ADLAGELRVLGQAKQEVEHKKKKLEVQL--QDLQ 1265
Cdd:PLN03229 569 EVMDrpEIKEKMEALKAEVASsgassgdeLDDDlKEKVEKMKkeieLELAGVLKSMGLEVIGVTKKNKDTAEQTppPNLQ 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1266 SKCsdgERARAELSDKVHKLQNevesVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDER 1345
Cdd:PLN03229 649 EKI---ESLNEEINKKIERVIR----SSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKF 721
|
330
....*....|..
gi 241982718 1346 NSLQDQLDEEME 1357
Cdd:PLN03229 722 EELEAELAAARE 733
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1201-1595 |
5.33e-04 |
|
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: 45.11 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1201 HTQAVEELTEQL-EQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCsDGERARAELS 1279
Cdd:pfam17380 228 HTLAPYEKMERRkESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM-EQERLRQEKE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1280 DKVHKL-------------QNEVESVTGMLNEAEGKAIKLAKDVA--SLGSQLQDTQELLQEETRQKLNVSTKLRQLEDE 1344
Cdd:pfam17380 307 EKAREVerrrkleeaekarQAEMDRQAAIYAEQERMAMERERELEriRQEERKRELERIRQEEIAMEISRMRELERLQME 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1345 RNSLQDQLDEEMEAKQNLErhvstlnIQLSDSKKKLQDFASTIE-VMEEGKKRLQKEMEGLSqqyEEKAAAYDKLEKTKN 1423
Cdd:pfam17380 387 RQQKNERVRQELEAARKVK-------ILEEERQRKIQQQKVEMEqIRAEQEEARQREVRRLE---EERAREMERVRLEEQ 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1424 RLQQELDDLVVDLDNQRQlvSNLEKKQKKFDQLLAEEKNisskyadeRDRAEAEAREKETKALslaraleealeakeELE 1503
Cdd:pfam17380 457 ERQQQVERLRQQEEERKR--KKLELEKEKRDRKRAEEQR--------RKILEKELEERKQAMI--------------EEE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1504 RTNKMLKAEMEDLvsskddvGKNVHELEKSKRAletqmEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQAR 1583
Cdd:pfam17380 513 RKRKLLEKEMEER-------QKAIYEEERRREA-----EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
410
....*....|..
gi 241982718 1584 DEQNEEKRRQLQ 1595
Cdd:pfam17380 581 IVESEKARAEYE 592
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1146-1885 |
5.41e-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: 45.20 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1146 EELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALdeetrsheaQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKS 1225
Cdd:pfam10174 130 KELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEML---------QSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1226 KQTLEKENADLAGELRVLGQAKQEVEhKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEvesvtGMLN-EAEGKAI 1304
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPA-KTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTN-----GLLHtEDREEEI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1305 KLAKDVASLGSQLQDTQELLQEETRQKlnvstklrqlEDERNSLQDQLDeemeakqnlerhvsTLNIQLSDSKKKLQDFA 1384
Cdd:pfam10174 275 KQMEVYKSHSKFMKNKIDQLKQELSKK----------ESELLALQTKLE--------------TLTNQNSDCKQHIEVLK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1385 STIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK----QKKFDQLLAEE 1460
Cdd:pfam10174 331 ESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKinvlQKKIENLQEQL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1461 KNISSKYADERDRAEAEAREKETKALSLaraleealeakeelertnkmlkAEMEDLVSSKDDVGKNV-HELEKSKRALET 1539
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTDTAL----------------------TTLEEALSEKERIIERLkEQREREDRERLE 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1540 QMEEMKTQLEELEDELQAtedaklrlevnmqalkgqferdlqardeqneekrrqLQRQLHEYETELEDERKQRALAAAAK 1619
Cdd:pfam10174 469 ELESLKKENKDLKEKVSA------------------------------------LQPELTEKESSLIDLKEHASSLASSG 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1620 KKLEGDLKDLELQADsaiKGREEAIkqlrKLQAQMKDFQRELDDARasrdeifaTSKENEKKAKSLEADLMQLQEdlaaa 1699
Cdd:pfam10174 513 LKKDSKLKSLEIAVE---QKKEECS----KLENQLKKAHNAEEAVR--------TNPEINDRIRLLEQEVARYKE----- 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1700 ERARKQADLEKEELAEELASSlsgRNTLQDEK-RRLEARIAQLEEELEEEQGNMEAMSDRVRKATlqAEQLsnELATERS 1778
Cdd:pfam10174 573 ESGKAQAEVERLLGILREVEN---EKNDKDKKiAELESLTLRQMKEQNKKVANIKHGQQEMKKKG--AQLL--EEARRRE 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1779 TAQKNESARQQLERQNKELRSKLQEVEgAVKAKLKSTVAALEAKIA-----------QLEEQVEQearEKQAATKSLKQK 1847
Cdd:pfam10174 646 DNLADNSQQLQLEELMGALEKTRQELD-ATKARLSSTQQSLAEKDGhltnlraerrkQLEEILEM---KQEALLAAISEK 721
|
730 740 750
....*....|....*....|....*....|....*...
gi 241982718 1848 DKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQ 1885
Cdd:pfam10174 722 DANIALLELSSSKKKKTQEEVMALKREKDRLVHQLKQQ 759
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1781-1929 |
5.60e-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: 43.76 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1781 QKNESARQQLERQNKELRSKLQEVEGAVKA------KLKSTVAALEAKIAQLEEQVEQ-EAREKQAATKSLKQKD-KKLK 1852
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAAlearleAAKTELEDLEKEIKRLELEIEEvEARIKKYEEQLGNVRNnKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1853 EVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLR 1929
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1089-1703 |
5.86e-04 |
|
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: 44.74 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1089 EEELQAALARLDEEIAQKnnaLKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQEL 1168
Cdd:pfam07111 54 ELEGSQALSQQAELISRQ---LQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1169 RAKREQEVtvlKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKqtlekenadlAGELRVLGQAKQ 1248
Cdd:pfam07111 131 RKNLEEGS---QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKR----------AGEAKQLAEAQK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1249 EVEHKKKKLEVQLQDLQSKCS----------------------DGERA------------RAELSDKVHKLQNEVESVTG 1294
Cdd:pfam07111 198 EAELLRKQLSKTQEELEAQVTlveslrkyvgeqvppevhsqtwELERQelldtmqhlqedRADLQATVELLQVRVQSLTH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1295 MLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQK---LNVSTKLRQLE--DERNSLQDQLDEemeakqnLERHVSTL 1369
Cdd:pfam07111 278 MLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKvfaLMVQLKAQDLEhrDSVKQLRGQVAE-------LQEQVTSQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1370 NIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMeglsqqyeekaaayDKLEKTKNRLQQELDDLVVDLdnqRQLVSNLEKK 1449
Cdd:pfam07111 351 SQEQAILQRALQDKAAEVEVERMSAKGLQMEL--------------SRAQEARRRQQQQTASAEEQL---KFVVNAMSST 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1450 QKKFDQLLAEEKNISSKYADERDRAEAEAREKETkalslaraleealeakeelertnkmlkaeMEDLVSSKDDVGKNVHE 1529
Cdd:pfam07111 414 QIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHT-----------------------------IKGLMARKVALAQLRQE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1530 LEKSKRALETQMEEMKTQLEELEDElqatedaKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEder 1609
Cdd:pfam07111 465 SCPPPPPAPPVDADLSLELEQLREE-------RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQ--- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1610 KQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLR---------------KLQAQMKDFQRELDDARASRDEIFAT 1674
Cdd:pfam07111 535 RAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygqalqekvaevetRLREQLSDTKRRLNEARREQAKAVVS 614
|
650 660 670
....*....|....*....|....*....|..
