|
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: 1485.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 848 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 927
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 928 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR 1007
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1008 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTK 1087
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1088 KEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1167
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1168 LRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1247
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1248 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEE 1327
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1328 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQR 1407
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1408 LEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALS 1487
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1488 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1567
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1568 NMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1647
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1648 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSAL 1727
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1728 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1807
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1808 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1887
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1907083614 1888 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| 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: 1452.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1907083614 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 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: 1332.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP-GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 416
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 417 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQKPRQLKDKADF 575
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmtETAFGSAYKTKKGMFRTVGQ 655
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 656 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1907083614 736 IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| 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: 1236.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP----GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 574
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGsAYKTKKGMFRTVG 654
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 1907083614 735 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 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: 1210.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 1907083614 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| 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: 1206.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 658
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 1907083614 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| 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: 1187.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHN----IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTEtaFGSAYKTKKGMFRTVG 654
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 1907083614 735 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 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: 1169.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASS---------HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 250 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQET 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 330 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 409
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKpRQL 569
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTgMTETAFGSayKTKKGM 649
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1907083614 730 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
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: 1154.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQETMEAMHIMGF 338
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 499 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 578
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSayKTKKGMFRTVGQLYK 658
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 738
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 1907083614 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| 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: 1115.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA----GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 247 RINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDN 325
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 326 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 566 PRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETafgsAYKT 645
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKST----PKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 646 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1907083614 726 QRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| 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: 1021.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipGELERQLLQANPILESFGNAKTVKNDNS 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 240 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIP 318
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGgCLTVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 319 GQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGMNVMEFTRAIL 397
Cdd:smart00242 235 GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 398 TPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCIN 477
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQ 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 558 GSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgldqvtgmtet 637
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS---------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 638 afGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:smart00242 534 --GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 718 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 783
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1461 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 924.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 36 VWIPSERHGFEAASIKEERGDEVMVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 191 VIQYLAHVASSHkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 270
Cdd:COG5022 172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 271 AVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKV 349
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 350 VSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATY 429
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 430 ERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 509
Cdd:COG5022 406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 510 DFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHSKFQKPRQLKDKadFCIIHYAGKVDYK 587
Cdd:COG5022 485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 588 ADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVgldqvtgmtetafgsayktKKGMFRTVGQLYKESLTKLMAT 667
Cdd:COG5022 561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 668 LRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA----IPKGFMDG 743
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 744 KQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQLSALKVLQRNC 823
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 824 AAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEEL--LKVKEKQTKVEGELEEMERKHQqlleeknilAEQLQAETE 901
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIikLQKTIKREKKLRETEEVEFSLK---------AEVLIQKFG 852
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 902 LFAEAEEMRARLaaKKQELEEilhdlesrveeeeernQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIK 981
Cdd:COG5022 853 RSLKAKKRFSLL--KKETIYL----------------QSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKS 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 982 KMEEEVLLLEDQNSKFIKEKKLMEDRIAECSS--QLAEEEEKAKNLAKIRNKQEVmISDLEERLKKEEKTRQELEKAKRK 1059
Cdd:COG5022 915 LSSDLIENLEFKTELIARLKKLLNNIDLEEGPsiEYVKLPELNKLHEVESKLKET-SEEYEDLLKKSTILVREGNKANSE 993
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1060 LDG---ETTDLQDQIAELQAQVDELKV---------QLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDF 1127
Cdd:COG5022 994 LKNfkkELAELSKQYGALQESTKQLKElpvevaelqSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRR 1073
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1128 ESEKASRNKAEKQK--RDLSEELEALKTELEDT-------LDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQ--- 1195
Cdd:COG5022 1074 ENSLLDDKQLYQLEstENLLKTINVKDLEVTNRnlvkpanVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSvlq 1153
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1196 ---DMRQRHATALEELS-----EQLEQAKRFKANLEKNKQGLETDNKELACEVK-VLQQVKAESEHKRKKLDAQVQELHA 1266
Cdd:COG5022 1154 lelDGLFWEANLEALPSpppfaALSEKRLYQSALYDEKSKLSSSEVNDLKNELIaLFSKIFSGWPRGDKLKKLISEGWVP 1233
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1267 KVSEGDRLRVELAEKANKLQNELDN--VSTLLEEAEKKGIKFAKDA----AGLESQLQDTQELLQEETRQKLNLSSRIRQ 1340
Cdd:COG5022 1234 TEYSTSLKGFNNLNKKFDTPASMSNekLLSLLNSIDNLLSSYKLEEevlpATINSLLQYINVGLFNALRTKASSLRWKSA 1313
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1341 LEEEKNSLQEQQEEEEEARKNLEKQVLALQsQLADTKKKVDDDLGTIesleeakKKLLKDVEALSQRLEEKVLA-YDKLE 1419
Cdd:COG5022 1314 TEVNYNSEELDDWCREFEISDVDEELEELI-QAVKVLQLLKDDLNKL-------DELLDACYSLNPAEIQNLKSrYDPAD 1385
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....
gi 1907083614 1420 KTKNRLQQELDDLTVDLDHQRQIVSNLEKK--QKKFDQLLAEEK 1461
Cdd:COG5022 1386 KENNLPKEILKKIEALLIKQELQLSLEGKDetEVHLSEIFSEEK 1429
|
|
| 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: 868.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL-----SNGYIPIPGQQDKDNFQETMEA 332
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 333 MHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNT--DQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 570 KDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdvdrivgldqvtgmtetafgsayktkkgm 649
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 650 frtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1907083614 730 ILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 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: 786.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVA------SSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 253 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 330
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 491 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR-- 567
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 568 -QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDQVtgmTETAFGSAYKTK 646
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDST---EDPKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 647 KGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14927 550 KAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1907083614 726 QRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 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: 778.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSH--KGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 416 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKAD 574
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 575 --FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvTGMTETAFGSAYKTKKGMFRT 652
Cdd:cd14913 477 ahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA--------TADADSGKKKVAKKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14913 549 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1907083614 733 PNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14913 629 ASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 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: 756.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLK---DKA 573
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgLDQVTGMTETAFGSAYKtKKGMFRTV 653
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD------HAGQSGGGEQAKGGRGK-KGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907083614 734 NAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 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: 746.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHL-KSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK---A 573
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgldqvtgmtETAFGSAYKTKKGM-FRT 652
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 1907083614 733 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| 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: 727.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGrkDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ETQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 418 DFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 497 EEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK--FQKPRQLKDKad 574
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRfvaelwkdvdrivgldqvtgmtetafgsayktKKgmfrTVG 654
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------------KK----TVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS 593
|
650 660 670
....*....|....*....|....*....|....*..
gi 1907083614 735 AIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01380 594 KEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
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: 719.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 416
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 417 ADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14929 316 VTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 497 EEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK--A 573
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivglDQVTGmTETAFGSAYKTKKGMFRTV 653
Cdd:cd14929 472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAIQFGEKKRKKGASFQTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14929 544 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 1907083614 734 NAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14929 624 RTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
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: 710.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 416 QADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 496 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK-- 572
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKpe 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDqvtGMTETAFGsayKTKKG-MFR 651
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGAD---APIEKGKG---KAKKGsSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 652 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14917 548 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1907083614 732 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14917 628 NPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 696.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 181 GAGKTENTKKVIQYLAHVASSHKGRKDHN--IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 417
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 418 DFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 498 EYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKAD-- 574
Cdd:cd14918 402 EYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEah 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgldqVTGMTETAFGSAYKTKKGMFRTVG 654
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907083614 735 AIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14918 631 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
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: 694.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKA 573
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKGKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 574 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvTGMTETAFGSAYK--TKKG- 648
Cdd:cd14912 478 EahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQ--------TAEGASAGGGAKKggKKKGs 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 649 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14912 550 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1907083614 729 EILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14912 630 KVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| 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: 694.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKD--HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEgfNN---YRFLSNGYIPIPGQQDKDNFQETMEAM 333
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 334 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 414 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK 572
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 573 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDqvTGmtETAFGSAYKTKKGMF 650
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---ASAD--TG--DSGKGKGGKKKGSSF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 651 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1907083614 731 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| 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: 689.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHN---IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKDKA 573
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGKA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 574 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdriVGLDQVTGMTETAFGsayKTKKGMFR 651
Cdd:cd14923 477 EahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---KKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 652 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14923 551 TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1907083614 732 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14923 631 NASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 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: 689.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 334
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 415 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 495 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK- 572
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGKv 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 573 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgldqVTGMTETAFGSAYKTKKG-MF 650
Cdd:cd14910 478 eAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGKKKGsSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 651 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1907083614 731 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14910 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| 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: 677.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSHKGRKDH----NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEaasgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQETMEAM 333
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 334 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 414 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 494 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPRQLKDK 572
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 573 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvTGMTETAFGSAYKTKKG-M 649
Cdd:cd14915 477 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQ--------TAEAEGGGGKKGGKKKGsS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1907083614 730 ILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 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: 652.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--HLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 337 GFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 496 QEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADF 575
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 576 CIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTGMTETAfGSAYKTKKGMfRTVGQ 655
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGD-TTSRGTSKGK-PTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 656 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 1907083614 736 IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14883 626 RSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 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: 650.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 339 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 418
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 419 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 499 YQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlkDKAdFCII 578
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER---GGA-FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 579 HYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSayktkkgMFRTVGQLYK 658
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPLTKASGSDS-------QKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 659 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpK 738
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-S 614
|
650 660 670
....*....|....*....|....*....|...
gi 1907083614 739 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 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: 649.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER-----VKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 339 SHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG---RDYVQKAQTKE 415
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 496 QEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVEKLVQEQGSHSKFQKPRQLKD--K 572
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmtetafgsayKTKKGMFRT 652
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 1907083614 733 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| 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: 614.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDK 572
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 573 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkDVDRIVGLDqvtgmtetafgSAYKTKkgmfrT 652
Cdd:cd01381 468 S-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TRKKSP-----T 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd01381 530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 1907083614 733 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01381 610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| 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: 609.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAHVA--SSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGgrAVTEGRS-------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYiPIPGQQDKDNFQETMEAM 333
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 334 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIKVGRD-YVQ 409
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVIVTPDgIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRql 569
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgldqvtgmteTAFGSAYKtkkgm 649
Cdd:cd01384 466 LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------EGTSSSSK----- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd01384 529 FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFG 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1907083614 730 ILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01384 609 LLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| 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: 578.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNyrflsngyipipgqqDKDNFQETMEAMHIMG 337
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD---------------DVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKKERNT-------DQASMPENTVAQKlchLLGMNVMEF-----TRAILTPRIKVGR 405
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 486 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 565
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 566 PRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdvdrivgldqvTGMTET 637
Cdd:cd01382 450 PRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF------------ESSTNN 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 638 AFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 717
Cdd:cd01382 518 NKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907083614 718 RIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 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: 576.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgeHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSlSGCIEVEGVDDVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQAS---MPENTVAQKLCHLLGMNVMEFTRAILTPRIKV-GRDYVQKAQT 413
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14872 310 PAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 494 LEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKA 573
Cdd:cd14872 390 LEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgLDQVTGMTetafgsayktkkgmfrTV 653
Cdd:cd14872 467 EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQKTSKV----------------TL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtP 733
Cdd:cd14872 527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-V 605
|
650 660 670
....*....|....*....|....*....|....*....
gi 1907083614 734 NAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14872 606 KTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-771 |
1.57e-176 |
|
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: 552.07 E-value: 1.57e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGeaaseaieqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 244 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 324 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD--QASMPENTVAqKLCHLLGMNVMEFTRAILTPRI 401
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvlEDATTLQSLK-LAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 402 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 481
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 482 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVEKLVQ--- 555
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHAsfg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 556 ----------EQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVAELwkdvdri 625
Cdd:cd14890 477 rksgsggtrrGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELI-KQSRRSIREV------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 626 vgldqvtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 705
Cdd:cd14890 548 --------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 706 EGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14890 602 EAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-771 |
2.49e-176 |
|
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: 551.28 E-value: 2.49e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHkgrkdhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQ---ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 415 EQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlkDKAD 574
Cdd:cd01387 391 EQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTETAFGSAYKTKKGMFRTVG 654
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-----RAQTDKAPPRLGKGRFVTMKPRTPTVA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd01387 541 ARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL 620
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907083614 735 AIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 771
Cdd:cd01387 621 KLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-771 |
4.87e-171 |
|
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: 537.05 E-value: 4.87e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLsgAGEHLKSDLLLEGFNNYRFL-SNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASM--PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 414
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVqeqGSHSKFQK----PRqlK 570
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPR--T 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 571 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrIVGLDQVTGMTETAFGSAYKTKKGMF 650
Cdd:cd14903 461 SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 651 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1907083614 731 LTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 771
Cdd:cd14903 618 FLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-771 |
1.21e-169 |
|
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: 534.26 E-value: 1.21e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLahVASSHKGrkdHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG--SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKKER-NTDQASMPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 416 QADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 492 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPrQLKD 571
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 572 KAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdriVGLDQV-------------------- 631
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVavfrwavlrafframaafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 632 TGM----------------TETAFGSAYKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLV 695
Cdd:cd01385 541 AGRrraqrtaghsltlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELV 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 696 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd01385 619 LRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-769 |
5.48e-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: 531.29 E-value: 5.48e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 171 --DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 249 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDNF 326
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 327 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF-KKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQLCINYTNEKLQ 484
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 485 QLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSH 560
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 561 SKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdvdrivgldqvtgmtetafg 640
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 641 sayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 721 FQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------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 ... |
99-733 |
6.35e-166 |
|
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: 523.49 E-value: 6.35e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVT---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 254 -----GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP------------ 316
Cdd:cd14888 155 msgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 317 ------------IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL--- 381
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 382 CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIA 461
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 462 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWF 541
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 542 PKATDKTFVEKLVQEQGSHSKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 622 -VDRIVGLdqvtgmtetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14888 550 yLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|...
gi 1907083614 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-771 |
1.22e-165 |
|
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: 522.05 E-value: 1.22e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 337 GFSHEEILSMLKVVSSVLQFGNISFKkerNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR-DYVQKAQTKE 415
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 416 QADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 495 EQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDkaD 574
Cdd:cd14873 394 EQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--N 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVtgmtetafGSAYKTKKgmfRTVG 654
Cdd:cd14873 468 FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTL--------KCGSKHRR---PTVS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 655 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14873 537 SQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRN 616
|
650 660 670
....*....|....*....|....*....|....*..