gi 241982718 1675 SKENEKKA---KSLEADLMQLQEDLAAAERAR 1703
Cdd:pfam07111 615 LRQIQHRAtqeKERNQELRRLQDEARKEEGQR 646
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1064-1277 |
5.88e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1064 ASDFHEQIADLQAQIAELK---MQLAKKEEELQAALARLDEEIAQknnALKKIRELEGHISDLQEDLDSERAARNKAEKQ 1140
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEksvRQQQQQRASLLAQLKKQEEAISQ---ASRKLRETQNTLNQLNKQIDELNASIAKLEQQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1141 K----RDLGEELEAL-----KTELEDTLDSTATQQE---------LRAKREQEVTVLKKaldeeTRSH-EAQVQEMRQKH 1201
Cdd:PRK11637 119 QaaqeRLLAAQLDAAfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQ-----TREElAAQKAELEEKQ 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 1202 TQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEvehkkkklEVQLQDLQSKCSDGERARAE 1277
Cdd:PRK11637 194 SQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRAN--------ESRLRDSIARAEREAKARAE 261
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
867-1065 |
6.05e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.56 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 867 RQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAE--------AEEMRVRlaakKQELEEilhEMEARLEEEEDRG 938
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREEleleqqrrFEEIRLR----KQRLEE---ERQRQEEEERKQR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 939 QQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDilvmddqnsKLSKERKLLEErvsdlttnLAEE 1018
Cdd:pfam15709 412 LQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEM---------QLAEEQKRLME--------MAEE 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 241982718 1019 EEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDAS 1065
Cdd:pfam15709 475 ERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
871-1109 |
6.18e-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: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 871 AETELKELEQKHTQLAEEKTLLQEQLQAeteLYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQ 950
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDA---LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 951 QMLDleeqleeeeAARQKLQLEKVTAEAKIKKLEDDIlvmdDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKS 1030
Cdd:COG3883 91 RARA---------LYRSGGSVSYLDVLLGSESFSDFL----DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982718 1031 KHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNA 1109
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1413-1640 |
6.38e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1413 AAYDKLEKTKNR-LQQELDDLVVDLDN-------QRQLVSNLEK--------KQKKFDQLLAEEKNISSKYADERDRAEA 1476
Cdd:PHA02562 166 SEMDKLNKDKIReLNQQIQTLDMKIDHiqqqiktYNKNIEEQRKkngeniarKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1477 EAREKETKALSLARALEEALEAKEELERTNKMLK---------AEMEDLVSSKDDVGK---NVHELEKSKRALETQMEEm 1544
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKikdKLKELQHSLEKLDTAIDE- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1545 ktqLEELEDELQATEDAKLRLEVNMQALKGQFER-DLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLE 1623
Cdd:PHA02562 325 ---LEEIMDEFNEQSKKLLELKNKISTNKQSLITlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
250
....*....|....*....
gi 241982718 1624 GDLKDL--ELQADSAIKGR 1640
Cdd:PHA02562 402 KYHRGIvtDLLKDSGIKAS 420
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1004-1157 |
6.47e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1004 LEERVSDLTTNLAEEEEKAKNLtklkskhESMISELEVRLKKEEKSRQELEKLKRKLEGdasdfheQIADLQAQIAELKM 1083
Cdd:PRK09039 58 LNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERSRLQALLAELAG-------AGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1084 QLAKKE---EELQAALARLDEEIAQknnalkkireLEGHISDLQEDLDSERAARNKAEKQKRDLGEELE-ALKTELED 1157
Cdd:PRK09039 124 ELDSEKqvsARALAQVELLNQQIAA----------LRRQLAALEAALDASEKRDRESQAKIADLGRRLNvALAQRVQE 191
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1765-1895 |
6.76e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1765 QAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSL 1844
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1845 KQ-KDKKLKEvllQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQR 1895
Cdd:TIGR02794 127 KQaAEAKAKA---EAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA 175
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
978-1158 |
6.83e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 978 AKIKKLEDDILVMDDQ----NSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKS---- 1049
Cdd:PHA02562 174 DKIRELNQQIQTLDMKidhiQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDiedp 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1050 -------RQELEKLKRKLE---GDASDFHE---------QIADLQAQIAELK---MQLAKKEEELQAALARLDEEIAQKN 1107
Cdd:PHA02562 254 saalnklNTAAAKIKSKIEqfqKVIKMYEKggvcptctqQISEGPDRITKIKdklKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1108 NALKKIRELEGHISDLQEDLDSER-------AARNKAEKQKRDLGEELEALKTELEDT 1158
Cdd:PHA02562 334 EQSKKLLELKNKISTNKQSLITLVdkakkvkAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1537-1888 |
7.34e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1537 LETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLqRQLHEYETELEDERKQRALAA 1616
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL-RQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1617 AAKKKLEGDLKDLELQADSAIKGREEAIKQLRKlqaQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDL 1696
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQ---RVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1697 AAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNME--AMSDR---------------- 1758
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQErlNASERkveglgeelssmaaqr 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1759 ------VRKATLQAEQLSNELAtERSTAQKNESARQQLERQNkelrsKLQEVEgavkaKLKSTVAALEAKIAQLEEQVEQ 1832
Cdd:pfam07888 268 drtqaeLHQARLQAAQLTLQLA-DASLALREGRARWAQERET-----LQQSAE-----ADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1833 EAREKQAATKSL-KQKDKKLKEV------LLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEE 1888
Cdd:pfam07888 337 ERMEREKLEVELgREKDCNRVQLsesrreLQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
940-1110 |
7.56e-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: 43.37 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 940 QLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQ--NSKLSKERKLLEERVSDLTTNLAE 1017
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1018 EEEKAKNLTKLKSKHESMISELEVRLKKEEKsrqELEKLKRKLEgdasdfhEQIADLQAQIAELKMQLAKKEEELQAALA 1097
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELD-------EELAELEAELEELEAEREELAAKIPPELL 177
|
170
....*....|...
gi 241982718 1098 RLDEEIAQKNNAL 1110
Cdd:COG1579 178 ALYERIRKRKNGL 190
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1196 |
7.67e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 967 QKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKlkskhesmisELEVRLKKE 1046
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE----------ELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1047 EKSRQELEKLKRKLE-GDASDFHEQIADLQaQIAELKMQLAKKEEELQAALARLDEEI-AQKNNALKKIRELEGHISDLQ 1124
Cdd:COG3883 96 YRSGGSVSYLDVLLGsESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1125 EDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQE 1196
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
866-1074 |
7.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAER 945
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 946 KKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDIlvmddqNSKLSKERKLLEERVSDLTTNLAEEEEKAKNL 1025
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADLDADLESLPEYLALL 821
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 241982718 1026 TKLKSKHesmISELEVRLK--KEEKSRQELEKLKRKLEGDASDFHEQIADL 1074
Cdd:COG4913 822 DRLEEDG---LPEYEERFKelLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
883-1261 |
8.94e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 883 TQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEE 962
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 963 EAARQKLQLEKVTAEAKIKKLEDDIlvmddqnsklskerKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVR 1042
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDI--------------KTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1043 LKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLA---KKEEELQAALARLDEEIAQKNNALKKIRELEGH 1119
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahRKEAENEALLEELRSLQERLNASERKVEGLGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1120 ISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQE-LRAKREQEVTVLKKaLDEETRSHEAQVQEMR 1198
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQEREtLQQSAEADKDRIEK-LSAELQRLEERLQEER 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1199 QKHTQAVEELTE-------QLEQFKRAKANLDKSKQTLEKENADLAGElrvlgqaKQEVEHKKKKLEVQL 1261
Cdd:pfam07888 339 MEREKLEVELGRekdcnrvQLSESRRELQELKASLRVAQKEKEQLQAE-------KQELLEYIRQLEQRL 401
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
960-1475 |
9.01e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 960 EEEEAARQKLQLEKVTAEAKIKKLEDDILVMDD---QNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMI 1036
Cdd:PRK01156 207 ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKII 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1037 SElevrlkKEEKSRQELEKLkRKLEGDASDFHEQIADLQAQIAELKmQLAKKEEELQAALARLDEEIAQKNNALKKIREL 1116
Cdd:PRK01156 287 ND------PVYKNRNYINDY-FKYKNDIENKKQILSNIDAEINKYH-AIIKKLSVLQKDYNDYIKKKSRYDDLNNQILEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1117 EGHISDLQEDLDSERAARNKAEKQKRdlgeELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQE 1196
Cdd:PRK01156 359 EGYEMDYNSYLKSIESLKKKIEEYSK----NIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1197 MRQkHTQAVEELTEQLEQFKRAKA-----NLDKSKQTLEKENADLAG---ELRVLGQAKQEVEHKKKKLEVQLQDLQSKc 1268
Cdd:PRK01156 435 LRE-NLDELSRNMEMLNGQSVCPVcgttlGEEKSNHIINHYNEKKSRleeKIREIEIEVKDIDEKIVDLKKRKEYLESE- 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1269 sDGERARAE---LSDKVHKLQNEVESVTgMLNEAEGKAIKLAKDVASLGSQLQD---TQELLQEETRQKLNVSTKLRQLE 1342
Cdd:PRK01156 513 -EINKSINEynkIESARADLEDIKIKIN-ELKDKHDKYEEIKNRYKSLKLEDLDskrTSWLNALAVISLIDIETNRSRSN 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1343 DERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEgKKRLQKEMEGLSQQYEEKAAAYDKLEKTK 1422
Cdd:PRK01156 591 EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQE-NKILIEKLRGKIDNYKKQIAEIDSIIPDL 669
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1423 NRLQQELDDLVVDLDNQRQLV----SNLEKKQKKFDQLLAEEKNISSKYADERDRAE 1475
Cdd:PRK01156 670 KEITSRINDIEDNLKKSRKALddakANRARLESTIEILRTRINELSDRINDINETLE 726
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
862-1218 |
9.38e-04 |
|
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: 43.98 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQlqAETELYAEAEEMrvrlaaKKQELEEILHEMEARLEEEEDRGQQL 941
Cdd:pfam09731 88 QVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPK--SEQEKEKALEEV------LKEAISKAESATAVAKEAKDDAIQAV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 QAERKKMAQQMLDLEEQLEEeeAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEK 1021
Cdd:pfam09731 160 KAHTDSLKEASDTAEISREK--ATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 AKNLTKLKSKHESMISELEVRLKKEEKSR--------QELEKL-KRKLEGDASDFHEQIADLQAQIAELKMQLAKK-EEE 1091
Cdd:pfam09731 238 AQSLAKLVDQYKELVASERIVFQQELVSIfpdiipvlKEDNLLsNDDLNSLIAHAHREIDQLSKKLAELKKREEKHiERA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1092 LQAALARLDEEIAQKNNALKKIRELEghISDLQEDLDSERAARNKAEKQKrdLGEELEALKTELEDTLDSTATQQELRAK 1171
Cdd:pfam09731 318 LEKQKEELDKLAEELSARLEEVRAAD--EAQLRLEFEREREEIRESYEEK--LRTELERQAEAHEEHLKDVLVEQEIELQ 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 241982718 1172 REQEvtvlkkaldeetRSHEAQVQEMRQKHTQAVEELTEQLEQFKRA 1218
Cdd:pfam09731 394 REFL------------QDIKEKVEEERAGRLLKLNELLANLKGLEKA 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
863-1023 |
9.49e-04 |
|
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: 43.60 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 863 KIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAE----------AEEMRVRLAAKK--------QELEEIL 924
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrQPPLALLLSPEDfldavrrlQYLKYLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 925 HEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLL 1004
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
170
....*....|....*....
gi 241982718 1005 EERVSDLTTNLAEEEEKAK 1023
Cdd:COG4942 226 EALIARLEAEAAAAAERTP 244
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1003-1184 |
1.00e-03 |
|
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: 41.87 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1003 LLEERVSDLTTNLAEEEEKAKNLTK-LKSKHESMISELEVRLkkeeksRQELEKLKRKLEGDASDFHEQIAD-------- 1073
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQeLVDRLEKETEALRERL------QKDLEEVRAKLEPYLEELQAKLGQnveelrqr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1074 LQAQIAELKMQLAKKEEELQAALARLDEEIAQKnnALKKIRELEGHISDLQEDLdseraaRNKAEKQKRDLGEELEALKT 1153
Cdd:pfam01442 75 LEPYTEELRKRLNADAEELQEKLAPYGEELRER--LEQNVDALRARLAPYAEEL------RQKLAERLEELKESLAPYAE 146
|
170 180 190
....*....|....*....|....*....|.
gi 241982718 1154 ELEDTLDSTAtqQELRAKREQEVTVLKKALD 1184
Cdd:pfam01442 147 EVQAQLSQRL--QELREKLEPQAEDLREKLD 175
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1063-1659 |
1.11e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1063 DASDFHEQIADLQAQIAELKMQLAKKEeelqaalarldeeiAQKNNALKKIRELEGHIsdlqedldseraarNKAEKQKR 1142
Cdd:PRK01156 184 NIDYLEEKLKSSNLELENIKKQIADDE--------------KSHSITLKEIERLSIEY--------------NNAMDDYN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1143 DLGEELEALKTELE--DTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKA 1220
Cdd:PRK01156 236 NLKSALNELSSLEDmkNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1221 NLDKSKQTLEkenaDLAGELRVLGQAKQEVEHKKKKLEvqlqDLQSKCSDGEraraELSDKVHKLQNEVESVTGMLNEAE 1300
Cdd:PRK01156 316 NIDAEINKYH----AIIKKLSVLQKDYNDYIKKKSRYD----DLNNQILELE----GYEMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1301 gkaiKLAKDVASLGSQLQDTQELLQEETRQKLN-VSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNiqlsdSKKK 1379
Cdd:PRK01156 384 ----KNIERMSAFISEILKIQEIDPDAIKKELNeINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN-----GQSV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1380 LQDFASTIEvmEEGKKRLQKEmeglsqqYEEKAAaydKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKkqKKFDQLLAE 1459
Cdd:PRK01156 455 CPVCGTTLG--EEKSNHIINH-------YNEKKS---RLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKSINE 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1460 EKNISSKYADERD--RAEAEAREKETKALSLARALEEALEAKEELERT--NKMLKA----EMEDLVSSKDDVGKNVHELE 1531
Cdd:PRK01156 521 YNKIESARADLEDikIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTswLNALAVisliDIETNRSRSNEIKKQLNDLE 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1532 KSKRALETQMEEMKT----QLEELEDELQATEDAKLRLEVN---MQALKGQFE--RDLQARDEQNEEKRRQLQRQLHEYE 1602
Cdd:PRK01156 601 SRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENkilIEKLRGKIDnyKKQIAEIDSIIPDLKEITSRINDIE 680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1603 TELEDERKQRALAAAAKKKLEGDLKDLEL---QADSAIKGREEAIKQLRKLQAQMKDFQR 1659
Cdd:PRK01156 681 DNLKKSRKALDDAKANRARLESTIEILRTrinELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
869-1055 |
1.11e-03 |
|
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: 42.60 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 869 QKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhemearleeeedrgQQLQAERKKM 948
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI--------------EEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 949 AQQMLDLEEQLEEeeaarQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEeekaknltkl 1028
Cdd:COG1579 79 EEQLGNVRNNKEY-----EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---------- 143
|
170 180
....*....|....*....|....*..