gi 1907083614 735 AIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14873 617 LALPEDVRGK--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 |
3.20e-164 |
|
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: 517.60 E-value: 3.20e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVAsshkgrKDHNipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG------KANN--RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGagehLKSDLLLEGFN-------NYRFLSNGYIPIPGQQD--KDNFQETM 330
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKlpenkppRYLQNDGLTVQDIVNNSgnREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENTVA-QKLCHLLGMNVMEFTRAiLTPRIKVGR- 405
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEA-LTSHSVVTRg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 484 QQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVEKLvqEQGSHSK 562
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKF--HNNIKSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 563 FQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdvdrivgldqvtgmtetafgsa 642
Cdd:cd01379 463 YYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 643 yktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 722
Cdd:cd01379 517 ---------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFA 587
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1907083614 723 EFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd01379 588 DFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-771 |
3.53e-160 |
|
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: 506.54 E-value: 3.53e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAHVASShkgrkdhnIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS--------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD-------KDNFQETM 330
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 486
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 487 FNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKP 566
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 567 rqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdvdrivgldqvtgmtetafgsayktk 646
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 647 kgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14897 522 --------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1907083614 727 RYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-771 |
3.11e-159 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 504.68 E-value: 3.11e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 172 QSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNF 326
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 327 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQ----ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIK 402
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 403 VGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIFELNSFE 472
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KATDKTFVE 551
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 552 KLVQEQ-GSHSKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdvdrivgldq 630
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 631 vtgmtetafgsayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 710
Cdd:cd14892 536 -------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 711 CRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELDPNLYRIGQSKIFFR 771
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-731 |
4.16e-148 |
|
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: 472.87 E-value: 4.16e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHV------ASSHKGRKDHNIPGelerQLLQANPILESFGNAKTVKND 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSGIAA----KVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 238 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlksdlllegfnnyrflsngyipi 317
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE------------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 318 pGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQK-------LCHLLGMNVM 390
Cdd:cd14900 214 -AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 391 EFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAGFEIF 466
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 467 ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATD 546
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 547 KTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSSdrfvaelwkdVDriv 626
Cdd:cd14900 450 TTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD--- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 627 gldqvtgmtetafgsayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 706
Cdd:cd14900 509 ----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660
....*....|....*....|....*
gi 1907083614 707 GIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-771 |
2.21e-146 |
|
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: 469.39 E-value: 2.21e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 177 TGESGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 257 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKSDLLLEGFnnYRFLSNGYipipGQQD-----KDNFQET 329
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA----GCKRevqywKKKYDEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 330 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIKVGR- 405
Cdd:cd14889 227 CNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT-LTCTVTFTRg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQLCINYTNEKL 483
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 484 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 563
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 564 QKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQS-----SDRFVAELWKdVDRIVGLDQVTGMTETA 638
Cdd:cd14889 461 GKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSatpllSVLFTATRSR-TGTLMPRAKLPQAGSDN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 639 FGSAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 718
Cdd:cd14889 538 FNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWR 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 719 IVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 771
Cdd:cd14889 612 PSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-734 |
2.23e-144 |
|
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: 464.12 E-value: 2.23e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE-----------LERQLLQANPILESFGNAKTVKNDN 238
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 239 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE----GFNNYRFLSNG 313
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 314 YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFK-KERNTDQASMPENT-VAQKLCHLLGMNVME 391
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKeTLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 392 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 464
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 465 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 543 KATDKTFVEKLVQEQGSHSKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdv 622
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 623 driVGLDQVTGMTETAFGSAYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 702
Cdd:cd14907 554 ---SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 1907083614 703 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-771 |
7.32e-142 |
|
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: 456.43 E-value: 7.32e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 172 QSILCTGESGAGKTENTKKVIQYLAH--VASSHKGRKDHNI--------PGELERQLLQANPILESFGNAKTVKNDNSSR 241
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQsskkrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 242 FGKFIRINFDVTGY-IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPG 319
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 320 QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKErNTDQASMPENTVAQK-----LCHLLGMNVMEFTR 394
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAEIASESDKealatAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 395 AILTPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSFE 472
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEK 552
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 553 LVQEQGSHSKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHqSSDRFvaelwkdvdrivgLDQV 631
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKF-------------SDQM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 632 TGMTEtafgsayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 711
Cdd:cd14891 535 QELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 712 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-771 |
4.53e-138 |
|
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: 445.93 E-value: 4.53e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQkLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 415
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 416 QADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 496 QEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSKFQKPRQlkDK 572
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV--KR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvtGMTETAFGSAYKTKKGMfRT 652
Cdd:cd14904 466 TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKAP-KS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14904 536 LGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1907083614 733 PNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 771
Cdd:cd14904 616 PPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-771 |
1.08e-137 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 444.61 E-value: 1.08e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIpgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL-----RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQ--ASMPENTVAQKLCHLLGMNVmEFTRAILTPRIKV-GRDYVQKAQTK 414
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 415 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 494 LEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlkDKA 573
Cdd:cd14896 391 QEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgldqvtgmtetafgSAYKTKKGMfRTV 653
Cdd:cd14896 466 VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAE-----------------PQYGLGQGK-PTL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 654 GQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTp 733
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG- 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907083614 734 NAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14896 607 SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-771 |
2.75e-135 |
|
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: 439.34 E-value: 2.75e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE---LERQLLQANPILESFGNAKTVKNDNSSRFGKF 245
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 246 IRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--------HLKSDLLLEGFNNYRFLSNGYIPI 317
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 318 PGQ-QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE---NTVAQKLCHLLGMNVMEFT 393
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 394 RAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFEIFELNSF 471
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 472 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFV 550
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 551 EKLV--------QEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdnvatllhqssdrfvaelwkd 621
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 622 vdrivgldqvtgmtetafgsayKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 701
Cdd:cd14908 536 ----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 702 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQACERMIRALELDPNL---- 760
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSMKNIpedt 671
|
730
....*....|.
gi 1907083614 761 YRIGQSKIFFR 771
Cdd:cd14908 672 MQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-733 |
7.14e-134 |
|
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: 436.63 E-value: 7.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 169 REDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsNGYIP----IPGQQDK 323
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELL-NSYGPsfarKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 324 DN--FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAILT 398
Cdd:cd14902 240 YAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 399 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDIAGFEIFELNS 470
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 471 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFV 550
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 551 EKLVQEQGSHSKfqkprqlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkDVDRIVGLDQ 630
Cdd:cd14902 477 TKFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 631 VTGMTETAFGSAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 708
Cdd:cd14902 537 NRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAV 616
|
650 660
....*....|....*....|....*
gi 1907083614 709 RICRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14902 617 RIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-732 |
1.67e-133 |
|
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: 435.15 E-value: 1.67e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 168 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPGElerQLLQANPILESFGNAKTVKNDNSSR 241
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 242 FGKFIRINF-----DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN--NYRFLSNG- 313
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 314 -YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD---------------QASMPENTV 377
Cdd:cd14895 232 cYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 378 AQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK------ 448
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 449 ----RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEr 524
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 525 pANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDN 602
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 603 VATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGmfrtVGQLYKESLTKLMATLRNTNPNFVRCIIPN 682
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYIRCIKPN 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1907083614 683 HEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14895 623 DESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-824 |
1.01e-132 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 436.77 E-value: 1.01e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 256 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 336 MGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 490
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 570
Cdd:PTZ00014 500 VFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDS 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 571 DKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGldqvtgmtetafgsayKTKKGMF 650
Cdd:PTZ00014 577 NK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQL 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 651 rtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:PTZ00014 640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 731 LTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFA 807
Cdd:PTZ00014 718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVR 797
|
730
....*....|....*..
gi 1907083614 808 KKqqqlsaLKVLQRNCA 824
Cdd:PTZ00014 798 KN------IKSLVRIQA 808
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-769 |
1.97e-128 |
|
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: 418.62 E-value: 1.97e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMG 337
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 338 FSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPEN---TVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 412
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNeslEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 413 TKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd14876 314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 492 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFqKPRQLKD 571
Cdd:cd14876 392 FERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKVDS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 572 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGldqvtgmtetafgsayKTKKGMFr 651
Cdd:cd14876 468 NINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------KIAKGSL- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 652 tVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14876 531 -IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907083614 732 TPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 769
Cdd:cd14876 610 DLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-771 |
9.78e-125 |
|
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: 409.78 E-value: 9.78e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnipgeLERQLLQA-NPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV--------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE--GFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 335
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 336 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI------------LTPRIKV 403
Cdd:cd01386 233 LGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 404 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN------SFEQLCIN 477
Cdd:cd01386 313 SPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqrgaTFEDLCHN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALLDEECWFPKAT 545
Cdd:cd01386 392 YAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEALYPGSS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 546 DKTFVEKLVQEQG--SHSKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQSSDRFVAelw 619
Cdd:cd01386 472 DDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKETAA--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 620 kdvdrivgldqvtgmtetafgsayKTKKGMFRTVgqlyKESLTKLMATLRNTNPNFVRCIIPNH--EKRAGK-------- 689
Cdd:cd01386 549 ------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERStsspaagd 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 690 --LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACERMIRALELDPNLYR 762
Cdd:cd01386 601 elLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYR 680
|
....*....
gi 1907083614 763 IGQSKIFFR 771
Cdd:cd01386 681 IGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-733 |
2.04e-121 |
|
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: 399.22 E-value: 2.04e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGyipiPGQQDKDNFQETMEAMH 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 335 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTV---AQKLCHLLGMNVMEFTRAILTPRIKVGRDYV--Q 409
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 410 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 490 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQL 569
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 570 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgsayktkkgm 649
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAP----------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 650 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
....
gi 1907083614 730 ILTP 733
Cdd:cd14880 623 LLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-734 |
7.45e-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: 393.96 E-value: 7.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 177 TGESGAGKTENTKKVIQYLAHVASS--HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 255 YIV-GANIETYLLEKSR-AVRQAKDERTFHIFYQLLSGAGehlKSDLLLEGFNN----YRFL--------------SNGY 314
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGAS---KDERSKWGLNNdpskYRYLdarddvissfksqsSNKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 315 IPIPGQQDKD-NFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVM 390
Cdd:cd14906 238 SNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 391 EFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQGASFIGIL 458
Cdd:cd14906 318 VFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 459 DIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEE 538
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 539 CWFPKATDKTFVEKLVQEQgsHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL 618
Cdd:cd14906 475 CIMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 619 WKdvdrivglDQVTGMTETafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQ 698
Cdd:cd14906 553 FQ--------QQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQ 618
|
650 660 670
....*....|....*....|....*....|....*.
gi 1907083614 699 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 734
Cdd:cd14906 619 LRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-771 |
1.01e-114 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 380.00 E-value: 1.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 173 SILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 253 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETME 331
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 332 AMHIMgFSHEEILSMLKVVSSVLQFGNISFKKERN--TDQASMPENTVA-QKLCHLLGMNVMEFTRAILTPRIKVGRDYV 408
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 409 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLLINYANERLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECwfpkatdktfvekLVQeQGSHSKFQK 565
Cdd:cd14886 388 YFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQC-------------LIQ-TGSSEKFTS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 566 PRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLdqvtgm 634
Cdd:cd14886 451 SCKSKIKNNsfipgkgsqcnFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 635 tetafgsayktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 714
Cdd:cd14886 525 -----------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRG 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 715 FPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14886 592 FAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-771 |
4.01e-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: 375.69 E-value: 4.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 176 CTGESGAGKTENTKKVIQYLAHVASSHKGR-KDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFD-VT 253
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 254 GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRFLSNGYI----PIPGQ--QDKDNF 326
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 327 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILtprIKVGRD 406
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 407 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 485
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQ 564
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPyFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 565 KPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdrivgldqvtgmtetafgsaYK 644
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL------------------------LS 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 645 TKKGMFR---TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 721
Cdd:cd14875 529 TEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 722 QEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSKIFFR 771
Cdd:cd14875 609 EQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-728 |
2.87e-106 |
|
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: 357.87 E-value: 2.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 168 DREDQSILCTGESGAGKTENTKKVIQYLA-------HVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 239 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-----AGEHLKSDLLLEGFNNYRFLSN 312
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 313 GYIPI--PGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQ--------- 379
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 380 -KLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT----------- 447
Cdd:cd14899 321 tKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 448 ---KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIER 524
Cdd:cd14899 401 vddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 525 paNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 601
Cdd:cd14899 480 --RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 602 NVATLLHQSSDRFVAEL-----WKDVDRIVGLDQVTGMTETAFGSAYKTKkgmfrTVGQLYKESLTKLMATLRNTNPNFV 676
Cdd:cd14899 558 SAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAV-----SVGTQFKIQLNELLSTVRATTPRYV 632
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 677 RCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14899 633 RCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-771 |
6.90e-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: 336.62 E-value: 6.90e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 251 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFlsngyipipgqqDKDNFQETM 330
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST------------DLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 331 EAMHIMGFSHEEIlsmLKVVSSVLQFGNISFKKERNTDQASMPENT--------VAQKLCHLL-------GMNVMEFTRA 395
Cdd:cd14887 225 KTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkclssGLKVTEASRK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 396 ILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR------ 449
Cdd:cd14887 302 HLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesds 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 450 -------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQP 517
Cdd:cd14887 382 dedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 518 CIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVEKLVQEQGSHSKFQK--PRQ 568
Cdd:cd14887 462 ASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPAL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 569 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVaelwkdvdRIVGLDQVTGMtetafgSAYKTKKg 648
Cdd:cd14887 542 SRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGV------RAISSRR- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 649 mfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14887 606 --STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRY 683
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1907083614 729 EILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14887 684 ETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-770 |
6.06e-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: 331.05 E-value: 6.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSHKGRKdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGK 244
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 245 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGY--IPIPGQ 320
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 321 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMpENT-VAQKLCHLLGMNVMEFtRAIL 397
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTdVLDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 398 TPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIF---ELN 469
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 470 SFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALLDEEC-WFPK 543
Cdd:cd14879 386 SLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILDDQTrRMPK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 544 ATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndnvatllhqSSDrFVAelwk 620
Cdd:cd14879 458 KTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN---- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 621 dvdrivgldqvtgmtetafgsayktkkgMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14879 523 ----------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIR 573
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMIRALELDPNLYRIGQSKIFF 770
Cdd:cd14879 574 SLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-735 |
4.82e-97 |
|
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: 326.08 E-value: 4.82e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDvtGYIVGA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT---------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDlllegFNNYRFLSNGYIPIPgqQDKDNFQETMEAMHIMGFS 339
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSSTAGNKESIV--QLSEKYKMTCSAMKSLGIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 340 HeeILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADF 419
Cdd:cd14898 220 N--FKSIEDCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 420 AVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 499
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 500 QREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLvqeqgshSKFQKPRqLKDKADFCII- 578
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-INTKARDKIKv 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 579 -HYAGKVDYKADEWLMKNMDplndnvatllhqssdrfvaelwkdvdrivgldqvtGMTETAFGSAYKTKKGMFRTVGQLY 657
Cdd:cd14898 440 sHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDEGSKEDLVKYF 484
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 658 KESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 735
Cdd:cd14898 485 KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-771 |
2.14e-93 |
|
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: 318.30 E-value: 2.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTG 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 255 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY----IPIPGQQDKDNFQETM 330
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 331 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 410
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 411 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 487
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 488 NHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATDKTFVEKL--V 554
Cdd:cd14878 393 NEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLqsL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 555 QEQGSHSKFQKPRQ-------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdriv 626
Cdd:cd14878 460 LESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 627 gldqvtgmtetafgsaYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 706
Cdd:cd14878 532 ----------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLE 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 707 GIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALELDPNL--YRIGQSKIFFR 771
Cdd:cd14878 593 MVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVLQQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-771 |
5.83e-91 |
|
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: 310.41 E-value: 5.83e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAhvasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 259 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 338
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 339 sHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENT--VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 413
Cdd:cd14937 228 -HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 494 LEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKa 573
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 574 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTetafgsaYKtkkgmfrtv 653
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLIT-------FK--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 654 gqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEILTP 733
Cdd:cd14937 525 ---YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDY 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907083614 734 NAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 771
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-723 |
2.69e-82 |
|
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: 286.80 E-value: 2.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT---ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 251 D---------VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-AGEHLKSDLLLEGFNNYRFL---------- 310
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 311 ----------SNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKkerntdqasmpentvaqK 380
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------A 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 381 LCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-------- 452
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 453 ---SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpanpp 529
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 530 gVLALLDE-----ECWFPKATDKTFV-----EKLVQEQGSHSK-FQKPR--------QLKDKADFCIIHYAGKVDYKADE 590
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHdadgtakkQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 591 WLMKNMDPLNDNVATLLHQSSDRFVAElwkdvdrivgldqvtgmtetafgSAYKTKKGMFRTVGQLYKESLTKLMATLRN 670
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 671 TNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 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 |
2.74e-78 |
|
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: 273.14 E-value: 2.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 173 SILCTGESGAGKTENTKKVIQYLAHVASshkgrkdhnipGELE----RQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG-----------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 249 NFdVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 326
Cdd:cd14881 139 QV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 327 QETMEAMHIMGFsheEILSMLKVVSSVLQFGNISF--KKERNTDQASMPE-NTVAQklchLLGMNVMEFTRAiLTPRIK- 402
Cdd:cd14881 218 QAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFidGGGLEVDVKGETElKSVAA----LLGVSGAALFRG-LTTRTHn 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 403 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFELNSFEQL 474
Cdd:cd14881 290 ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 475 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDKTFVEKL 553
Cdd:cd14881 366 CINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 554 VQEQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdrfvaelwkdvdrivgldqvtg 633
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 634 mteTAFGsayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQ 713
Cdd:cd14881 499 ---CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAG 566
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1907083614 714 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 758
Cdd:cd14881 567 GYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-736 |
3.84e-72 |
|
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: 255.18 E-value: 3.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNipgelerqllQANPILESFGNAKTVKNDNSSRFGKFIRINFDvTGYIV 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSS----------AIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIE-TYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNTD-QASMPE--NTVAQKLCHLLGMNVMEFTRAILTPRIKVGrdyvqKAQT 413
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSEDG-----TTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 414 KEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 494 LEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQlKDK 572
Cdd:cd14874 373 DQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KER 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 573 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELwkdvdrivgldqvtgmtetaFGSAYKTKKGMFRT 652
Cdd:cd14874 450 LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL--------------------FESYSSNTSDMIVS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 653 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 732
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
....