gi 241982718 1029 KSKHESMISELEVRLKKEEKSRQELEK 1055
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAA 170
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
866-1414 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEmrvrLAAKKQELEEILHEMEARLEEEEDRGQQLQAER 945
Cdd:COG3096 512 QRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 946 KKMAQQMLDLEEQLEEEEAARQKL-QLEKVTAEAkikkLEDDILVMDDQNSKLSKERKLLEERvSDLTTNLAEEEEKAKN 1024
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALeRLREQSGEA----LADSQEVTAAMQQLLEREREATVER-DELAARKQALESQIER 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1025 LTKLKSKHESMISELEVRLKKEEKSR--------------------------QELEKLKRKL-------------EGDAS 1065
Cdd:COG3096 663 LSQPGGAEDPRLLALAERLGGVLLSEiyddvtledapyfsalygparhaivvPDLSAVKEQLagledcpedlyliEGDPD 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1066 DFHEQIADLQ-------AQIAELKMQLA--------------KKEEELQAALARLDEEIAQKNNALKKIRELEGHISD-- 1122
Cdd:COG3096 743 SFDDSVFDAEeledavvVKLSDRQWRYSrfpevplfgraareKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfv 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1123 ---LQEDLDSERAARNKAEKQKRdlgEELEALKTELEDTLdsTATQQELRAKREQeVTVLKK------ALDEETrsheaq 1193
Cdd:COG3096 823 gghLAVAFAPDPEAELAALRQRR---SELERELAQHRAQE--QQLRQQLDQLKEQ-LQLLNKllpqanLLADET------ 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1194 vqemrqkHTQAVEELTEQLEQFKRAKANLDKSKQTLEKEnADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKC----- 1268
Cdd:COG3096 891 -------LADRLEELREELDAAQEAQAFIQQHGKALAQL-EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalse 962
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1269 ----------SDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDV-------ASLGSQLQDTQELLQEetrqk 1331
Cdd:COG3096 963 vvqrrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYsqynqvlASLKSSRDAKQQTLQE----- 1037
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1332 lnvstklrqLEDERNSLQDQLDEEMEAKQNLERhvSTLNIQLSDSKKKLQDFASTIEV----MEEGKKRLQKEMEGLSQQ 1407
Cdd:COG3096 1038 ---------LEQELEELGVQADAEAEERARIRR--DELHEELSQNRSRRSQLEKQLTRceaeMDSLQKRLRKAERDYKQE 1106
|
....*..
gi 241982718 1408 YEEKAAA 1414
Cdd:COG3096 1107 REQVVQA 1113
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
996-1129 |
1.31e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 996 KLSKERKLLEERVSDLTTNLAE-EEEKAKNLTKLKSKHESMISELEvrLKKEEKSRQELEKLKRKLEGD----ASDFHEQ 1070
Cdd:cd22656 125 DLLKEAKKYQDKAAKVVDKLTDfENQTEKDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLneeyAAKLKAK 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1071 IADLQAQIAELKMQLAkKEEELQAALARLDEEI----AQKNNALKKIRELEGHISDLQEDLDS 1129
Cdd:cd22656 203 IDELKALIADDEAKLA-AALRLIADLTAADTDLdnllALIGPAIPALEKLQGAWQAIATDLDS 264
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1018-1211 |
1.41e-03 |
|
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: 43.67 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1018 EEEKAKN--LTKLK---SKHESMISELEVRLKKEEKSRQELEKLKRKLEGdasdFHEQIADLQAQIAEL-----KMQLAK 1087
Cdd:pfam15066 311 EEDMALNevLQKLKhtnRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQV----FVDIINKLKENVEELiedkyNVILEK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1088 KE-----EELQAALA----RLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQ----------KRDLGEEL 1148
Cdd:pfam15066 387 NDinktlQNLQEILAntqkHLQESRKEKETLQLELKKIKVNYVHLQERYITEMQQKNKSVSQclemdktlskKEEEVERL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 1149 EALKTELEdtldsTATQQELRA-KREQEVTVLK-KALDEETRSHEAQVQEMRQKHTQAVEELTEQ 1211
Cdd:pfam15066 467 QQLKGELE-----KATTSALDLlKREKETREQEfLSLQEEFQKHEKENLEERQKLKSRLEKLVAQ 526
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1679-1947 |
1.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1679 EKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQgnmEAMSDR 1758
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1759 VRKATLQAEQLS--NELATERSTAQ--KNESARQQLERQNKELrskLQEVEgAVKAKLKSTVAALEAKIAQLEEQVEQEA 1834
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSESFSDflDRLSALSKIADADADL---LEELK-ADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1835 REKQAATKSLKQKDKKLKevllQVEDERKMAEQYKEQAEKgntKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESN 1914
Cdd:COG3883 168 AAKAELEAQQAEQEALLA----QLSAEEAAAEAQLAELEA---ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250 260 270
....*....|....*....|....*....|...
gi 241982718 1915 EAMGREVNALKSKLRRGNEASFVPSRRAGGRRV 1947
Cdd:COG3883 241 AAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1764-1905 |
1.50e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1764 LQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKaKLKSTVAALEAKIAQLEEQVEQEAREKqaatks 1843
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-ELEAELEEKDERIERLERELSEARSEE------ 457
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1844 lKQKDKKLKEVllqvederkmaeqykeqaEKGNTKVKQLKRQLEEAEEesqRINANRRKLQR 1905
Cdd:COG2433 458 -RREIRKDREI------------------SRLDREIERLERELEEERE---RIEELKRKLER 497
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1097-1427 |
1.56e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1097 ARLDEEIAQKNNALkkiRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLdstatqqelrakreQEV 1176
Cdd:pfam07888 34 NRLEECLQERAELL---QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSR--------------EKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1177 TVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEqfkrakanLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKK 1256
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRE--------LEEDIKTLTQRVLERETELERMKERAKKAGAQRKE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1257 LEVQLQDLQSK-----------CSDGERAR---AELSDKVHKLQNEVESVTGMLNEAEGKAIKLakdvASLGSQLQDTQE 1322
Cdd:pfam07888 169 EEAERKQLQAKlqqteeelrslSKEFQELRnslAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN----EALLEELRSLQE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1323 LLQEETRQKLNVSTKLRQLEDERNSLQDQLDE-EMEAKQnlerhvstLNIQLSDSKKKLQdfastievmeEGKKRLQKEM 1401
Cdd:pfam07888 245 RLNASERKVEGLGEELSSMAAQRDRTQAELHQaRLQAAQ--------LTLQLADASLALR----------EGRARWAQER 306
|
330 340
....*....|....*....|....*.