gi 1907083614 733 PNAI 736
Cdd:cd14874 590 PGDI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-771 |
7.92e-71 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 252.71 E-value: 7.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnipgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY---------ILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 258 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDNFQETMEAMHIM 336
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 337 GFSHEEILSMLKVVSSVLQFGNISFKKERNtdQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAqtkeq 416
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR----- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 417 adfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14905 304 -----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 497 EEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF-QKPRQlkdkad 574
Cdd:cd14905 377 REYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 575 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRF-------------VAELWKDVD----------RIVGL--- 628
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakksplSIVKVlls 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 629 ------DQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAGKLDPHLVLDQLR 700
Cdd:cd14905 524 cgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSKIFFR 771
Cdd:cd14905 604 SLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-770 |
7.29e-68 |
|
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: 245.27 E-value: 7.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 172 QSILCTGESGAGKTENTKKVIQYLAHVASS----HKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 248 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgEH---LKSDLLL-EGFNNYRFLSNGyIPIPGQ--Q 321
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQA-DPLATNfaL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 322 DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQ-KLCHL-------LGMNVME 391
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDaQSCALkdpaqilLAAKLLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 392 FTRAILTPRIKVGRDYVQ---------KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQG----ASF 454
Cdd:cd14893 322 VEPVVLDNYFRTRQFFSKdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 455 IGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIDLIERP 525
Cdd:cd14893 402 VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFEDK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 526 anPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD------------FCIIHYAGKVDYKADEWLM 593
Cdd:cd14893 482 --PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 594 KNMDPLNDNVATLLHQSSDrfvaelwkDVDRIVGLDQVT--------------GMTETAFG----SAYKTKKGMFRTVGQ 655
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAaassekaakqteerGSTSSKFRksasSARESKNITDSAATD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 656 LYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYeiltpna 735
Cdd:cd14893 632 VYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------- 703
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907083614 736 ipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 770
Cdd:cd14893 704 --KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-731 |
6.08e-66 |
|
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: 237.33 E-value: 6.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 180 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPGELERqllqANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRVES----SIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 260 NIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKsDLLLEGFNNYRFLSngyIP--IPG----------QQDKDN 325
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLR---IPpeVPPsklkyrrddpEGNVER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 326 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKerNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 405
Cdd:cd14882 229 YKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 406 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNSFEQLCINYTN 480
Cdd:cd14882 307 SAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 481 EKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECwfPKATDKTFVEKLVQEQ 557
Cdd:cd14882 384 EQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQNYIMDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 558 gsHSKFQKPrqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivglDQVTGMtet 637
Cdd:cd14882 456 --HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 638 afgsayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 714
Cdd:cd14882 521 ------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKG 588
|
650
....*....|....*..
gi 1907083614 715 FPNRIVFQEFRQRYEIL 731
Cdd:cd14882 589 FSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-769 |
2.81e-59 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 218.94 E-value: 2.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 179 ESGAGKTENTKKVIQYLAHVA----------SSHKGRKDHNIP-----GELERQLLQANPILESFGNAKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrrlptnlNDQEEDNIHNEEntdyqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 244 KFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 324 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNI----SFKKE----------------------RNTDQASMPENTV 377
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 378 AQKL-CHLLGMNVMEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 454
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 455 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 534
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 535 LDEECWFPKATDKTFVEKLVQEQGSHSKF--QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSD 612
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRNSKyiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 613 RFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFVRCIIPNHEKRA- 687
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 688 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIRALELDPNLYRIGQSK 767
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 1907083614 768 IF 769
Cdd:cd14938 710 IF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-255 |
1.01e-58 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 200.26 E-value: 1.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 200 SSHKGRKDHN-------IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01363 81 FNGINKGETEgwvylteITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1005-1861 |
3.18e-35 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 147.51 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1005 EDRIAECSSQL------AEEEEKAKNL-AKIRNKQ-EVMISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQA 1076
Cdd:TIGR02168 192 EDILNELERQLkslerqAEKAERYKELkAELRELElALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1077 QVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1156
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1157 DTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATaLEELSEQLEQAKRFKANLEKNKQGLETDNkel 1236
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEI--- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1237 acevkvlqqvkaeSEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDaaglESQ 1316
Cdd:TIGR02168 424 -------------EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1317 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVdddlgTIESLEEAKKk 1396
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV-----VVENLNAAKK- 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1397 llkDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAeekGISARYAEERDRAEA 1476
Cdd:TIGR02168 561 ---AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1477 EAREKETKAL---------------SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1541
Cdd:TIGR02168 635 LELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1542 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQnEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1621
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL-EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1622 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1701
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1702 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSA-- 1779
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtl 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1780 ------AQKSDNARQQLERQNKELKAKLQELeGAVKSKFKATISALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEK 1849
Cdd:TIGR02168 954 eeaealENKIEDDEEEARRRLKRLENKIKEL-GPVNLAAIEEYEELKERYDFLTAQKEdlTEAKEtlEEAIEEIDREARE 1032
|
890
....*....|..
gi 1907083614 1850 KLKEIFMQVEDE 1861
Cdd:TIGR02168 1033 RFKDTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1131-1886 |
1.12e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 145.58 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1131 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQ----QELRTKREQE--------VAELKKALE--DETKNHEAQ 1193
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEdilNELERQLKSLERQaekaERYKELKAELrelelallVLRLEELREelEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1194 IQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDR 1273
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1274 LRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ-------EETRQKLNLSSRIRQLEEEKN 1346
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1347 SLQE-----QQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKkkllkdvEALSQRLEEKVLAYDKLEKT 1421
Cdd:TIGR02168 411 RLEDrrerlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL-------EELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1422 KNRLQQELDDLTVDLDHQRQI---VSNLEKKQKKF--------DQLLAEEKGISARYAEERDRAEAEAREKETKAL---- 1486
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGYEAAIEAALGGRLQAVVVENLNAAKkaia 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1487 SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKL--- 1563
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrp 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1564 ---------------------RLEVNMQAMKAQFE-RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1621
Cdd:TIGR02168 644 gyrivtldgdlvrpggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1622 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1701
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1702 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNdrfrkttLQVDTLNTELAAERSAAQ 1781
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1782 KSDNARQQLERQNKELKAKLQELEGAVKSKFKAtISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDE 1861
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESK-RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
810 820
....*....|....*....|....*.
gi 1907083614 1862 -RRHADQYKEQMEKANARMKQLKRQL 1886
Cdd:TIGR02168 956 aEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1005-1858 |
1.90e-30 |
|
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: 131.73 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1005 EDRIAECSSQLAEEEEKAKNLAKIRNKQEvMISDLEERLKKEE-----KTRQELEKAKRKLDGETTDLQDQIAELQAQVD 1079
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1080 ELKVQLTKKEEELQGALARGDDETLHKNNALKVA-RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDT 1158
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1159 LDTTAAQQELRTKREQEVAELKKALEDEtknhEAQIQDMRQRHATALEELS---EQLEQAKRFKANLEKNKQGLETDNKE 1235
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDL----RAELEEVDKEFAETRDELKdyrEKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1236 LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLES 1315
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1316 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQeeeeearknlEKQVLALQSQLADTKKK--VDDDLGTIESLEEA 1393
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVG----------ERYATAIEVAAGNRLNNvvVEDDAVAKEAIELL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1394 KKKLL-----------KDVEALSQRLEEKV---LAYDKLE---KTKNRLQQELDDLTV--DLDHQRQIVSN--------- 1445
Cdd:TIGR02169 568 KRRKAgratflplnkmRDERRDLSILSEDGvigFAVDLVEfdpKYEPAFKYVFGDTLVveDIEAARRLMGKyrmvtlege 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1446 -LEKKQKKFDQLLAEEKGISaRYAEERDRAEAEAREKEtkalSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG 1524
Cdd:TIGR02169 648 lFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1525 KNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQTRDEQNEEKKRLLLKQVRELEAE 1604
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1605 LEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKS 1684
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1685 LEAEILQLQEELAsserarrHAEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttl 1764
Cdd:TIGR02169 873 LEAALRDLESRLG-------DLKKERDELEAQL-------RELERKIEELEAQIEKKRKRLSELKAKLEALEEE------ 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1765 qvdtlNTELAAERSAAQKSDNARQQLERQNKELKAKLQELE--GAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1842
Cdd:TIGR02169 933 -----LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
890
....*....|....*.
gi 1907083614 1843 LVRRTEKKLKEIFMQV 1858
Cdd:TIGR02169 1008 RIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1185-1934 |
7.21e-30 |
|
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: 130.18 E-value: 7.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1185 DETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKA--NLEKNKQG--LETDNKELACEVKVLQQVKAESEHKRKKLDAQ 1260
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1261 VQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQ 1340
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1341 LEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEK 1420
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1421 TKNRLQQELDDLTVDLDHQR--QIVSNLEKKQKKFDQLLAEEKGISARYAE---ERDRAEAEAREKETKALSLARALEEA 1495
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEEaeqALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1496 LEAKEEFERQNKQ----------------------------LRADMEDL-MSSKDDVGKNVHELEKS---KRALEQQVEE 1543
Cdd:TIGR02168 502 EGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVvVENLNAAKKAIAFLKQNelgRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1544 MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTR----------DEQNEEKKRLLLkqvRELEAELEDER---- 1609
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRP---GYRIVTLDGDLvrpg 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1610 ----KQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1685
Cdd:TIGR02168 659 gvitGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1686 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQleeeleeEQSNMELLNDRFRKTTLQ 1765
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-------LKEELKALREALDELRAE 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1766 VDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSkFKATISALEAKIGQLEEQLEQEAKERAAANKLVR 1845
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1846 RTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANAS-RRKLQRELDDA-------TEANEGL 1917
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAealenkiEDDEEEA 970
|
810
....*....|....*..
gi 1907083614 1918 SREVSTLKNRLRRGGPI 1934
Cdd:TIGR02168 971 RRRLKRLENKIKELGPV 987
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1054-1698 |
2.26e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.13 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1054 EKAKRKLDGETTDL---QDQIAELQAQVDELKVQ---------LTKKEEELQGALargddetlhknnALKVARELQAQIA 1121
Cdd:COG1196 175 EEAERKLEATEENLerlEDILGELERQLEPLERQaekaeryreLKEELKELEAEL------------LLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1122 ELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDEtknheaqiQDMRQRH 1201
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL--------EERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1202 ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEK 1281
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1282 ANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKN 1361
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1362 LEKQVLALQSQLADtkkkvdddlgtieslEEAKKKLLKDVEALSQRLEEKVLAYDKLEKtKNRLQQELDDLTVDldhqrq 1441
Cdd:COG1196 475 LEAALAELLEELAE---------------AAARLLLLLEAEADYEGFLEGVKAALLLAG-LRGLAGAVAVLIGV------ 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1442 ivsnlekkQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD 1521
Cdd:COG1196 533 --------EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1522 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVnmQAMKAQFERDLQTRDEQNEEKKRLLLKQVREL 1601
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT--LEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1602 EAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEiFAQSKESEKK 1681
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-ALEELPEPPD 761
|
650
....*....|....*..
gi 1907083614 1682 LKSLEAEILQLQEELAS 1698
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1671 |
1.30e-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: 125.94 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 849 RQEEELQakdeeLLKVKEKQTKVEGELEEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKK-QELEEILHDL 927
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALLVLRlEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 928 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR 1007
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1008 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTK 1087
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1088 KEEELQGALARgdDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQE 1167
Cdd:TIGR02168 405 LEARLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1168 LRTKREQEvaelkkaleDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNK-ELACE------- 1239
Cdd:TIGR02168 477 LDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalggrl 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1240 ----VKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLqnelDNVSTLLEEAEKKGIKFAKDAAGLES 1315
Cdd:TIGR02168 548 qavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI----EGFLGVAKDLVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1316 Q------LQDTQELLQEETRQ---------------------------KLNLSSRIRQLEEEKNSLQEQQEEEEEARKNL 1362
Cdd:TIGR02168 624 GvlvvddLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1363 EKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQi 1442
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA- 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1443 vsNLEKKQKKFDQLLAEEKGISARYAEERDRAEA---EAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSS 1519
Cdd:TIGR02168 783 --EIEELEAQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1520 KDDVGKNVHELE-------KSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKR 1592
Cdd:TIGR02168 861 IEELEELIEELEseleallNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-QLELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1593 LLLKQVREL-EAELEDERKQRALAVASKKKMEIDLKDLEAQIEA---ANKARDEVIKQLRKLQAQMKDYQRELEEARASR 1668
Cdd:TIGR02168 940 NLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
...
gi 1907083614 1669 DEI 1671
Cdd:TIGR02168 1020 EEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1167-1858 |
2.11e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.05 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1167 ELRTKREQevAELKkaLEdETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKA------NLEKNKQGLETDNKELacEV 1240
Cdd:COG1196 169 KYKERKEE--AERK--LE-ATEENLERLEDILGELERQLEPLERQAEKAERYRElkeelkELEAELLLLKLRELEA--EL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1241 KVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDT 1320
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1321 QELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKD 1400
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1401 VEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQivsNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEARE 1480
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE---ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1481 KETKALSLARaleealeakeefERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRaLEQQVEEMRTQLEELEDELQATED 1560
Cdd:COG1196 479 LAELLEELAE------------AAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1561 AKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKAR 1640
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1641 DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANS 1720
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1721 ASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKsdnARQQLERQNKEL--- 1797
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER---ELERLEREIEALgpv 782
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 1798 --KAkLQELEgavkskfkatisALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEKKLKEIFMQV 1858
Cdd:COG1196 783 nlLA-IEEYE------------ELEERYDFLSEQREdlEEAREtlEEAIEEIDRETRERFLETFDAV 836
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1692 |
4.19e-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: 124.40 E-value: 4.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 849 RQEEELQAKDEELLKVKEKQtkVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE 928
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 929 SRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRI 1008
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1009 AECssqlaeeeekaknlakirnkqevmisdleerlkkeektRQELEKAKRKLDgettDLQDQIAELQAQVDELKVQLtkk 1088
Cdd:TIGR02168 375 EEL--------------------------------------EEQLETLRSKVA----QLELQIASLNNEIERLEARL--- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1089 eEELQGALARGDDETLHKNNALKvarelQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQEL 1168
Cdd:TIGR02168 410 -ERLEDRRERLQQEIEELLKKLE-----EAELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1169 RTKREQevaelkkalEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNK-ELACE-------- 1239
Cdd:TIGR02168 478 DAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalggrlq 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1240 ---VKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAnklqNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1316
Cdd:TIGR02168 549 avvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIL----KNIEGFLGVAKDLVKFDPKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1317 LQDTQELLQE-ETRQKLNLSSRIRQLEEEK-----------NSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDL 1384
Cdd:TIGR02168 625 VLVVDDLDNAlELAKKLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELR 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1385 GTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDL-DHQRQIVSNLEKKQKKFDQLLAEEKGI 1463
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1464 sARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEE 1543
Cdd:TIGR02168 785 -EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1544 MRTQLEELEDELQATEDAKLRLEVNMQAmkAQFERDLQTRDEQNEEKKRlllkqvRELEAELEDERKQralavaskkkme 1623
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALAL--LRSELEELSEELRELESKR------SELRRELEELREK------------ 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1624 idLKDLEAQIEAANKARDEVIKQLRklqaqmKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1692
Cdd:TIGR02168 924 --LAQLELRLEGLEVRIDNLQERLS------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1036-1917 |
5.86e-26 |
|
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: 117.09 E-value: 5.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1036 ISDLEERLKKEEKTRQELEKAKRKLDgettdlqdqiaELQAQVDELKVQLTKKEEElqgalargddetlhKNNALKvare 1115
Cdd:TIGR02169 162 IAGVAEFDRKKEKALEELEEVEENIE-----------RLDLIIDEKRQQLERLRRE--------------REKAER---- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1116 LQAQIAELQEDFESEKASR-NKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKALEDETKNHEAQI 1194
Cdd:TIGR02169 213 YQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKL-------TEEISELEKRLEEIEQLLEELNKKIKDLG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1195 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETdnkelacevkvlQQVKAESEhkRKKLDAQVQELHAKVSEGDRL 1274
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE------------RLAKLEAE--IDKLLAEIEELEREIEEERKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1275 RVELAEKANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEE 1354
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKE-------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1355 EEEARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDdltv 1434
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA---- 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1435 DLDHQRQIVSNLEKKQKKFDQLLaeEKGISARYAEERDRAEAEarEKETKALSLAraleealeakeeferqnkqLRADME 1514
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVG--ERYATAIEVA-------------------AGNRLN 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1515 DLMSSKDDVGKNVHELEKSK---RALEQQVEEMRTQLEELEdelQATEDAKLRLEVNMQAMKAQFE-------RDlqTRD 1584
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafkyvfGD--TLV 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1585 EQNEEKKRLLLKQVR--ELEAELEDE--------RKQRALAVASKKKMEiDLKDLEAQIEAANKARDEVIKQLRKLQAQM 1654
Cdd:TIGR02169 626 VEDIEAARRLMGKYRmvTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRL 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1655 KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1734
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1735 EARIAQLEEELEEEQsnMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV------ 1808
Cdd:TIGR02169 785 EARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngk 862
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1809 KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRqLEE 1888
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-PKG 941
|
890 900
....*....|....*....|....*....
gi 1907083614 1889 AEEEATRANASRRKLQRELDDATEANEGL 1917
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
218-712 |
1.08e-25 |
|
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: 116.00 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 218 LLQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAVRQA------KDERTFHIFYQ 286
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 287 LLSGAGEH-----LKSDLLLEGFN--NYRFLSNGYIPIPG--------QQDKDNFQETMEAMHIMGFSHEEILSMLKVVS 351
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 352 SVLQFGNISFKKERNTDQASMPEN---TVAQKLCHLLGMNVME-FTRAILTPRIKV--GRDYVQKAQTKEQADFAVEALA 425
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 426 KATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQlfnh 489
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 490 tmfileqEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATD----------KTFVEKLVQEQGS 559
Cdd:cd14894 565 -------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 560 HSKfQKPRQLKDKA----------DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRivgLD 629
Cdd:cd14894 638 RLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ---LG 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 630 QVTGMTETAFGSAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIR 709
Cdd:cd14894 714 WSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQME 792
|
...
gi 1907083614 710 ICR 712
Cdd:cd14894 793 ICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1321-1886 |
2.40e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.03 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1321 QELLQEETRQKLNLSS-RIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK 1399
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1400 DVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAR 1479
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1480 EKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDdvgknvhELEKSKRALEQQVEEMRTQLEELEDELQATE 1559
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-------RLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1560 DAKLRLEvnmqamkaQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKA 1639
Cdd:COG1196 449 EEEAELE--------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1640 RdeVIKQLRKLQAQMKDYQRELEEARASR--------DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERD 1711
Cdd:COG1196 521 G--LAGAVAVLIGVEAAYEAALEAALAAAlqnivvedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1712 ELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLE 1791
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1792 RQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQ 1871
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 1907083614 1872 M---EKANARMKQLKRQL 1886
Cdd:COG1196 759 PpdlEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1706 |
1.84e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.47 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 844 LLQVTRQEEELQAKDEEllkVKEKQTKVEGELEEMERkHQQLLEEKNILA--EQLQAETELFAEAEEMRARLAAKKQELE 921
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE---KRQQLERLRREREKAER-YQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 922 EILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGarqKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEK 1001
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG---ELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1002 KLMEDRIAECSSQLAEEE-EKAKNLAKIRNKQEVM---ISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQ 1077
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERkRRDKLTEEYAELKEELedlRAELEEVDKEFAETRDELKDYREKLE----KLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1078 VD---ELKVQLTKKEEELQGALARGDDetlhKNNALKVARE-LQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT 1153
Cdd:TIGR02169 408 LDrlqEELQRLSEELADLNAAIAGIEA----KINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1154 ELE------DTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELS----------------EQ 1211
Cdd:TIGR02169 484 ELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAgnrlnnvvveddavakEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1212 LEQAKRFKAN----LEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELhakvseGDRLRVELAEKANKLQN 1287
Cdd:TIGR02169 564 IELLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF------GDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1288 ELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEEtrqklNLSSRIRQLEEEKNSLQEQqeeeeeaRKNLEKQVL 1367
Cdd:TIGR02169 638 KYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ-----RLRERLEGLKRELSSLQSE-------LRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1368 ALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLE 1447
Cdd:TIGR02169 706 ELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1448 KKQKKFDQLLAEEKGISARyaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNV 1527
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1528 HELEKSKRALEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqferDLQTRDEQNEEKKRLLLKQVRELEAELED 1607
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1608 ERKQRALAVASKKKMEIDLKDLEAQIeAANKARDEVIKQLRKLQAQMKDYQRELEE-------ARASRDEIFAQSKESEK 1680
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKE 993
|
890 900
....*....|....*....|....*.
gi 1907083614 1681 KLKSLEAEILQLQEELASSERARRHA 1706
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
807-1449 |
2.55e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 807 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRvftkvkplLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQL 885
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELE--------AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 886 LEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdlesrveeeeeRNQILQNEKKKMQAHIQDLEEQLDEEEGA 965
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--------------RLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 966 RQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKK 1045
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1046 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQE 1125
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1126 DFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATAL 1205
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1206 EELSEQLEQAKRFKANLeknkqGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKL 1285
Cdd:COG1196 586 AALAAALARGAIGAAVD-----LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1286 QNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQ 1365
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1366 VLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALsqrleEKV--LA---YDKLEKTKNRLQQELDDLTVDLDHQR 1440
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-----GPVnlLAieeYEELEERYDFLSEQREDLEEARETLE 815
|
....*....
gi 1907083614 1441 QIVSNLEKK 1449
Cdd:COG1196 816 EAIEEIDRE 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1740 |
2.77e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 111.70 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 859 EELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrarlAAKKQELEEILHDLEsrVEEEEERN 938
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-----AERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 939 QILQNEKKKMQAHIqdleeqldeeegARQKLQLEKVTAE--AKIKKMEEEVLLLEDQNSKFikeKKLMEDRIAECSSQLA 1016
Cdd:TIGR02169 233 EALERQKEAIERQL------------ASLEEELEKLTEEisELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1017 EEEEKAKNLAKIrnkqevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1096
Cdd:TIGR02169 298 ELEAEIASLERS-------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1097 ARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEV 1176
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE---AKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1177 AELKKAlEDETKNHEAQIQDMRQRH---ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLqqvkaesEHK 1253
Cdd:TIGR02169 448 LEIKKQ-EWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-------KAS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1254 RKKLDAQVQELhAKVSEGDRLRVELAekankLQNELDNVSTLLEEAEKKGIKFAKdaaglESQLQDTQELLQEETRQKLN 1333
Cdd:TIGR02169 520 IQGVHGTVAQL-GSVGERYATAIEVA-----AGNRLNNVVVEDDAVAKEAIELLK-----RRKAGRATFLPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1334 LSSRIRqleeeknslqeqqeeeeearknlEKQVLALQSQLADTKKK-------VDDDLGTIESLEEAKKKL--------- 1397
Cdd:TIGR02169 589 DLSILS-----------------------EDGVIGFAVDLVEFDPKyepafkyVFGDTLVVEDIEAARRLMgkyrmvtle 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1398 ----------------LKDVEALSQRLEEKVLAY----DKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK----QKKF 1453
Cdd:TIGR02169 646 gelfeksgamtggsraPRGGILFSRSEPAELQRLrerlEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEI 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1454 DQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFErqnkQLRADMEDLMSSKDDVGknVHELEKS 1533
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH----KLEEALNDLEARLSHSR--IPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1534 KRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRA 1613
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1614 LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE------SEKKLKSLEA 1687
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQA 958
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1688 EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:TIGR02169 959 ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1106-1881 |
3.40e-24 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 111.36 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1106 KNNALKVARELQAQIAELQEDFESekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALED 1185
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1186 ETKNHEAQiqdmRQRHATALEELSEQLEQAKRFKANLEKNKQGLETD--NKELACEVKVLQQVKAESEHKR--------- 1254
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvDFEEASGKKIYEHDSMSTMHFRslgsaiski 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1255 -KKLDAQVQELHAKV-SEGDRLRVELAEKANK----LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ---LQDTQELLQ 1325
Cdd:pfam15921 226 lRELDTEISYLKGRIfPVEDQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1326 EETRQKLnlSSRIRQLEEeknslqeqqeeeeearknLEKQVLALQSQLADTKKKVDDdlgTIESLEeaKKKLLKDVEALS 1405
Cdd:pfam15921 306 EQARNQN--SMYMRQLSD------------------LESTVSQLRSELREAKRMYED---KIEELE--KQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1406 QRLEEkvlayDKLEKTKNRLQQELDDLTVDLdHQRQIVSNLEKKQKKfdQLLAEEKGISARYAEERdraeaeaREKETKA 1485
Cdd:pfam15921 361 ARTER-----DQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNK--RLWDRDTGNSITIDHLR-------RELDDRN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1486 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRL 1565
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1566 EVNMQAMKAqferdlqTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKD-----LEAQIE-----A 1635
Cdd:pfam15921 506 QEKERAIEA-------TNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDkvieiLRQQIEnmtqlV 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1636 ANKARDEVIKQLRK--LQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1713
Cdd:pfam15921 579 GQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1714 ADEIANSASGKSALLDEkrrleariaqleeeleeeqsnMELLNDRFRKTTLQVDT----LNTELAAERSAAQKSDNARQQ 1789
Cdd:pfam15921 659 LNEVKTSRNELNSLSED---------------------YEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLKS 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1790 LERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERaaanKLVRRTEKKLKEIFMQVEDERRHADQYK 1869
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVATEKNKMAGEL 792
|
810
....*....|..
gi 1907083614 1870 EQMEKANARMKQ 1881
Cdd:pfam15921 793 EVLRSQERRLKE 804
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1544 |
5.28e-23 |
|
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: 107.45 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 925
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 926 DLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ-----LEKVTAEAKIKKMEEEVLLLEDQNSKFIKE 1000
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieeLLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1001 KKLMEDRIAECSSQLAEEEEK----AKNLAKIRNKQEvMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI---AE 1073
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQAldaaERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1074 LQAQVDelkvqlTKKEEELQGALARGDD------ETLHKNNALKVA---------RELQAQIAELQEDFESEKASRNKAE 1138
Cdd:TIGR02168 535 YEAAIE------AALGGRLQAVVVENLNaakkaiAFLKQNELGRVTflpldsikgTEIQGNDREILKNIEGFLGVAKDLV 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1139 KQKRDLSEELEAL--KTELEDTLDTTAAQQEL-------------------------------RTKREQEVAELKKALEd 1185
Cdd:TIGR02168 609 KFDPKLRKALSYLlgGVLVVDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIE- 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1186 ETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELH 1265
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1266 AKVSEGDRLRVELAEKANKLQNELDNVSTLLEEaekkgikfakdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1345
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKA--------------LREALDELRAELTLLNEEAANLRERLESLERRI 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1346 NSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRL 1425
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEEL-------IEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1426 QQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKG-ISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFER 1504
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1907083614 1505 QNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1544
Cdd:TIGR02168 987 VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1131-1740 |
1.95e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.40 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1131 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQ-------QELRTKREQEVAELKKALEDETKNHEAQIQDMRQR 1200
Cdd:COG1196 171 KERKEEAERKLEATEENLERLEdilGELERQLEPLERQaekaeryRELKEELKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1201 HATALEELSEQLEQAkrfKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAE 1280
Cdd:COG1196 251 LEAELEELEAELAEL---EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1281 KANKLQNELDNVSTL----------LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQE 1350
Cdd:COG1196 328 LEEELEELEEELEELeeeleeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1351 QQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELD 1430
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1431 DLTVDLDHQRQIVSNLEKKQK--KFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA----RALEEALEAKEEFER 1504
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALqnivVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1505 QNKQLRA------DMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFER 1578
Cdd:COG1196 568 AAKAGRAtflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1579 DLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ 1658
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1659 RELEEARASRDEIFAQSK----ESEKKLKSLEAEILQLQEELASSERARRH-------AEQERDELADEIANSASGKSAL 1727
Cdd:COG1196 728 EQLEAEREELLEELLEEEelleEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDL 807
|
650
....*....|...
gi 1907083614 1728 LDEKRRLEARIAQ 1740
Cdd:COG1196 808 EEARETLEEAIEE 820
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1314-1930 |
5.04e-21 |
|
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: 101.02 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1314 ESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEeeeeARKNLEKQVLALQSQLADTKKKVDDDLGTIES---- 1389
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ----AETELCAEAEEMRARLAARKQELEEILHELESrlee 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1390 -------LEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEekg 1462
Cdd:pfam01576 87 eeersqqLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1463 isaryaeerdrAEAEAREKETKALSLARALEealeakeeferQNKQLRADMEDLMSSKDdvgKNVHELEKSKRALEQQVE 1542
Cdd:pfam01576 164 -----------FTSNLAEEEEKAKSLSKLKN-----------KHEAMISDLEERLKKEE---KGRQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1543 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKM 1622
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1623 EIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELE-EARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1701
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1702 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQ 1781
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1782 KSDNARQQLERQNKELKAKLQElEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDE 1861
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1862 RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:pfam01576 537 AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1720 |
1.23e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.22 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 849 RQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEleEILHDLE 928
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE--EVRKAEE 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 929 SRVEeeeernqilQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRI 1008
Cdd:PTZ00121 1193 LRKA---------EDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1009 AECSSQLAEEEEKAKNLAKIRNKQEVMISDleERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvqltKK 1088
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK----KK 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1089 EEELQGALARGDDETLHKNNALKVARElQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQEL 1168
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1169 RTKREqevaELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelACEVKVLQQVKA 1248
Cdd:PTZ00121 1417 KKKAD----EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKKADEAKK 1490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1249 ESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNEldnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEET 1328
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--------EEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1329 RQKlnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTK----KKVDDDLGTIESLEEAKKKlLKDVEAL 1404
Cdd:PTZ00121 1563 KKK---AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELKKAEEE-KKKVEQL 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1405 SQRLEEKVLAYDKLEKTknrlqqelddltvdlDHQRQIVSNLEKKQKKFDQLLAEEkgisARYAEERDRAEAEAREKETK 1484
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---------------EEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKEAE 1699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1485 AlslARALEEALEAKEEFERQNKQLRADMEDLMSskddvgkNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLR 1564
Cdd:PTZ00121 1700 E---AKKAEELKKKEAEEKKKAEELKKAEEENKI-------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1565 LEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEidlkdleaqieaankarDEVI 1644
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-----------------DSAI 1832
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1645 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSleaEILQLQEELASSERARRHAEQERDELADEIANS 1720
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNK---EKDLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1596-1886 |
2.21e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.86 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1596 KQVRELEAELEdeRKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQS 1675
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1676 KESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL 1755
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1756 NDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAK 1835
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1836 ERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1886
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
847-1716 |
2.36e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 95.42 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 847 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlAAKKQELEEILHD 926
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 927 LESRVEEEEERNQILQNEKKKMQAHIqdleeqldeeegarQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED 1006
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1007 RIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKrkldgettDLQDQIAELQAQVDELKVQLT 1086
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE--------EELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1087 KKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDF-ESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaq 1165
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLlKEEKKEELEILEEEEESIELKQGKLTEEKEELEK---- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1166 QELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQ 1245
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1246 VKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ 1325
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1326 EETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALS 1405
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEIL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1406 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgisaryaeerdrAEAEAREKETKA 1485
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE------------EEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1486 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRL 1565
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELK 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1566 EVNMQAMKAQFE-RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVI 1644
Cdd:pfam02463 844 EEQKLEKLAEEElERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 1645 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKsleaEILQLQEELASSERARRHAEQERDELADE 1716
Cdd:pfam02463 924 KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN----KRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1314-1930 |
2.47e-18 |
|
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: 92.43 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1314 ESQLQDTQELLQeetRQKLNLSSRIRQLE--EEKNSLQEQQEEEEEARKNLEKQVLALQsqLADTKKKVDDDLGTIESLE 1391
Cdd:TIGR02168 178 ERKLERTRENLD---RLEDILNELERQLKslERQAEKAERYKELKAELRELELALLVLR--LEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1392 EAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTvdldhqrQIVSNLEKKQKKFDQLLAEEKGISARYAEER 1471
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-------NEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1472 DRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEEL 1551
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1552 EDELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEA 1631
Cdd:TIGR02168 406 EARLERLEDRRERL-----------------QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1632 QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK--LKSLEAEILQLQE--ELASSERARRHAE 1707
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgILGVLSELISVDEgyEAAIEAALGGRLQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1708 Q---ERDELADEI----ANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQ--------------V 1766
Cdd:TIGR02168 549 AvvvENLNAAKKAiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1767 DTLNTELAAERS-----------------------AAQKSDNARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKI 1823
Cdd:TIGR02168 629 DDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAEL-EKALAELRKEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1824 GQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKL 1903
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
650 660
....*....|....*....|....*..