gi 241982718 1402 EGLSQQYEekaAAYDKLEKTKNRLQQ 1427
Cdd:pfam07888 307 ETLQQSAE---ADKDRIEKLSAELQR 329
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1336-1484 |
1.87e-03 |
|
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: 42.22 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1336 TKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQ---------KEMEGLSQ 1406
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1407 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDnqrQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETK 1484
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELA---ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
862-1168 |
2.18e-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: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQL 941
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 942 QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEK 1021
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1022 AKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHE-----------------QIADLQAQIAELKMQ 1084
Cdd:pfam07888 215 ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqaelhqarlQAAQLTLQLADASLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1085 L-------AKKEEELQAA-------LARLDEEIAQKNNALKKIR-ELEGHISDLQEDLDSERAARNKAEKQKRDLGEELE 1149
Cdd:pfam07888 295 LregrarwAQERETLQQSaeadkdrIEKLSAELQRLEERLQEERmEREKLEVELGREKDCNRVQLSESRRELQELKASLR 374
|
330
....*....|....*....
gi 241982718 1150 ALKTELEDTLdstATQQEL 1168
Cdd:pfam07888 375 VAQKEKEQLQ---AEKQEL 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
862-1048 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLLQEQLQA-----------ETELYAEAEEMRVRLAAKKQELEEILHEMEAR 930
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAAleaelaelekeIAELRAELEAQKEELAELLRALYRLGRQPPLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 931 LEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSD 1010
Cdd:COG4942 124 LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
|
170 180 190
....*....|....*....|....*....|....*...
gi 241982718 1011 LTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEK 1048
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
866-1138 |
2.37e-03 |
|
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: 42.36 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAETELKEleqkhtQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAER 945
Cdd:pfam19220 124 ERQLAAETEQNR------ALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 946 KKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIkkleddilvmDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNL 1025
Cdd:pfam19220 198 AELETQLDATRARLRALEGQLAAEQAERERAEAQL----------EEAVEAHRAERASLRMKLEALTARAAATEQLLAEA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1026 TKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQ---LAKKEEELQAALARLDEE 1102
Cdd:pfam19220 268 RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERaemLTKALAAKDAALERAEER 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 241982718 1103 IA---QKNNALKKIRE-----LEGHISDLQEDLDSERAARNKAE 1138
Cdd:pfam19220 348 IAslsDRIAELTKRFEveraaLEQANRRLKEELQRERAERALAQ 391
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1769-1925 |
2.52e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1769 LSNELAT-----ERSTAQKNESARQ-QLERQNKelrsklQEVEGAVkAKLKSTVAALEAKIAQLEEQVEQEAREKQAATK 1842
Cdd:PRK09039 44 LSREISGkdsalDRLNSQIAELADLlSLERQGN------QDLQDSV-ANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1843 SLKQKDKKLKEvllqvedERKMAEQYKEQAEKGNTKVKQLKRQL---EEAEEESQ-RINANRRKLQrelDEATESNEAMG 1918
Cdd:PRK09039 117 RAGELAQELDS-------EKQVSARALAQVELLNQQIAALRRQLaalEAALDASEkRDRESQAKIA---DLGRRLNVALA 186
|
....*..
gi 241982718 1919 REVNALK 1925
Cdd:PRK09039 187 QRVQELN 193
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1509-1656 |
2.65e-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: 42.71 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1509 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRL---EVNMQALKGQFE---RDLQA 1582
Cdd:pfam05667 340 LQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVE 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982718 1583 RDEQNEEKRRQL---QRQLHEYETELEDERKQRALAAAAkkklegdLKDLELQADSAIKGREEAIKQlrkLQAQMKD 1656
Cdd:pfam05667 420 LAGQWEKHRVPLieeYRALKEAKSNKEDESQRKLEEIKE-------LREKIKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1642-1842 |
2.69e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1642 EAIKQLRKLQAQMKDFQRELDDARASRDEIFATS-KENEkkakslEADLMQLQEDLAAAERARKQADLEKEELAEELASS 1720
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAAlQPGE------EEELEEERRRLSNAEKLREALQEALEALSGGEGGA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1721 LSgrnTLQDEKRRLEaRIAQleeeleeEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLE-RQN----- 1794
Cdd:COG0497 243 LD---LLGQALRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEeRLAllrrl 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1795 ---------------KELRSKLQEVEGAvkaklKSTVAALEAKIAQLEEQVEQEARE-----KQAATK 1842
Cdd:COG0497 312 arkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaarKKAAKK 374
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1278-1530 |
2.84e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1278 LSDKVHKLQNEVESVTGMLNEAEGKaIKLAKDvaslgsqLQDTQELLQEETRQKL-NVSTKLRQLEDERNSLQDQLDEEM 1356
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQ-IKTYNK-------NIEEQRKKNGENIARKqNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1357 EA----KQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKkrlqkEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDL 1432
Cdd:PHA02562 244 LNlvmdIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGG-----VCPTCTQQISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1433 VVDLDNQRQLVSNLEKKQKKFDQLLAEEKNIssKYADERDRAEAEAREKETKALSLARALEEALEakeelertnKMLKAE 1512
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKISTN--KQSLITLVDKAKKVKAAIEELQAEFVDNAEEL---------AKLQDE 387
|
250
....*....|....*...
gi 241982718 1513 MEDLVSSKDDVGKNVHEL 1530
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHR 405
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
862-1382 |
2.85e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELE--QKHTQLAEEKTLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLeeeedrgQ 939
Cdd:PRK10246 267 QQALAAEEKAQPQLAALSlaQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQS-------A 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 940 QLQAERKKMAQQMldleeqleeeeAARQKLQL---EKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEErVSDLTTNLA 1016
Cdd:PRK10246 340 ELQAQQQSLNTWL-----------AEHDRFRQwnnELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNA-LPAITLTLT 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1017 eEEEKAKNLTKLKSKHesmisELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAAL 1096
Cdd:PRK10246 408 -ADEVAAALAQHAEQR-----PLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1097 ARLDEEiaqknnalKKIRELEGHISDLQE---------------------DLDSERAARNKAEKQKRDLGEELEALKTEL 1155
Cdd:PRK10246 482 TICEQE--------ARIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLDALEKEVKKLGEEGAALRGQL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1156 eDTLDSTATQQELRAKR----EQEVTV------------------LKKALDEETRsHEAQVQEMRQKHT-QAveELTEQL 1212
Cdd:PRK10246 554 -DALTKQLQRDESEAQSlrqeEQALTQqwqavcaslnitlqpqddIQPWLDAQEE-HERQLRLLSQRHElQG--QIAAHN 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1213 EQFKRAKANLDKSKQTLEKENADLA-------GELRVLGQAKQEVEHKKKKlEVQLQDLQSKCsdgerarAELSDKVHKL 1285
Cdd:PRK10246 630 QQIIQYQQQIEQRQQQLLTALAGYAltlpqedEEASWLATRQQEAQSWQQR-QNELTALQNRI-------QQLTPLLETL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1286 QNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEET------RQKLNVSTKLRQLEDERNSLQDQLDEEMEA- 1358
Cdd:PRK10246 702 PQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAqrlqkaQAQFDTALQASVFDDQQAFLAALLDEETLTq 781
|
570 580
....*....|....*....|....*...