gi 1907083614 1904 QRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTL 814
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
850-1420 |
3.26e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 91.66 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 850 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEqLQAETElfaEAEEMRARLAAKKQELEEILHDLES 929
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELE---SLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 930 RVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARqKLQLEKVTAEAKIKKMEEEVLLLEDQNSkfikEKKLMEDRIA 1009
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1010 ECSSQLAEEEEKAKNLAKIRNKQEVMisdleERLKKEEKTR---------QELEKAKRKLDGETTDLQDQIAELQAQVDE 1080
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEEL-----ERLKKRLTGLtpeklekelEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1081 LKvqltKKEEELQGAlargddetlhKNNALKVARELQAQiaELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1160
Cdd:PRK03918 424 LK----KAIEELKKA----------KGKCPVCGRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1161 TTAAQQELRtkREQEVAELKKALEDETKNHEAQiqdmrqrhatALEELSEQLEQAKRFKANLEKNKQGLETD---NKELA 1237
Cdd:PRK03918 488 VLKKESELI--KLKELAEQLKELEEKLKKYNLE----------ELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEELK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1238 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKfakdaagLESQL 1317
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-------LEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1318 QDTQELLQEETRQKLNLSSRIRQL-----EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEE 1392
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
570 580 590
....*....|....*....|....*....|
gi 1907083614 1393 AKKKLLKDVEALS--QRLEEKVLAYDKLEK 1420
Cdd:PRK03918 709 AKKELEKLEKALErvEELREKVKKYKALLK 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1484 |
9.79e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 845 LQVTRQEEELQaKDEELLKVKEKQTKVEGELEEMERKHQQLLE-EKNILAEQLQAETELFAEAEEmrARLAAKKQELEEI 923
Cdd:PTZ00121 1178 AEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEE--AKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 924 LHDLESRVEEEEERNQILQNEKKKM-----QAHIQDLEEQLDEEEGARQKLQLEKVTAEAK----IKKMEEEVLLLEDQN 994
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKadelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 995 SKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKK--EEKTRQELEKAKRKLDGETTDLQDQIA 1072
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1073 ELQAQVDEL--KVQLTKKEEEL--QGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKAS--RNKAEKQKRDlSE 1146
Cdd:PTZ00121 1415 AAKKKADEAkkKAEEKKKADEAkkKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeAKKADEAKKK-AE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1147 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataleelSEQLEQAKRFKANLEKNK 1226
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--------ADELKKAEELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1227 qgleTDNKELACEVKVLQQVKAESEHKRKKldAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTllEEAEKKGIKF 1306
Cdd:PTZ00121 1566 ----AEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEEKKKVEQ 1637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1307 AKDAAglESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlalQSQLADTKKKVdddlgt 1386
Cdd:PTZ00121 1638 LKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-----LKKEAEEAKKA------ 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1387 iESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISAR 1466
Cdd:PTZ00121 1705 -EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
650
....*....|....*...
gi 1907083614 1467 YAEERDRAEAEAREKETK 1484
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
977-1576 |
1.70e-17 |
|
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: 88.92 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 977 EAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKA 1056
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1057 KRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEEL---QGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKAS 1133
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1134 RNKAEKQKRDLSEELEALKTELEDT----LDTTAAQQELRTKREQEVAELKKAlEDETKNHEAQIQDMRqrhaTALEELS 1209
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTqtqlNQLKDEQNKIKKQLSEKQKELEQN-NKKIKELEKQLNQLK----SEISDLN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1210 EQLEQ--AKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKkldaqvqELHAKVSEGDRLRVELAEKANKLQN 1287
Cdd:TIGR04523 302 NQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-------ELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1288 ELDNVSTLLEEAEKKGIKFAKdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVL 1367
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQIND----LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1368 ALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLE 1447
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1448 KKQKKFDQLLA--EEKGISARYAEERDRAEAEAREKETKALSLaraleeaLEAKEEFERQNKQLRADMEDLMSSKDDVGK 1525
Cdd:TIGR04523 531 SEKKEKESKISdlEDELNKDDFELKKENLEKEIDEKNKEIEEL-------KQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1526 NVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF 1576
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1203-1922 |
1.94e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 89.20 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1203 TALEELSEQLEQAKRFKANLEKNKQgletdnkelacEVKVLQQVKAESEhKRKKLDAQVQELHAkvsEGDRLRVELAE-K 1281
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDARE-----------QIELLEPIRELAE-RYAAARERLAELEY---LRAALRLWFAQrR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1282 ANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLS-SRIRQLEEEKNSLQEQQEEEEEARK 1360
Cdd:COG4913 290 LELLEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1361 NLEKQVLALQSQLADTKkkvdddlgtiESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQR 1440
Cdd:COG4913 363 RLEALLAALGLPLPASA----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1441 QIVSNLEKKQKKFDQLLAEEKGISA---RYA------EERDRAEAEAREKE--TKALSLARALEEALEAKEEFERQNKQL 1509
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEaelPFVgelievRPEEERWRGAIERVlgGFALTLLVPPEHYAAALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1510 RADMEdlmsskdDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAtedaklRLEVNMQAMKAQFERDLQTrdeqneE 1589
Cdd:COG4913 513 RLVYE-------RVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDYVCVDSPEELRR------H 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1590 KKRL----LLKQVRELeAELEDERKQRALAV----ASKKkmeidLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1661
Cdd:COG4913 574 PRAItragQVKGNGTR-HEKDDRRRIRSRYVlgfdNRAK-----LAALEAELAELEEELAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1662 EEARAsrdeiFAQSKESEKKLKSLEAEILQLQEELASSERAR---RHAEQERDELADEIANSASGKSALLDEKRRLEARI 1738
Cdd:COG4913 648 EALQR-----LAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1739 AQLEEELEEEQSNMELLNDRFRK-TTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV---KSKFKA 1814
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMrafNREWPA 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1815 TISALEAKIGQLEE------QLEQE---AKERAAANKLVRRTEKKLKEIFMQVEDERRHAdqyKEQMEKANARMKQLK-- 1883
Cdd:COG4913 803 ETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRIPfg 879
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1907083614 1884 --RQLeeAEEEATRANASRRKLQRELDDATEANEGLSREVS 1922
Cdd:COG4913 880 pgRYL--RLEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
828-1396 |
2.14e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.43 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 828 KLRHWQWWRVFTKVKPLLQVTRQ---EEELQAKDEELLKVKEKQTKVEGELEEMERKhqqlLEEKNILAEQLQAETELFA 904
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 905 EAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAK----- 979
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaee 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 980 IKKMEEEVLLLEDQNSKFIKEKKLMED-RIAECSSQLAEEEEKAKNLAKirnKQEVMISDLEERLKKEEKTRQELEKAKR 1058
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1059 KLDGETTDLQDQIAELQAQVDELK--VQLTKKEEELQGALARGDDETLHKNNALKVARELQaQIAELQEDFESEKASRNK 1136
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1137 AEKQKRdlseELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATAlEELSEQLEQAK 1216
Cdd:PTZ00121 1559 KAEEKK----KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKK 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1217 RF----KANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQElhakvsEGDRLRVELAEKANKLQNELDNV 1292
Cdd:PTZ00121 1634 KVeqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKKEAEEAKKAEEL 1707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1293 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQ 1372
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
570 580 590
....*....|....*....|....*....|...
gi 1907083614 1373 LADTK---------KKVDDDLGTIESLEEAKKK 1396
Cdd:PTZ00121 1784 ELDEEdekrrmevdKKIKDIFDNFANIIEGGKE 1816
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
855-1555 |
4.59e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.81 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 855 QAKDEELLKVKEKQTKVEGE---LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH---DLE 928
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQilgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 929 SRVEEEEERNQILQNEKKKMQAHiqdleeqldeeEGARQKLQLEKVTAEAKIKKMEEEVllledqnskfikekKLMEDRI 1008
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEEL-----------KEEIEELEKELESLEGSKRKLEEKI--------------RELEERI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1009 AECSSQLAEEEEKAKNLAKIRNKQEVMISdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvQLTKK 1088
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1089 EEELQGALARgdDETLHKnnALKVARELQAQIAELqedfeSEKASRNKAEKQKRDLsEELEALKTELEDTLDTTAAQqel 1168
Cdd:PRK03918 347 LKELEKRLEE--LEERHE--LYEEAKAKKEELERL-----KKRLTGLTPEKLEKEL-EELEKAKEEIEEEISKITAR--- 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1169 RTKREQEVAELKKALEdetknheaQIQDMRQRHATALEELSEqlEQAKRFKAnleknkqgletdnkELACEVKVLQQVKA 1248
Cdd:PRK03918 414 IGELKKEIKELKKAIE--------ELKKAKGKCPVCGRELTE--EHRKELLE--------------EYTAELKRIEKELK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1249 ESEHKRKKLDAQVQELHAKVSEGDRLRV--ELAEKANKLQNELDNVStlLEEAEKKGIKFakdaaglesqlqdtqellqE 1326
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYN--LEELEKKAEEY-------------------E 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1327 ETRQKLN-LSSRIRQLEEEKNSLQEQQEEeeeaRKNLEKQVLALQSQLADTKKKvdddlgtiesLEEAKKKLLKDVEALS 1405
Cdd:PRK03918 529 KLKEKLIkLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKE----------LEELGFESVEELEERL 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1406 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEErdraeaEAREKETKA 1485
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEY 668
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1486 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEqQVEEMRTQLEELEDEL 1555
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1387-1930 |
7.31e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.02 E-value: 7.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1387 IESLEEAKKKLLKDVEALSQRLEEKVLaYDKLektkNRLQQELDDLTVDLDHqrqivsnLEKKQKKFDQLLAEEKGISAR 1466
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDL-HERL----NGLESELAELDEEIER-------YEEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1467 YAEERDRAE------AEAREK----ETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRA 1536
Cdd:PRK02224 246 HEERREELEtleaeiEDLRETiaetEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1537 LEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK---AQFERDLQTRDEQNEEKKrlllKQVRELEAELEDERKQRA 1613
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRR----EEIEELEEEIEELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1614 LAvaskkkmEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDE--------------IFAQSKESE 1679
Cdd:PRK02224 402 DA-------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1680 KKLKSLEAEILQLQEELASSErarrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRf 1759
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1760 rkttlqVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfkATISALEAKIGQLEEQLEqeakeraa 1839
Cdd:PRK02224 546 ------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIE-------- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1840 anklvRRTEKKlkEIFMQVEDERRhadqykEQMEKANARMKQLKRQ-----LEEAEEEATRANASRRKLQRELDDATEAN 1914
Cdd:PRK02224 610 -----RLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER 676
|
570
....*....|....*.
gi 1907083614 1915 EGLSREVSTLKNRLRR 1930
Cdd:PRK02224 677 DDLQAEIGAVENELEE 692
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
942-1873 |
9.03e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.95 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 942 QNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKME-------EEVLLLEDQNSKFIKEKKLmedriaecSSQ 1014
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLkekleleEEYLLYLDYLKLNEERIDL--------LQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1015 LAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLdgettdLQDQIAELQAQVDELKVQLTKKEEELQG 1094
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1095 ALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQ 1174
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1175 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEqakrfKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKR 1254
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-----SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1255 KKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNL 1334
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1335 SSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLA 1414
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1415 YDKLEKTKNRLQQELDDlTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEE 1494
Cdd:pfam02463 634 LTKLKESAKAKESGLRK-GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1495 ALEAKEEFERQNKQLRADMEDLmsskddvgknvhelekSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1574
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKI----------------NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1575 QFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQaqm 1654
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE--- 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1655 kdyqrelEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIansasgkSALLDEKRRL 1734
Cdd:pfam02463 854 -------EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL-------NLLEEKENEI 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1735 EARIAQLEEELeeeqsnmellndrfrkttLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA 1814
Cdd:pfam02463 920 EERIKEEAEIL------------------LKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1815 TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQME 1873
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
980-1795 |
1.11e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 980 IKKMEEevLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRK 1059
Cdd:PTZ00121 1026 IEKIEE--LTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1060 LDGETTDLQDQIAELQAQV---DELKVQLTKKEEELQGAL-ARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1135
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKkaeDARKAEEARKAEDARKAEeARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARK 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1136 KAEKQKRDlseelEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQA 1215
Cdd:PTZ00121 1184 AEEVRKAE-----ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1216 KRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRvELAEKANKLQNELDNVSTL 1295
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1296 LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlssrirqlEEEKNSLQEQQEEEEEARKNLEkqvlaLQSQLAD 1375
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----------EEAKKKADAAKKKAEEKKKADE-----AKKKAEE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1376 TKKKVDDdlgtIESLEEAKKKllkdVEALSQRLEEKVLAyDKLEKtKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQ 1455
Cdd:PTZ00121 1403 DKKKADE----LKKAAAAKKK----ADEAKKKAEEKKKA-DEAKK-KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1456 LLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKE-EFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK 1534
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1535 RALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLK--QVRELEAELEDERKQR 1612
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEK 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1613 ALAVASKKKMEIDLKDLEA--QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK---LKSLEA 1687
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeeLKKKEA 1712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1688 EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRrleaRIAQLEEELEEEQSNMELLNDRFRKTTLQVD 1767
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
810 820
....*....|....*....|....*...
gi 1907083614 1768 TLNTELAAERSAAQKSDNARQQLERQNK 1795
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1114-1721 |
5.98e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.20 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1114 RELQAQIAELQEDFESEKASRNKAEK--QKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDEtknHE 1191
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA---EL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1192 AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKE-LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSE 1270
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1271 GDRlrvELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQEllqeetrqklnlssRIRQLEEEKNSLQE 1350
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEE-------ALAEAEAALRDLRR--------------ELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1351 QqeeeeeaRKNLEKQVLALQSQLADTKKKVDDDL-----------------GTIESL-----------EEAKKKLLKDVE 1402
Cdd:COG4913 434 R-------KSNIPARLLALRDALAEALGLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvpPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1403 ALSQRLE---EKVLAYDKLEKT-----------------------KNRLQQELDDLTVD----LDHQR-------QIVSN 1445
Cdd:COG4913 507 RLHLRGRlvyERVRTGLPDPERprldpdslagkldfkphpfrawlEAELGRRFDYVCVDspeeLRRHPraitragQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1446 LEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKEtKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG- 1524
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1525 --KNVHELEKSKRALEQ---QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVR 1599
Cdd:COG4913 666 aeREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1600 ELEAELEDERKQRALAVASKKKMEidlkDLEAQIEAANKARDEVIKQLRKLqaqMKDYQRELEEARASRDEIFAQSKESE 1679
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYL 818
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1907083614 1680 KKLKSLEAEIL-QLQEELAssERARRHAEQERDELADEIANSA 1721
Cdd:COG4913 819 ALLDRLEEDGLpEYEERFK--ELLNENSIEFVADLLSKLRRAI 859
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
966-1593 |
9.20e-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: 9.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 966 RQKLQLEKVTAEA-KIKKMEEEVLLLEDQNSKF-----IKEKKLMEDRIAECSSQLAEEEEKaknlakirnkqevmISDL 1039
Cdd:COG4913 249 EQIELLEPIRELAeRYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAE--------------LERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1040 EERLKKEEKTRQELEKAKRKLDGettdlqDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQ 1119
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1120 IAELQEDFESEKAS----RNKAEKQKRDLSEELEALKTELEdtldttaaqqELRTKR---EQEVAELKKALEDETKNHEA 1192
Cdd:COG4913 389 AAALLEALEEELEAleeaLAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1193 QIQ------DMRQRHA---TALEEL-----------SEQLEQAKRFkanLEKNKQGLETdnkelacevkVLQQVKAESEH 1252
Cdd:COG4913 459 ELPfvgeliEVRPEEErwrGAIERVlggfaltllvpPEHYAAALRW---VNRLHLRGRL----------VYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1253 -KRKKLDAQ--VQELHAKVSE-GDRLRVELAEKANKLQneLDNVSTLleEAEKKGI-----------KFAKDAagleSQL 1317
Cdd:COG4913 526 pERPRLDPDslAGKLDFKPHPfRAWLEAELGRRFDYVC--VDSPEEL--RRHPRAItragqvkgngtRHEKDD----RRR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1318 QDTQELLQEETRQKLN-LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ--SQLADTKKKVDDDLGTIESLEEAK 1394
Cdd:COG4913 598 IRSRYVLGFDNRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1395 KKLLK---DVEALSQRLEEKVLAYDKLEKTKN-------RLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgis 1464
Cdd:COG4913 678 ERLDAssdDLAALEEQLEELEAELEELEEELDelkgeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER--- 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1465 aRYAEERDRAEAEAREKETKALSLARaleealeakeefeRQNKQLRADMEDLMSS-KDDVGKNVHELEKSKRALEqQVEE 1543
Cdd:COG4913 755 -FAAALGDAVERELRENLEERIDALR-------------ARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLA 819
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1544 MRTQLEelEDEL-QATEDAKLRLEVNMQAMKAQFERDLqtRDEQNEEKKRL 1593
Cdd:COG4913 820 LLDRLE--EDGLpEYEERFKELLNENSIEFVADLLSKL--RRAIREIKERI 866
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1204-1929 |
9.54e-16 |
|
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: 83.58 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1204 ALEELSEQLEQAKRFKANLEKNKQGLET--DNKELACEVKVLQQVKAESE-----HKRKKLDAQVQELHAKVSEGDRLRV 1276
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERlrREREKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1277 ELAEKANKLQNELDNVSTLLEEAEKK--------GIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1348
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKikdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1349 QEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQE 1428
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1429 LDDLTVDLDHQRQIVSNLEKKQKKFDqllaeekgisaryaEERDRAEAEAREKETKALSLAraleealEAKEEFERQNKQ 1508
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWKLEQLA-------ADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1509 LRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAT-----------EDAKLRLEV----NMQAMK 1573
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgERYATAIEVaagnRLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1574 AQFERDLQTRDEQNEEKKR-----LLLKQVRELEAELEDERKQRALAVAskkkmeIDLKDLEAQIEAANK--ARDEVIKQ 1646
Cdd:TIGR02169 554 VEDDAVAKEAIELLKRRKAgratfLPLNKMRDERRDLSILSEDGVIGFA------VDLVEFDPKYEPAFKyvFGDTLVVE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1647 ----LRKL--QAQMKDYQRELEE--------ARASRDEIFAQSKESEKkLKSLEAEILQLQEELASSERARRHAEQERDE 1712
Cdd:TIGR02169 628 dieaARRLmgKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1713 LadeiansasgKSALLDEKRRLEARiaqleeeleeeQSNMELLNDRFRKttlqvdtLNTELAAERSAAQKSDNARQQLER 1792
Cdd:TIGR02169 707 L----------SQELSDASRKIGEI-----------EKEIEQLEQEEEK-------LKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1793 QNKELKAKLQELEgAVKSKFKATISALEAKIG-----QLEEQLEQEAKERAAANKLVRRTEKKLKEIFM---QVEDERRH 1864
Cdd:TIGR02169 759 ELKELEARIEELE-EDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQE 837
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1865 ADQY----KEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELddateanEGLSREVSTLKNRLR 1929
Cdd:TIGR02169 838 LQEQridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL-------GDLKKERDELEAQLR 899
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
844-1429 |
3.52e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 844 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELE----EMERKHQQLLEEK-NILAEQLQAETELFAEAEEMRARLAAKKQ 918
Cdd:PRK02224 158 LLQLGKLEEYRERASDARLGVERVLSDQRGSLDqlkaQIEEKEEKDLHERlNGLESELAELDEEIERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 919 ELEEILHDLESRveeeEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLL-------LE 991
Cdd:PRK02224 238 EADEVLEEHEER----REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 992 DQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI 1071
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1072 AELQAQVDELKVQLTKKEEELQGALARGDDetLHKNNA-----LKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSE 1146
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDE--LREREAeleatLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1147 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAlEDETKNHEAQIQDMRQRHATALEELSEQLEQAkrfkANLEKNK 1226
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERA----EELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1227 QGLEtdnkelacevkvlqqvkAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNeLDNVSTLLEEAEKKGikf 1306
Cdd:PRK02224 547 AELE-----------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE--- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1307 aKDAAGLESQLQDTQElLQEETRQKL-NLSSRIRQLEEEKNslQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLG 1385
Cdd:PRK02224 606 -DEIERLREKREALAE-LNDERRERLaEKRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1386 TIESLEEAKKKL------LKDVEALSQRLEEKVLAYDKLEKTKNRLQQEL 1429
Cdd:PRK02224 682 EIGAVENELEELeelrerREALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1280-1886 |
3.52e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.65 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1280 EKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEAR 1359
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1360 KNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKL--LKDVEALSQRLEEKVLAYDKLEK-------TKNRLQQELD 1430
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELKEKAEEYIKLSEfyeeyldELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1431 DLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKAlslaraleealeakeeferQNKQLR 1510
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-------------------ELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1511 ADMEDLmsSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFERDLQTRDEQNEEK 1590
Cdd:PRK03918 379 KRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1591 KRLLlkqvRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKAR--DEVIKQLRKLQAQMKDYQRE-LEEARAS 1667
Cdd:PRK03918 451 KELL----EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1668 RDEIFAQSKESEKKLKSLEAEILQLQE---ELASSERARRHAEQERDELADEIANSASGKSALLDEKrrleariaqleee 1744
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEER------------- 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1745 leeeQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG 1824
Cdd:PRK03918 594 ----LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 1825 QLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEdERRHADQYKEQMEKANARMKQLKRQL 1886
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKV 730
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
846-1693 |
5.91e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 81.25 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLleeKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 925
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI---KALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 926 DLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfikekklme 1005
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATR------------ 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1006 driaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQL 1085
Cdd:TIGR00606 377 -------LELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1086 TKKEEELQGALARGDDETLHKNNALKVARELQAQIAELqedfesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ 1165
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1166 QELRTKREQEVAELKKALEDETKNHEaQIQDMRQRHATALEELSEQLEQAKRFKA---NLEKNKQGLETDNKELACEVKV 1242
Cdd:TIGR00606 524 MEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQTRDRLAKLNKELAS 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1243 LQQVKAESEHKRKKLDAQVQELHAKVSEgdrlrvelAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQE 1322
Cdd:TIGR00606 603 LEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTD 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1323 -------LLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKK 1395
Cdd:TIGR00606 675 enqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1396 KLLKDVEALSQRLEEKvlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1475
Cdd:TIGR00606 755 KVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1476 AEarEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEleksKRALEQQVEEMRTQLEELEDEL 1555
Cdd:TIGR00606 831 KQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLVELSTEVQSLIREI 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1556 QATEDAKLRLEVNMQAMKAQFERDLQTRDEQN---EEKKRLLLKQVRELEAELED-ERKQRALAVASKKKMEIDLKDLEA 1631
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETSNkkaQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELNTVNA 984
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083614 1632 QIEAANKARDEVIKQLRKLQAQM--KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQ 1693
Cdd:TIGR00606 985 QLEECEKHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1257-1828 |
6.06e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.85 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1257 LDAQVQELHAKvsegdrlrvELAEKANKLQNELDNVSTLLEEAEKKgikfaKDAAglESQLQDTQELLQ--EETRQklnl 1334
Cdd:PRK02224 192 LKAQIEEKEEK---------DLHERLNGLESELAELDEEIERYEEQ-----REQA--RETRDEADEVLEehEERRE---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1335 ssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIEsLEEAkkkllkDVEALSQRLEEkvla 1414
Cdd:PRK02224 252 --ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-LDDA------DAEAVEARREE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1415 ydkLEKTKNRLQQELDDLTVDL-DHQRQIvsnlekkqkkfdqllaeekgisARYAEERDRAEAEAREKETKALSLARALE 1493
Cdd:PRK02224 319 ---LEDRDEELRDRLEECRVAAqAHNEEA----------------------ESLREDADDLEERAEELREEAAELESELE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1494 EALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK 1573
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1574 A-------QFERDLQTRDEQNEekkrlllkQVRELEAELEDERKQRAlAVASKKKMEIDLKDLEAQIEAANKARDEVIKQ 1646
Cdd:PRK02224 454 CpecgqpvEGSPHVETIEEDRE--------RVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1647 LRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADeIANSASGKSA 1726
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIAD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1727 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqVDTLNTELAAERSAAQKSDnaRQQLERQNKELKAKLQELEg 1806
Cdd:PRK02224 604 AEDEIERLREKREALAELNDERRERLAEKRER-------KRELEAEFDEARIEEARED--KERAEEYLEQVEEKLDELR- 673
|
570 580
....*....|....*....|..
gi 1907083614 1807 AVKSKFKATISALEAKIGQLEE 1828
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELEE 695
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1125-1866 |
1.19e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1125 EDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQrhata 1204
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----- 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1205 lEELSEQLEQAKRfkanLEKNKQGLETDNkelACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1284
Cdd:PTZ00121 1166 -AEEARKAEDAKK----AEAARKAEEVRK---AEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1285 LQNELDNVstlleEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNSlqeqqeeeEEARKNLEK 1364
Cdd:PTZ00121 1238 DAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKA--------DEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1365 QVLALQSQLADTKKKVDDdlgTIESLEEAKKKllkdVEALSQRLEEKvlaYDKLEKTKNRLQQELDDLTVDLDHQRQIVS 1444
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADE---AKKKAEEAKKK----ADAAKKKAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1445 NLEKKQKKFDQllAEEKGISARYAEERDRAEAEAREK--ETKALSLARALEEALEAKEEFERQNKQLRADMEDlmSSKDD 1522
Cdd:PTZ00121 1372 KKEEAKKKADA--AKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE--AKKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1523 VGKNVHELEKSKRALEQQVEEMRT--QLEELEDELQATEDAKLRLEVNMQamKAQFERDLQTRDEQNEEKKRLLLKQVRE 1600
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1601 LEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1680
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1681 KLKSLEA----EILQLQEELASSERARRHAEQERDELADEIANS---------ASGKSALLDEKRRLEARIAQLEEELEE 1747
Cdd:PTZ00121 1606 KMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1748 EQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQqlERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLE 1827
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE--ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907083614 1828 EQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHAD 1866
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
840-1432 |
3.07e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.86 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 840 KVKPLLQVTRQEEELQAKDEELL-KVKEKQTKVEGELEEMER--KHQQLLEEKNILAEQLQAETELFA-EAEEMRARLAA 915
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHtELQSKMRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRdAHEVATSIREI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 916 KKQELEEI--LHDLESRVEEEEERNQILQNEKKKMQAhiqdLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQ 993
Cdd:TIGR00618 371 SCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDILQR----EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 994 NSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIrnkqevmisdleerLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1073
Cdd:TIGR00618 447 ITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI--------------HLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1074 LQAqvdelKVQLTKKEEELQGALARGDDETLHKNNALKVAR----ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELE 1149
Cdd:TIGR00618 513 PNP-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1150 ALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKN-----HEAQIQDMRQRHATALEELSEQL------EQAKRF 1218
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLqdvrlHLQQCSQELALKLTALHALQLTLtqervrEHALSI 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1219 KANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLdaqvQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEE 1298
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL----RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1299 AEKKGIKFAKDA--AGLESQLQDTQELL------QEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1370
Cdd:TIGR00618 744 SLKELMHQARTVlkARTEAHFNNNEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 1371 SQLADTKKKVDDDLgtiesleEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDL 1432
Cdd:TIGR00618 824 ETLVQEEEQFLSRL-------EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
970-1567 |
3.64e-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: 78.62 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 970 QLEKVTAEAKiKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKI-----RNKQEVMISDLEERLK 1044
Cdd:pfam15921 246 QLEALKSESQ-NKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiqeqaRNQNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1045 KEEKTRQELEKAKRKLDGettdlqdqiaelqaQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1124
Cdd:pfam15921 325 TVSQLRSELREAKRMYED--------------KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1125 EDFESEKASRNKAEKQKRDLSEELEALKTELEDtldttaaqqelrtkREQEVAELKKALedetKNHEAQIQDMRQRHATA 1204
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDD--------------RNMEVQRLEALL----KAMKSECQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1205 LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQ---------------------VKAESEHKRKKLDAQVQE 1263
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESsertvsdltaslqekeraieaTNAEITKLRSRVDLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1264 LHAKVSEGDRLR----------VELAEKANK---LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQ 1330
Cdd:pfam15921 533 LQHLKNEGDHLRnvqtecealkLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1331 KLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVlalqsqlADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEE 1410
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV-------KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1411 KVlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQL-LAEEKGISARyaeerdRAEAEAREKETKALSLA 1489
Cdd:pfam15921 686 KS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK------RGQIDALQSKIQFLEEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1490 raLEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRT-------QLEELEDELQATEDAK 1562
Cdd:pfam15921 757 --MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQES 834
|
....*
gi 1907083614 1563 LRLEV 1567
Cdd:pfam15921 835 VRLKL 839
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1248-1928 |
3.74e-14 |
|
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: 78.57 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1248 AESEHKRKKLDAQVQELHAKVsegDRLRVEL--AEKANKLQNELDNVSTLLEEAEKKgiKFAKDAAGLESQLQDTQELLQ 1325
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQL---ERLRRERekAERYQALLKEKREYEGYELLKEKE--ALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1326 EETRQKLNLSSRIRQLEEEKNSLQEQQeeeeeaRKNLEKQVLALQSQLADTKkkvdddlGTIESLEEAKKKLLKDVEALS 1405
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI------KDLGEEEQLRVKEKIGELE-------AEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1406 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDhqrQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKE--- 1482
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRD---KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklk 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1483 TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAK 1562
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1563 LRLEVNMQAMKAQFERdLQTRDEQNEEKKRLLLKQVRELEAELE------------DERKQRALAVASKKKME------- 1623
Cdd:TIGR02169 479 DRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNnvvvedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1624 ---------------------------------------------IDLKDLEAQIEAANK--ARDEVIKQ----LRKL-- 1650
Cdd:TIGR02169 558 avakeaiellkrrkagratflplnkmrderrdlsilsedgvigfaVDLVEFDPKYEPAFKyvFGDTLVVEdieaARRLmg 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1651 QAQMKDYQRELEE--------ARASRDEIFAQSKESEkKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSAS 1722
Cdd:TIGR02169 638 KYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1723 GKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLER-----QNKEL 1797
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1798 KAKLQELEgAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANA 1877
Cdd:TIGR02169 797 QAELSKLE-EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1878 RMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
979-1805 |
4.44e-14 |
|
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: 78.55 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 979 KIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAE----EEEKAKNLAKIRNKQevmISDLEERLKKEEKTRQELE 1054
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRT---VREKERELVDCQRELEKLN 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1055 KAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQG--------ALARGDDETLHKNNALKVARELQAQIAELQED 1126
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1127 FESEKASRNK-AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKR---EQEVAELKKALEDETKNHEAQIQDMRQRH 1201
Cdd:TIGR00606 413 LCADLQSKERlKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIkelQQLEGSSDRILELDQELRKAERELSKAEK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1202 ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESehkRKKLDAQVQELHAKVSEGDRLRVELAEK 1281
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1282 ANK--LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL---EEEKNSLQEQQEEEE 1356
Cdd:TIGR00606 570 PNKkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1357 EARKNLekQVLALQSQLADTK-KKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAY----DKLEKTKNRLQQELDD 1431
Cdd:TIGR00606 650 KSSKQR--AMLAGATAVYSQFiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLApdklKSTESELKKKEKRRDE 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1432 LTVDLDHQRQIvsnLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKET--KALSLARALEEALEAKEEFERQNKQL 1509
Cdd:TIGR00606 728 MLGLAPGRQSI---IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKVCLTDVTIMERFQMELKDV 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1510 RADMEDLMSSKD--DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA---QFERDLQTRd 1584
Cdd:TIGR00606 805 ERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRR- 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1585 EQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKardevikqlrKLQAQMKDYQRELEEA 1664
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK----------KAQDKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1665 RASRDEIFAQSKES-EKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEE 1743
Cdd:TIGR00606 954 HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEV 1033
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 1744 ELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELE 1805
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1136-1852 |
5.02e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1136 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKK---ALEDETKNHEAQIQDMRQRHATaLEELSEQL 1212
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEISSELPELREELEKLEKEVKE-LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1213 EQAKRFKANLEKNKQGLETDNKELacevkvlqqvkaesEHKRKKLDAQVQELHAKVSEGDRLRvELAEKANKLQNELDNV 1292
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIREL--------------EERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1293 STLLEEAEKKGIKFAKDAAGLESQLQDTQELlqeetrqklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqVLALQSQ 1372
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEK-----------EERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1373 LADTKKKVdddlgTIESLEEAKKKLlkdvEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdldhqRQIVSNLEKKQKK 1452
Cdd:PRK03918 374 LERLKKRL-----TGLTPEKLEKEL----EELEKAKEEIEEEISKITARIGELKKEIKEL-------KKAIEELKKAKGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1453 F---DQLLAEE--KGISARYAEERDRAEAEAREKETKaLSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK-N 1526
Cdd:PRK03918 438 CpvcGRELTEEhrKELLEEYTAELKRIEKELKEIEEK-ERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKyN 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1527 VHELEKSKRALEQQVEEMRT---QLEELEDELQatedaklrlevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEA 1603
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKlkgEIKSLKKELE--------------------------KLEELKKKLAELEKKLDELEE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1604 ELED-ERKQRALAVASKKKMEIDLKDLEAQIEAANKARDeVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1682
Cdd:PRK03918 571 ELAElLKELEELGFESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1683 KSLEAEIlqlqeelasSERARRHAEQERDELADEIAnsasgksalldekrRLEARIAQLEEELEEEQSNMELLNDRFrkt 1762
Cdd:PRK03918 650 EELEKKY---------SEEEYEELREEYLELSRELA--------------GLRAELEELEKRREEIKKTLEKLKEEL--- 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1763 tlqvdtlntelaaersaaQKSDNARQQLERQNKELkAKLQELEGAVKS-KFKATISALeAKIGQLEEQLEQEAKERAAAN 1841
Cdd:PRK03918 704 ------------------EEREKAKKELEKLEKAL-ERVEELREKVKKyKALLKERAL-SKVGEIASEIFEELTEGKYSG 763
|
730
....*....|.