gi 241982718 1359 ----KQNLERHVSTLNIQLSDSKKKLQD 1382
Cdd:PRK10246 782 leqlKQNLENQRQQAQTLVTQTAQALAQ 809
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1795-1925 |
3.22e-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: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1795 KELRSKLQEVE---------GAVKAKL---KSTVAALEAKIAQL--------EEQVEQEAREKQAATKSLKQKDKKLKEV 1854
Cdd:COG2433 346 DAYKNKFERVEkkvppdvdrDEVKARVirgLSIEEALEELIEKElpeeepeaEREKEHEERELTEEEEEIRRLEEQVERL 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 1855 LLQVED-ERKMAEQyKEQAEKGNTKVKQLKRQLEEAEEESQRINANRRK---LQRELDEATESNEAMGREVNALK 1925
Cdd:COG2433 426 EAEVEElEAELEEK-DERIERLERELSEARSEERREIRKDREISRLDREierLERELEEERERIEELKRKLERLK 499
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1284-1647 |
3.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1284 KLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLE 1363
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1364 RHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLV 1443
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1444 SNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDV 1523
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1524 GKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYET 1603
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 241982718 1604 ELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQL 1647
Cdd:COG4372 327 KLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
980-1207 |
3.52e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 980 IKKLEDDILVMD-------DQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEvRLKKEEKSRQE 1052
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLE-KLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1053 LEK-LKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEElQAALARLDEEIAQKNNALkkiRELEGHISDLQEDLDSER 1131
Cdd:PLN02939 216 TEGlCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET-EERVFKLEKERSLLDASL---RELESKFIVAQEDVSKLS 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1132 AARNKAEKQKRD-LGEELEALKTELEDTLDSTATQQELRAKreqeVTVLKKALDEETRSHEA-QVQEMRQKHTQAVEE 1207
Cdd:PLN02939 292 PLQYDCWWEKVEnLQDLLDRATNQVEKAALVLDQNQDLRDK----VDKLEASLKEANVSKFSsYKVELLQQKLKLLEE 365
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
964-1105 |
4.18e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 964 AARQKLQLEKVTAEakIKKLEDDILVMDDQNSKLSKERKLL-EERVSDLTTNLAEEEEKaknltklkskhesmISELEVR 1042
Cdd:COG0542 399 AARVRMEIDSKPEE--LDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEE--------------LEALKAR 462
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1043 LKKEEKSRQELEKLKRKLEGDasdfHEQIADLQAQIAELKMQLAKKEEELQAALArlDEEIAQ 1105
Cdd:COG0542 463 WEAEKELIEEIQELKEELEQR----YGKIPELEKELAELEEELAELAPLLREEVT--EEDIAE 519
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
866-1095 |
4.36e-03 |
|
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: 42.03 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAETELKELE--QKHTQLAEEKT-LLQEQLQAETELYAEAEEMRVRlaaKKQELEEilhemearleeEEDRGQQlQ 942
Cdd:pfam17380 386 ERQQKNERVRQELEaaRKVKILEEERQrKIQQQKVEMEQIRAEQEEARQR---EVRRLEE-----------ERAREME-R 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 943 AERKKMAQQMLDLEEQLEEEEAARQKLQLEKvtaEAKIKKLEDDilvmddqnsklsKERKLLEERVSDLTTNLAEEEEKA 1022
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEK---EKRDRKRAEE------------QRRKILEKELEERKQAMIEEERKR 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1023 KNLTKLKSKHESMISELEVRLKKEEKSRQELE-KLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAA 1095
Cdd:pfam17380 516 KLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1820-1930 |
4.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1820 EAKIAQLEEQVEQEAREKQAATKSLKqkdkklKEVLLQVEDE--RKMAEQYKEQAEKgNTKVKQLKRQLEEAEEESQRIN 1897
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIK------KEALLEAKEEihKLRNEFEKELRER-RNELQKLEKRLLQKEENLDRKL 102
|
90 100 110
....*....|....*....|....*....|...
gi 241982718 1898 ANRRKLQRELDEATESNEAMGREVNALKSKLRR 1930
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1051-1155 |
4.89e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1051 QELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKirELEGHISDLQEDLDSE 1130
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKK--EADEIIKELRQLQKGG 600
|
90 100
....*....|....*....|....*..
gi 241982718 1131 RAA--RNKAEKQKRDLGEELEALKTEL 1155
Cdd:PRK00409 601 YASvkAHELIEARKRLNKANEKKEKKK 627
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1780-1905 |
5.04e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1780 AQKNESARQQLERQNKELRSKLQEVEgavkaklkstvaaLEAK--IAQLEEQVEQEAREKQaatKSLKQKDKKLKEVLLQ 1857
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL-------------LEAKeeIHKLRNEFEKELRERR---NELQKLEKRLLQKEEN 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 241982718 1858 VEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQRINANRR-KLQR 1905
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLqELER 146
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1027-1160 |
5.17e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1027 KLKSKHESMISELEVRLKKEEKSRQELEKLKRklegdasdfhEQIADLQAQIAELKMQLAKKEEELQAALARLDEEiaqk 1106
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAE---- 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 241982718 1107 nnalkkiRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLD 1160
Cdd:COG0542 467 -------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
976-1258 |
5.18e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 976 AEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKaknLTKLKSKHEsmisELEVRLKKEEKSRQELEK 1055
Cdd:PTZ00440 1054 MKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNK---LIEIKNKSH----EHVVNADKEKNKQTEHYN 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1056 LKRKlegDASDFHEQIADLQAQIAELKMQLAKKEE----ELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSer 1131
Cdd:PTZ00440 1127 KKKK---SLEKIYKQMEKTLKELENMNLEDITLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQ-- 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1132 aARNKAEKQKRDLGEELE---------ALKTELEDtLDSTATQQELRAKREQEVTVLKkaldeetrSHEAQVQEMRQKHT 1202
Cdd:PTZ00440 1202 -VKKNMSKERNDHLTTFEynayydkatASYENIEE-LTTEAKGLKGEANRSTNVDELK--------EIKLQVFSYLQQVI 1271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1203 QAVEELTEQLEQFKRAKA------------NLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLE 1258
Cdd:PTZ00440 1272 KENNKMENALHEIKNMYEflisidsekilkEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAK 1339
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
995-1233 |
5.37e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 995 SKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKkeeksrqELEKLKrKLEGDASDF------- 1067
Cdd:PRK05771 75 EKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIE-------RLEPWG-NFDLDLSLLlgfkyvs 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1068 ------HEQIADLQAQIAELK----------------MQLAKKEEELQAALARLD---EEIAQKNNALKKIRELEGHISD 1122
Cdd:PRK05771 147 vfvgtvPEDKLEELKLESDVEnveyistdkgyvyvvvVVLKELSDEVEEELKKLGferLELEEEGTPSELIREIKEELEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1123 LqedldseraarnkaEKQKRDLGEELEALKTELEDTLdsTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRqkht 1202
Cdd:PRK05771 227 I--------------EKERESLLEELKELAKKYLEEL--LALYEYLEIELERAEALSKFLKTDKTFAIEGWVPEDR---- 286
|
250 260 270
....*....|....*....|....*....|.