gi 1907083614 1842 KLVRRTEKKLK 1852
Cdd:PRK03918 764 VRVKAEENKVK 774
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1015-1716 |
8.70e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 77.32 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1015 LAEEEEKAKNLAKIRNKQEV-MISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI--AELQAQVDELKvQLTKKEEE 1091
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYtQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTyhERKQVLEKELK-HLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1092 LQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEK-----QKRDLSEELEALKTELEDTLDTTAAQQ 1166
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1167 ELRTKREQEVAELKKALEDETkNHEAQIQDMRQRHAtALEELSEQLEQAKRFKANLEKNKQgLETDNKELACEVKVLQQV 1246
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQS-SIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHT-LTQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1247 KAESEHKRKKLDAQVQELHAKVSEGDRLRVELA----------EKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1316
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAhakkqqelqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1317 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNL-------------EKQVLALQSQLADTKKKVDDD 1383
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrmqrgEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1384 LGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdLDHQRQIV-SNLEKKQKKFDQLLAEEKG 1462
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL---SEAEDMLAcEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1463 ISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK---RALEQ 1539
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQtllRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1540 QVEEMRTQLEELEDELQATEdaklrlevnmqamkaqfeRDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASK 1619
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLG------------------SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1620 KKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK----KLKSLEAEILQLQEE 1695
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLK 853
|
730 740
....*....|....*....|.
gi 1907083614 1696 LASSERARRHAEQERDELADE 1716
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQL 874
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1172-1885 |
1.30e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.10 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1172 REQEVAELKKALEDETK-NHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKnkqgletdnKELACEVKVLQQVKAES 1250
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEA---------FGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1251 EHKRKKldaqvqelhAKVSEGDRLRVELAEKANKLQNeldnvstlLEEAEKkgikfAKDAAGLESQLQDTQELLQEETRQ 1330
Cdd:PTZ00121 1114 ARKAEE---------AKKKAEDARKAEEARKAEDARK--------AEEARK-----AEDAKRVEIARKAEDARKAEEARK 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1331 klnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlALQSQLADTKKKVDDdlgtIESLEEAKK-KLLKDVEALSQRLE 1409
Cdd:PTZ00121 1172 ----AEDAKKAEAARKAEEVRKAEELRKAEDARK---AEAARKAEEERKAEE----ARKAEDAKKaEAVKKAEEAKKDAE 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1410 EkvlAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEE--KGISARYAEERDRAEAEAR--EKETKA 1485
Cdd:PTZ00121 1241 E---AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEkkKADEAKKAEEKKKADEAKKkaEEAKKA 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1486 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELE---DELQATEDAK 1562
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAK 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1563 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKqralAVASKKKMEIDLKDLEAQIEAANKARDE 1642
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1643 VIKQLRKLQAQMKDYQRELEEARASRDEifAQSKESEKKlkslEAEILQLQEELASSERARRHAEQERdelADEIANSAS 1722
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKK----KADEAKKAEEAKKADEAKKAEEAKK---ADEAKKAEE 1544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1723 GKSAllDEKRRLE-ARIAQLEEELEEEQSNMELLNDRFRKTTL--QVDTLNTELAAERSAAQKSDNARQQLERQNKELKA 1799
Cdd:PTZ00121 1545 KKKA--DELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1800 KLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTE---KKLKEIFMQVEDERRHADQYKEQMEKAN 1876
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
....*....
gi 1907083614 1877 aRMKQLKRQ 1885
Cdd:PTZ00121 1703 -KAEELKKK 1710
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
854-1508 |
1.37e-13 |
|
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: 76.30 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 854 LQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEE 933
Cdd:pfam05483 115 IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 934 eeernQILQNEKKKMQAhiqdleeqldeeEGARQKLQLEKVTAEAKIKKMEEEvllledqnskFIKEKKLMEDRIAECSS 1013
Cdd:pfam05483 195 -----MILAFEELRVQA------------ENARLEMHFKLKEDHEKIQHLEEE----------YKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1014 QLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTD----LQDQIAELQAQVDELKVQLTKKE 1089
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTIC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1090 EELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ---- 1165
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKevel 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1166 QELRT-----------------------KREQEVAELKKALEDETKNHEAQ---IQDMRQRHATALEELSEQLEQAKRFK 1219
Cdd:pfam05483 408 EELKKilaedeklldekkqfekiaeelkGKEQELIFLLQAREKEIHDLEIQltaIKTSEEHYLKEVEDLKTELEKEKLKN 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1220 ANLEKNKQGLETDNKEL-------ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgdrLRVELAEKANKLQNELDNV 1292
Cdd:pfam05483 488 IELTAHCDKLLLENKELtqeasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN---LRDELESVREEFIQKGDEV 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1293 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQ 1372
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1373 LADTKKKVDDDLGTIESLEEAKK----KLLKDVEALSQRLEEKVlaydklektknRLQQELDdltVDLDHQ-RQIVSNLE 1447
Cdd:pfam05483 645 LASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADEAV-----------KLQKEID---KRCQHKiAEMVALME 710
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1448 KKQKKFDQLLAEEKGISARYaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQ 1508
Cdd:pfam05483 711 KHKHQYDKIIEERDSELGLY-KNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKE 770
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
917-1693 |
1.55e-13 |
|
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: 76.31 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 917 KQELEEILHDLESRVEEEEER----NQILQNEKKKMQAHIQDLEEQLdeeegarQKLQLEKvTAEAKIKKME---EEVLL 989
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRlnesNELHEKQKFYLRQSVIDLQTKL-------QEMQMER-DAMADIRRREsqsQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 990 LEDQNS--KFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQEL------------EK 1055
Cdd:pfam15921 145 NQLQNTvhELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfrslgsaiSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1056 AKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAlargddetlHKNNALKVARELQAQIAELqedfeSEKASrn 1135
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQ---------HQDRIEQLISEHEVEITGL-----TEKAS-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1136 KAEKQKRDLSEELEALKtelEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQA 1215
Cdd:pfam15921 289 SARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1216 KRF---KANLEKNKQGLETD----NKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNE 1288
Cdd:pfam15921 366 DQFsqeSGNLDDQLQKLLADlhkrEKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1289 LDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQqeeeeearknlEKQVLA 1368
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-----------ERAIEA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1369 LQSQLADTKKKVDDDLGTIESL---EEAKKKLLKDVEALSQRLEEKvlaydklEKTKNRLQQELDDLTVDLDHQRQIVSN 1445
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLkneGDHLRNVQTECEALKLQMAEK-------DKVIEILRQQIENMTQLVGQHGRTAGA 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1446 LEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM----SSKD 1521
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRN 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1522 DVGKNVHELEKSKRALEQQVEEMRT-------QLEELEDELQATEDAKLRLE-VNMQAMKAQFerDLQTRDEQNEEKKRL 1593
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEMETttnklkmQLKSAQSELEQTRNTLKSMEgSDGHAMKVAM--GMQKQITAKRGQIDA 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1594 LLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQieaankaRDEVIKQLRKLQAQMKDYQRELEEARASRDEIFA 1673
Cdd:pfam15921 746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-------KNKMAGELEVLRSQERRLKEKVANMEVALDKASL 818
|
810 820
....*....|....*....|
gi 1907083614 1674 QSKESEKKLKSLEAEILQLQ 1693
Cdd:pfam15921 819 QFAECQDIIQRQEQESVRLK 838
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
844-1592 |
2.84e-13 |
|
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: 75.78 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 844 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQE 919
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleikREAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 920 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEG-ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFI 998
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLElARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 999 KEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGettdlqdqiaeLQAQV 1078
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV-----------LLALI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1079 DELKVQLTKKEEELQGALARGDDETLHKN-NALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED 1157
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVENYKVAIsTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1158 TLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELA 1237
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1238 CEVKVLQQVKAES--EHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLES 1315
Cdd:pfam02463 677 EIQELQEKAESELakEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1316 QLQDTQEllQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKK 1395
Cdd:pfam02463 757 LKKEEKE--EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1396 KLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1475
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1476 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsskddvgknvhELEKSKRALEQQVEEMRTQLEELEDEL 1555
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-----------EEEERNKRLLLAKEELGKVNLMAIEEF 983
|
730 740 750
....*....|....*....|....*....|....*..
gi 1907083614 1556 QATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKR 1592
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1135-1803 |
4.00e-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: 74.67 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1135 NKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREqevaELKKALEDETKNHEAQIQDMRQrhataleelseqleq 1214
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDE----EKINNSNNKIKILEQQIKDLND--------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1215 akrfKANLEKNK-QGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVS 1293
Cdd:TIGR04523 90 ----KLKKNKDKiNKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1294 TLLEEAEKKGIKFAKDAAGLESQLQDTQellQEETRQKLNLSSrIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQL 1373
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIK---NKLLKLELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1374 ADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLT--VDLDHQRQIVSNLEKKQK 1451
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnqKEQDWNKELKSELKNQEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1452 KFDQL---LAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVH 1528
Cdd:TIGR04523 322 KLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKL-------RLEVNMQAMKAQFERDLQTRDEQNEEKKrLLLKQVREL 1601
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLK-VLSRSINKI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1602 EAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARasrDEIfaQSKESEKK 1681
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE---DEL--NKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1682 LKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1761
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1907083614 1762 TTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQE 1803
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
967-1732 |
4.48e-13 |
|
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: 74.76 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 967 QKLQLEKVTAEAKIK----KMEEEVLLLEDQNsKFIKEKKLMEDRIaecSSQLAEEEEKAKNLAKIRNKQEVMISDLEER 1042
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1043 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHknnalkVARELQAQIAE 1122
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH------LEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1123 LQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDetknheaqIQDMRQRHA 1202
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--------IKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1203 TALEELSEQLEQAKRFKANLEKNKQG-LETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEK 1281
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1282 anklqneldnvSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEEtrqklnlssriRQLEEEKNSLQEQQEEEEEARKN 1361
Cdd:pfam05483 390 -----------SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-----------KQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1362 LEKQVLALQSQLADTKKKVDDDLGTIESLE-EAKKKLLKDVEALSQRleekvlayDKLEKTKNRLQQELDDLTVDLDHQR 1440
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1441 QIVSNLEKKQKKFDQLLA--EEKGISARYAEERDRAEAEAREKETKAL--SLARALEEALEAKEEFERQNKQLRADMEDL 1516
Cdd:pfam05483 520 EDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEFIQKGDEVKCKldKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1517 MSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQatedaklRLEVNMQAMKAQFERDLQTRDEQNEEKKrlllk 1596
Cdd:pfam05483 600 KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN-------KLELELASAKQKFEEIIDNYQKEIEDKK----- 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1597 qVRELEAELEDERKQRALAVASKKKMEIDLkdleaqieaanKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1676
Cdd:pfam05483 668 -ISEEKLLEEVEKAKAIADEAVKLQKEIDK-----------RCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1677 ESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEiansASGKSALLDEKR 1732
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME----AKENTAILKDKK 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
842-1257 |
6.96e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 842 KPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEknilAEQLQAETELFAEAEEMRARLAAK-KQEL 920
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER----HELYEEAKAKKEELERLKKRLTGLtPEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 921 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ--------------LEKVTAEakIKKMEEE 986
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPvcgrelteehrkelLEEYTAE--LKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 987 VLLLEDQNSKFIKEKKLMEDRIAEcSSQLAEEEEKAKNLAKIRNK-QEVMISDLEERLKKEEKTRQELEKAKRKLDGETT 1065
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1066 DLQdQIAELQAQVDELKVQLTKKEEELqgalarGDDETLHKNNALKVARELQAQIAELqEDFESEKASRNKAEKQKRDLS 1145
Cdd:PRK03918 547 ELE-KLEELKKKLAELEKKLDELEEEL------AELLKELEELGFESVEELEERLKEL-EPFYNEYLELKDAEKELEREE 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1146 EELEALKTELEDTLDTTA-AQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEK 1224
Cdd:PRK03918 619 KELKKLEEELDKAFEELAeTEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
410 420 430
....*....|....*....|....*....|...
gi 1907083614 1225 NKQGLETdNKELACEVKVLQQVKAESEHKRKKL 1257
Cdd:PRK03918 699 LKEELEE-REKAKKELEKLEKALERVEELREKV 730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1277-1926 |
7.52e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.90 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1277 ELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEE 1356
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1357 EARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDL 1436
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1437 DHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLradmedl 1516
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1517 msskDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRLLLK 1596
Cdd:TIGR04523 270 ----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1597 QVRELEAELEDERKQralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAsrdeifaQSK 1676
Cdd:TIGR04523 343 QISQLKKELTNSESE-------NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK-------LNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1677 ESEKKLKSLEAEILQLqeelasserarrhaEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1756
Cdd:TIGR04523 409 QKDEQIKKLQQEKELL--------------EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1757 DRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQ--EA 1834
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNKddFE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1835 KERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATranasrrKLQRELDDATEAN 1914
Cdd:TIGR04523 554 LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-------SLEKELEKAKKEN 626
|
650
....*....|..