gi 241982718 1203 qaVEELTEQLEQFKRAKANLDKSKQTLEKEN 1233
Cdd:PRK05771 287 --VKKLKELIDKATGGSAYVEFVEPDEEEEE 315
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1635-1928 |
5.99e-03 |
|
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: 41.48 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1635 SAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAA--AERARKQADLEKEE 1712
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEkiAEYTKSIDIKKATE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1713 LAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQgnmEAMSDRVRKATLQAEQLSNELATERSTAQKNeSARQQLER 1792
Cdd:COG5185 313 SLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQ---ESLTENLEAIKEEIENIVGEVELSKSSEELD-SFKDTIES 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1793 QNKELRSKLQEVEGavkaKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQyKEQA 1872
Cdd:COG5185 389 TKESLDEIPQNQRG----YAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADE-ESQS 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 241982718 1873 EKGNTKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKL 1928
Cdd:COG5185 464 RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1752-1842 |
6.01e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 40.80 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1752 MEAMSDRVRKATLQAEQLSNELATERSTAqKNESARQQLERQNKELRSKLQEVEGAVKAklkSTVAALEAKIAQLEEQVE 1831
Cdd:COG4223 2 IAALEAAVAELPAQLTALEQRLAALEAAP-AAAAATAALEARLAALRAALAAAREAVAA---AAAAALEARLAALEAKAA 77
|
90
....*....|.
gi 241982718 1832 QEAREKQAATK 1842
Cdd:COG4223 78 APEAEAAAAAR 88
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1765-1929 |
6.13e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1765 QAEQLSNELAT---ERSTAQKNESARQ---QLERQNKELRSKLQEVEGAVKA-KLKSTVAALEAKIAQLEEQVEQEAREK 1837
Cdd:COG3206 149 LAAAVANALAEaylEQNLELRREEARKaleFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1838 QAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEES-------------QRINANRRKLQ 1904
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpdvialrAQIAALRAQLQ 308
|
170 180
....*....|....*....|....*
gi 241982718 1905 RELDEATESNEAmgrEVNALKSKLR 1929
Cdd:COG3206 309 QEAQRILASLEA---ELEALQAREA 330
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
846-1211 |
6.25e-03 |
|
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: 41.64 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 846 QVTRQEEEMQAKEEEMQKIKErqqkaetelkelEQKHTQLAEektllqeqlqaetelyAEAEEMRVRLAAKKQELEEIlh 925
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKN------------EGDHLRNVQ----------------TECEALKLQMAEKDKVIEIL-- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 926 emearlEEEEDRGQQLQAERKKMAQQMLDleeqleeeeaarQKLQLEKVTAEAKIKKLEDDILvMDDQNSKLSKerklLE 1005
Cdd:pfam15921 568 ------RQQIENMTQLVGQHGRTAGAMQV------------EKAQLEKEINDRRLELQEFKIL-KDKKDAKIRE----LE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1006 ERVSDLTTN----LAEEEEKAKNLTKLKSKHESMISELevrlkkeEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAEL 1081
Cdd:pfam15921 625 ARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLNEV-------KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKL 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1082 KMQLAKKEEELQAALARLDEEIAQKNNAL-------KKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEElealKTE 1154
Cdd:pfam15921 698 KMQLKSAQSELEQTRNTLKSMEGSDGHAMkvamgmqKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE----KNK 773
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 241982718 1155 LEDTLDSTATQQ-----ELRAKREQE------VTVLKKALDEETRSHeAQVQEMRQKHTQAVEELTEQ 1211
Cdd:pfam15921 774 LSQELSTVATEKnkmagELEVLRSQErrlkekVANMEVALDKASLQF-AECQDIIQRQEQESVRLKLQ 840
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1069-1260 |
6.35e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1069 EQIADLQAQIAELKMQLAKKEEELQAalarldeeiaqKNNALKKIRELEGHIsdlqedldseRAARNKAEKQKRDLGEEL 1148
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLEA-----------KEEIHKLRNEFEKEL----------RERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1149 EALKTELEDtLDstatqqelraKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELtEQLEQFKRAKAN---LDKS 1225
Cdd:PRK12704 96 ENLDRKLEL-LE----------KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLTAEEAKeilLEKV 163
|
170 180 190
....*....|....*....|....*....|....*
gi 241982718 1226 KQTLEKENADLAGELRVlgQAKQEVEHKKKKLEVQ 1260
Cdd:PRK12704 164 EEEARHEAAVLIKEIEE--EAKEEADKKAKEILAQ 196
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1561-1898 |
6.36e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 41.54 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1561 AKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGR 1640
Cdd:COG0840 6 LLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1641 EEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASS 1720
Cdd:COG0840 86 LALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1721 LSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEA--MSDRVRKATLQAEQLSNELA----TERSTAQKNESARQqLERQN 1794
Cdd:COG0840 166 LLEAAALALAAAALALALLAAALLALVALAIILAllLSRSITRPLRELLEVLERIAegdlTVRIDVDSKDEIGQ-LADAF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1795 KELRSKLQEVEGAVKA---KLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQ 1871
Cdd:COG0840 245 NRMIENLRELVGQVREsaeQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASEL 324
|
330 340
....*....|....*....|....*..
gi 241982718 1872 AEKGNTKVKQLKRQLEEAEEESQRINA 1898
Cdd:COG0840 325 AEEGGEVVEEAVEGIEEIRESVEETAE 351
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
866-1663 |
6.74e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 866 ERQQKAETELKELEqkhTQLAEEKTLLQEQLQAETE-LYAEAEEMRVRLAAKKQELEEIlhemearleeeedrgqQLQAE 944
Cdd:PRK10246 191 EQHKSARTELEKLQ---AQASGVALLTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSL----------------NWLTR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 945 RKKMAQQMLDLEEQLEEEEAARQKL--QLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKA 1022
Cdd:PRK10246 252 LDELQQEASRRQQALQQALAAEEKAqpQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIR 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1023 KNLTKLKSKHESMISELEVRLKKEEKSR---QELEKLKRKLEGDASDfHEQIADLQAQIAELKMQLAKKEEelqAALARL 1099
Cdd:PRK10246 332 HHAAKQSAELQAQQQSLNTWLAEHDRFRqwnNELAGWRAQFSQQTSD-REQLRQWQQQLTHAEQKLNALPA---ITLTLT 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1100 DEEIAQKNNALKKIRELEGHISDLQEDLDSERaarnkaeKQKRDLGEELEALKTELEDtLDSTATQQELRAK-REQEVTV 1178
Cdd:PRK10246 408 ADEVAAALAQHAEQRPLRQRLVALHGQIVPQQ-------KRLAQLQVAIQNVTQEQTQ-RNAALNEMRQRYKeKTQQLAD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1179 LKKALDEETRSHEAQVQEMRQKHTQ-----------AVEELTE-QLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQA 1246
Cdd:PRK10246 480 VKTICEQEARIKDLEAQRAQLQAGQpcplcgstshpAVEAYQAlEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQ 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1247 KQEVEHKKKKLEVQLQDLQSkcsdgerARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLakdvaSLGSQLQDTQELLQE 1326
Cdd:PRK10246 560 LQRDESEAQSLRQEEQALTQ-------QWQAVCASLNITLQPQDDIQPWLDAQEEHERQL-----RLLSQRHELQGQIAA 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1327 ETRQklnVSTKLRQLEDERNSLQDQLDeemeakqnlerhvstlniQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQ 1406
Cdd:PRK10246 628 HNQQ---IIQYQQQIEQRQQQLLTALA------------------GYALTLPQEDEEASWLATRQQEAQSWQQRQNELTA 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1407 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEknisskyADERDRAeAEAREKETKAL 1486
Cdd:PRK10246 687 LQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQD-------VLEAQRL-QKAQAQFDTAL 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1487 SLARALEEALeakeelertnkMLKAEMEDlvsskddvgKNVHELEKSKRALETQMEEMKTQLEELEDELQAtedaklrle 1566
Cdd:PRK10246 759 QASVFDDQQA-----------FLAALLDE---------ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQ--------- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1567 vnMQALKGQFeRDLQARDEQNEEKRRQLQRQLHEYETELEDERKQralaaaakkklegdlkdlelqadsaIKGREEAIKQ 1646
Cdd:PRK10246 810 --HQQHRPDG-LDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQ-------------------------LKQDADNRQQ 861
|
810
....*....|....*..
gi 241982718 1647 LRKLQAQMKDFQRELDD 1663
Cdd:PRK10246 862 QQALMQQIAQATQQVED 878
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
862-1094 |
7.40e-03 |
|
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: 41.26 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 862 QKIKERQQKAETELKELEQKHTQLAEEKTLL----QEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDR 937
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNK 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 938 GQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTN--- 1014
Cdd:pfam15921 687 SEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhf 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1015 LAEEEEK-AKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAE---LKMQLAKKEE 1090
Cdd:pfam15921 767 LKEEKNKlSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQEsvrLKLQHTLDVK 846
|
....
gi 241982718 1091 ELQA 1094
Cdd:pfam15921 847 ELQG 850
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1797-1925 |
7.70e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.73 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1797 LRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQaaTKSLKQKdkklkevllQVEDERKMAEQYKEQAEkgn 1876
Cdd:pfam02841 178 LQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAE--QELLREK---------QKEEEQMMEAQERSYQE--- 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 241982718 1877 tKVKQLKRQLEEAEE----ESQRINANRRKLQRELDEAT--ESNEAMGREVNALK 1925
Cdd:pfam02841 244 -HVKQLIEKMEAEREqllaEQERMLEHKLQEQEELLKEGfkTEAESLQKEIQDLK 297
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1509-1649 |
8.18e-03 |
|
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: 39.91 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1509 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFE-RDLQARDEQN 1587
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 241982718 1588 EEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRK 1649
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1415-1859 |
8.31e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.05 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1415 YDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEE 1494
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1495 ALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKG 1574
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1575 QFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQM 1654
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1655 KDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRL 1734
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1735 EARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAKLKS 1814
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 241982718 1815 TVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVE 1859
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAAL 525
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1810-1922 |
8.44e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1810 AKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSlkqKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEA 1889
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQEL 476
|
90 100 110
....*....|....*....|....*....|...
gi 241982718 1890 EEESQRINANRRKLQRELDEATESNEAMGREVN 1922
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1067-1174 |
8.95e-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: 40.51 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1067 FHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNAL----KKIRELEGHISDLQEDLDS--ERAARNKAEKQ 1140
Cdd:pfam09787 59 LREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLaterSARREAEAELERLQEELRYleEELRRSKATLQ 138
|
90 100 110
....*....|....*....|....*....|....*.
gi 241982718 1141 KR--DLGEELEALKTELEDTLDSTATQQELRAKREQ 1174
Cdd:pfam09787 139 SRikDREAEIEKLRNQLTSKSQSSSSQSELENRLHQ 174
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1523-1688 |
9.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1523 VGKNVHELEKSKRALETQmEEMKTQLEELEDELQATEDAKLrLEVN--MQALKGQFERDLQARDEQNEEKRRQLQRQLHE 1600
Cdd:PRK12704 20 IGYFVRKKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1601 YETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRE--LDDARA-SRDEIFATSKE 1677
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKE 177
|
170
....*....|.
gi 241982718 1678 NEKKAKsLEAD 1688
Cdd:PRK12704 178 IEEEAK-EEAD 187
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
874-1472 |
9.01e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 874 ELKELEQKHTQLAEEKTLLQEQLQAETELYAEAeemrvrlaakKQELEEILHEMEARleeeedrgqqlqAERKKMAQQML 953
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQY----------KKDVTELLNKYSAL------------AIKNKFAKTKK 1544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 954 DLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKlleeRVSDLTTNLAEEEEKAKNLTKLKSKHE 1033
Cdd:TIGR01612 1545 DSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNK----AAIDIQLSLENFENKFLKISDIKKKIN 1620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1034 SMISELEVRLKKEEKSRQELEKLKRKLEGDA----SDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEE------- 1102
Cdd:TIGR01612 1621 DCLKETESIEKKISSFSIDSQDTELKENGDNlnslQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHkknyeig 1700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1103 IAQKNNALKKI--RELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELrakreqeVTVLK 1180
Cdd:TIGR01612 1701 IIEKIKEIAIAnkEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNI-------IAGCL 1773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1181 KALDEETRSHEaqvqEMRQKHTQAVEELTEQLEQFKRAKANLDKskqtLEKENADlagelRVLGQAKQEVEHKKKKLEVQ 1260
Cdd:TIGR01612 1774 ETVSKEPITYD----EIKNTRINAQNEFLKIIEIEKKSKSYLDD----IEAKEFD-----RIINHFKKKLDHVNDKFTKE 1840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1261 LQDLQ------SKCSDGERARAELSDKVHKLQNEVESVTGMLN--------EAEGKAIKLAKDVASLGSQLQDTQEL--- 1323
Cdd:TIGR01612 1841 YSKINegfddiSKSIENVKNSTDENLLFDILNKTKDAYAGIIGkkyysykdEAEKIFINISKLANSINIQIQNNSGIdlf 1920
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1324 ----------LQEETRQKLN----------VSTKLR-----------QLEDERNSLQDQLDEEMEAKQNLE--RHVSTLN 1370
Cdd:TIGR01612 1921 dniniailssLDSEKEDTLKfipspekepeIYTKIRdsydtlldifkKSQDLHKKEQDTLNIIFENQQLYEkiQASNELK 2000
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1371 IQLSDSKKKLQDFASTIEVMEEGKKRLQKeMEGLSQQYEE--KAAAYDKLEKTKNRLQQELDDLVVDLDNQ--RQLVSNL 1446
Cdd:TIGR01612 2001 DTLSDLKYKKEKILNDVKLLLHKFDELNK-LSCDSQNYDTilELSKQDKIKEKIDNYEKEKEKFGIDFDVKamEEKFDND 2079
|
650 660
....*....|....*....|....*.
gi 241982718 1447 EKKQKKFDQLLAEEKNISSKYADERD 1472
Cdd:TIGR01612 2080 IKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1750-1916 |
9.60e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1750 GNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKelrsklQEVEGAVKAKLKSTVAALEAKIAQLEEQ 1829
Cdd:PRK09510 73 SAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK------QAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1830 VEQEAREKQAATksLKQKDKKLKEVLLQVEDERKMAEQYKEQAE-KGNTKVKQLKRQLEEAEEESQRINANRRKLQRELD 1908
Cdd:PRK09510 147 AKAEAEAKRAAA--AAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
....*...
gi 241982718 1909 EATESNEA 1916
Cdd:PRK09510 225 AAAAKAAA 232
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1760-1910 |
9.93e-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: 40.48 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982718 1760 RKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAvKAKLKSTVAALEAKIAQLEEQVEQEAREKQA 1839
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGA-TAQLRAAQAAVKAAQAQLAQAQIDLARRRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 241982718 1840 ATKSLKQKDKKL--KEVLLQVEDERKMAEQYKEQAEKgnTKVKQLKRQLEEAEEESQRINANRRKLQRELDEA 1910
Cdd:pfam00529 133 APIGGISRESLVtaGALVAQAQANLLATVAQLDQIYV--QITQSAAENQAEVRSELSGAQLQIAEAEAELKLA 203
|
|
| |