gi 1907083614 1915 EGLSREVSTLKN 1926
Cdd:TIGR04523 627 EKLSSIIKNIKS 638
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
803-1449 |
9.14e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.02 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 803 RKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEgeleemERKH 882
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE------EAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 883 QQLLEEKnilAEQLQAETELFAEAEEMRARLAAKKQELEeilhdlesrveeeeernqilqnekkkmqahiqdleeqldee 962
Cdd:PTZ00121 1446 ADEAKKK---AEEAKKAEEAKKKAEEAKKADEAKKKAEE----------------------------------------- 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 963 egARQKLQLEKVTAEAkiKKMEEEVLLLEDQNSKFIKEKKLMEDRIAEcSSQLAEEEEKAKNLAKIRNKQEVMISDLEER 1042
Cdd:PTZ00121 1482 --AKKADEAKKKAEEA--KKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1043 LKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQVDELKVQ----LTKKEEELQGALARGDDETLHKNNALKVARELQA 1118
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1119 QIAELQEDFESEKasrNKAEKQKRdlSEELEALKTELEdtldttaAQQELRTKREQEvaELKKALEDETKNHEAQIQDmr 1198
Cdd:PTZ00121 1634 KVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE-------AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE-- 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1199 qrhatalEELSEQLEQAKRFKAnlEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQE------LHAKVSEGD 1272
Cdd:PTZ00121 1698 -------AEEAKKAEELKKKEA--EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEK 1768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1273 RLRVELAEKANKLQNELDnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEET----RQKLNLSSRIRQLEEEKNSL 1348
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELD------EEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvinDSKEMEDSAIKEVADSKNMQ 1842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1349 QEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQE 1428
Cdd:PTZ00121 1843 LEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
650 660
....*....|....*....|.
gi 1907083614 1429 lDDLTVDLDHQRQIVSNLEKK 1449
Cdd:PTZ00121 1923 -EYIKRDAEETREEIIKISKK 1942
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1301 |
3.46e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 840 KVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQE 919
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 920 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEdqnsKFIK 999
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1000 EKKLMEDRIAECSSQLAEEEEKaknlaKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETT---------DLQDQ 1070
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliklkELAEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1071 IAELQAQVDELKVQ-LTKKEEELQGALARgddetlhknnalkvARELQAQIAELQEDFESEKASRNKA---EKQKRDLSE 1146
Cdd:PRK03918 505 LKELEEKLKKYNLEeLEKKAEEYEKLKEK--------------LIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1147 ELEALKTELEdtldttaaqqELRTKREQEVAELKKALEdETKNHEAQIQDMRQRhataLEELSEQLEQAKRFKANLEKNK 1226
Cdd:PRK03918 571 ELAELLKELE----------ELGFESVEELEERLKELE-PFYNEYLELKDAEKE----LEREEKELKKLEEELDKAFEEL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1227 QGLETDNKELACEVKVLQQVKAESEHKRK-----KLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEK 1301
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1253-1710 |
3.74e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1253 KRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAEKKGIKFAKDAAGLEsQLQDTQELLQEETRQKL 1332
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1333 NLSSRIRQLEEEKNSLQeqqeeeeeARKNLEKQVLALQSQLADTKKKVDDDL-GTIESLEEAKKKLLKDVEALSQRLEEK 1411
Cdd:COG4717 140 ELAELPERLEELEERLE--------ELRELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1412 VLAYDKLEKTKNRLQQELDDLTVDLDHQrqivsNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA-- 1489
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAA-----ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1490 --------RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--ATE 1559
Cdd:COG4717 287 allflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1560 DAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDERK--QRALAVASKKKMEIDLKDLEAQIEAAN 1637
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 1638 KARDEVIKQLRKLQAQMKDY--QRELEEARASRDEIFAQskesekkLKSLEAEILQLQEELASSERARRHAEQER 1710
Cdd:COG4717 446 EELEELREELAELEAELEQLeeDGELAELLQELEELKAE-------LRELAEEWAALKLALELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1613-1853 |
4.60e-12 |
|
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: 70.18 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1613 ALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1692
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1693 QEELasserarrhaEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1772
Cdd:COG4942 96 RAEL----------EAQKEELAELLR-------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1773 LAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLK 1852
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
.
gi 1907083614 1853 E 1853
Cdd:COG4942 238 A 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
899-1627 |
5.20e-12 |
|
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: 71.41 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 899 ETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLdeeegaRQKLQLEKVTAEA 978
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK------RDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 979 KIKKMEEEVLLLEDQNSKFIKEK----KLMEDRIAECSSQLAEEEEKAK----NLAKIRNKQEVMISDLEERLKK----- 1045
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKaltgKHQDVTAKYNRRRSKIKEQNNRdiagi 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1046 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALArgddETLHKNNALKVARELQAQIAELQE 1125
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG----ELKLRLNQATATPELLLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1126 DFESEKASRNKAEKQKRDLSEELEALKTELEDTLDttAAQQElrtkrEQEVAELKKALEdetknhEAQIQDMRQRHaTAL 1205
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRRDQASE--ALRQA-----SRRLEERQSALD------ELELQLFPQAG-TLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1206 EELSEQLEQAKRFKANLEKNKQGLETDnkeLACEVkVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRvelaEKANKL 1285
Cdd:pfam12128 538 HFLRKEAPDWEQSIGKVISPELLHRTD---LDPEV-WDGSVGGELNLYGVKLDLKRIDVPEWAASEEELR----ERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1286 QNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQeetrqklNLSSRIRQLEEEKNSLQeqqeeeeearknlekq 1365
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK-------NARLDLRRLFDEKQSEK---------------- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1366 vLALQSQLADTKKKVDDDlgtIESLEEAKKKLLKDVEALSQRLEEkvlaydklEKTKNRLQQELDDLTVDLDHQRQIVSN 1445
Cdd:pfam12128 667 -DKKNKALAERKDSANER---LNSLEAQLKQLDKKHQAWLEEQKE--------QKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1446 LEKKQKKFDQLLAEEKGISARYAEE-------RDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS 1518
Cdd:pfam12128 735 KAAIAARRSGAKAELKALETWYKRDlaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1519 SKDDVGKNVHELEKSkraLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLllkQV 1598
Cdd:pfam12128 815 QLSNIERAISELQQQ---LARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQG---SI 888
|
730 740
....*....|....*....|....*....
gi 1907083614 1599 RELEAELEDERKQRALAVASKKKMEIDLK 1627
Cdd:pfam12128 889 GERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1449 |
5.80e-12 |
|
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: 71.36 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 847 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNilaEQLQAETELFAEAEEMRARLaakKQELEEILHD 926
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT---QQLEEKAAAYDKLEKTKNRL---QQELDDLLVD 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 927 LESrveeeeeRNQILQNEKKKMQ-----------AHIQDLEEQLDEEEGARQK----LQLEKVTAEAKIKKME------- 984
Cdd:pfam01576 589 LDH-------QRQLVSNLEKKQKkfdqmlaeekaISARYAEERDRAEAEAREKetraLSLARALEEALEAKEElertnkq 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 985 -----EEVLLLEDQNSKFIKE----KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEK 1055
Cdd:pfam01576 662 lraemEDLVSSKDDVGKNVHElersKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1056 AKRKLdgettdLQDQIAELQAQVDELKVQLT-------KKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFE 1128
Cdd:pfam01576 742 EKRRQ------LVKQVRELEAELEDERKQRAqavaakkKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1129 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAEL----------KKALEDETKNHEAQIQDMR 1198
Cdd:pfam01576 816 EARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELadeiasgasgKSALQDEKRRLEARIAQLE 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1199 qrhatalEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQvkaeSEHKRKKLDAQVQELHAKVSEgdrlrvel 1278
Cdd:pfam01576 896 -------EELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQK----SESARQQLERQNKELKAKLQE-------- 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1279 aekanklqneldnvstlLEEAEKKgiKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknslqeqqeeeeea 1358
Cdd:pfam01576 957 -----------------MEGTVKS--KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEK--------------- 1002
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1359 rknlekqvlalqsQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDH 1438
Cdd:pfam01576 1003 -------------KLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNES 1069
|
650
....*....|.
gi 1907083614 1439 QRQIVSNLEKK 1449
Cdd:pfam01576 1070 MNREVSTLKSK 1080
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
999-1221 |
8.00e-12 |
|
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: 69.41 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 999 KEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQV 1078
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1079 DEL--KVQLTKKEEELQGALARGDDETLHKNNAL--KVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTE 1154
Cdd:COG4942 107 AELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 1155 LedtldttAAQQELRTKREQEVAELKKaledETKNHEAQIQDMRQRhATALEELSEQLEQAKRFKAN 1221
Cdd:COG4942 187 R-------AALEALKAERQKLLARLEK----ELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
1.18e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 60.91 E-value: 1.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907083614 31 TAKKLVWIPSERHGFEAASIKEERGDEVMVELaENGKKAMVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
872-1475 |
3.08e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 872 EGELEEMERKHQQLLEEKNiLAEQLQAETELFAEAEEMRARLAA-----KKQELEEILHDLESRVEEEEERNQILQNEKK 946
Cdd:COG4913 241 HEALEDAREQIELLEPIRE-LAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 947 KMQAHIQDLEEQLDEEEGAR-QKLQLEKVTAEAKIKKMEEEVLLLEDQ----NSKFIKEKKLMEDRIAECSSQLAEEEEK 1021
Cdd:COG4913 320 ALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1022 AKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE-LQAQVDELK-----VQLTKKEEELQGA 1095
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPfvgelIEVRPEEERWRGA 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1096 LAR--GD------------DETLHKNNALKVARELQAQ-IAELQEDFESEKASRNkaekqkrDLSEELEALKTELEDTLD 1160
Cdd:COG4913 480 IERvlGGfaltllvppehyAAALRWVNRLHLRGRLVYErVRTGLPDPERPRLDPD-------SLAGKLDFKPHPFRAWLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1161 TTAAQQELRTK--REQEVAELKKALEDE--TKN----HEAQIQDMRQRH-------ATALEELSEQLEQAKRfkanlekn 1225
Cdd:COG4913 553 AELGRRFDYVCvdSPEELRRHPRAITRAgqVKGngtrHEKDDRRRIRSRyvlgfdnRAKLAALEAELAELEE-------- 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1226 kqgletdnkelacEVKVLQQVKAESEHKRKKLDAQvQELHAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAEKkgik 1305
Cdd:COG4913 625 -------------ELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVAS----AEREIAELEAELERLDA---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1306 FAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKkvdDDLG 1385
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF---AAAL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1386 TIESLEEAKKKLLKDVEALSQRLEEkvlAYDKLEKTKNRLQQELDDLTVDLD------------HQRQIVSNLEKKQKKF 1453
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNR---AEEELERAMRAFNREWPAETADLDadleslpeylalLDRLEEDGLPEYEERF 836
|
650 660
....*....|....*....|....*..
gi 1907083614 1454 DQLLAEEKG-----ISARYAEERDRAE 1475
Cdd:COG4913 837 KELLNENSIefvadLLSKLRRAIREIK 863
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1535-1930 |
3.35e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1535 RALEQQVEEMRTQ---LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQ 1611
Cdd:COG4913 238 ERAHEALEDAREQielLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1612 RALAVASKKKME--------IDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQrelEEARASRDEIFAQSKESEKKLK 1683
Cdd:COG4913 318 LDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1684 SLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSA----------------------------LLD------ 1729
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiparllalrdalaealgldeaelpfvgeLIEvrpeee 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1730 -------------------------------EKRRLEARI-AQLEEELEEEQSNMELLNDR------FRKTTLQvDTLNT 1771
Cdd:COG4913 475 rwrgaiervlggfaltllvppehyaaalrwvNRLHLRGRLvYERVRTGLPDPERPRLDPDSlagkldFKPHPFR-AWLEA 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1772 ELAaERSAAQKSDNArQQLER------------QNKEL-------------------KAKLQELEGAVKsKFKATISALE 1820
Cdd:COG4913 554 ELG-RRFDYVCVDSP-EELRRhpraitragqvkGNGTRhekddrrrirsryvlgfdnRAKLAALEAELA-ELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1821 AKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeiFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASR 1900
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510
....*....|....*....|....*....|
gi 1907083614 1901 RKLQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1063-1832 |
7.42e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1063 ETTDLQDQIAELQAQVDELkvqltkkeEELQGALargdDETLHKNNALKVARELQAQIAELQEDFESEKASRNK-----A 1137
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1138 EKQKRDLSEELEALKTELEDTldttaaqqelrtkrEQEVAELKKALEDetknHEAQIQDMRQRHATALEELSEQLEQakr 1217
Cdd:COG4913 287 QRRLELLEAELEELRAELARL--------------EAELERLEARLDA----LREELDELEAQIRGNGGDRLEQLER--- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1218 fkanleknkqgletdnkelacEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRlrvELAEKANKLQNELDNVSTLLE 1297
Cdd:COG4913 346 ---------------------EIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1298 EAEkkgikfaKDAAGLESQLQDTQEllqeetrqklnlssRIRQLEEEKNSLQEQqeeeeeaRKNLEKQVLALQSQLADTK 1377
Cdd:COG4913 402 ALE-------EALAEAEAALRDLRR--------------ELRELEAEIASLERR-------KSNIPARLLALRDALAEAL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1378 KKVDDDL-----------------GTIESL-----------EEAKKKLLKDVEALSQRLEekvLAYDKLEKT-KNRLQQE 1428
Cdd:COG4913 454 GLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvpPEHYAAALRWVNRLHLRGR---LVYERVRTGlPDPERPR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1429 LDDltvdldhqRQIVSNLEKKQKKFDQLLAEEkgisarYAEERDRA---EAEAREKETKALSLARaleealeakeeferq 1505
Cdd:COG4913 531 LDP--------DSLAGKLDFKPHPFRAWLEAE------LGRRFDYVcvdSPEELRRHPRAITRAG--------------- 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1506 nkqlradmedLMSSkddvGKNVHELEKSKRALEQQV--EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDlqtr 1583
Cdd:COG4913 582 ----------QVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL---- 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1584 deqneEKKRLLLKQVRELEAElederkqralavaskkkmEIDLKDLEAQIEAANKARDEVIK---QLRKLQAQMKDYQRE 1660
Cdd:COG4913 644 -----QERREALQRLAEYSWD------------------EIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAE 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1661 LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELassERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDA 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1741 LEEELEEEQSNMELLNDRFRKT-TLQVDTLNTELAAERSAAQKsdnaRQQLERQN-KELKAKLQELEGAVKSKFKATI-S 1817
Cdd:COG4913 778 LRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEEDGlPEYEERFKELLNENSIEFVADLlS 853
|
810
....*....|....*
gi 1907083614 1818 ALEAKIGQLEEQLEQ 1832
Cdd:COG4913 854 KLRRAIREIKERIDP 868
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1040-1870 |
2.08e-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: 66.51 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1040 EERLKKEEKT---RQELEKAKRKLDGEttdlQDQIAELQAQVDELKVQLTKKEEELQGALArgddetlHKN---NAL--- 1110
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAASD-------HLNlvqTALrqq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1111 -KVAR------ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED---TLDT--TAA---QQELRTKRE-Q 1174
Cdd:COG3096 347 eKIERyqedleELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqALDVqqTRAiqyQQAVQALEKaR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1175 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLEtdnkelacevKVLQQVKAESEHKR 1254
Cdd:COG3096 427 ALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVC----------KIAGEVERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1255 -KKLDAQVQELHAKVSEGDRLRVELAEkANKLQNELDNVSTLLEEaekkgikFAKDAAGLESQLQDTQELLQEETRQKLN 1333
Cdd:COG3096 497 aRELLRRYRSQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEE-------FCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1334 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV---LALQSQLADTKKKVDDDLGTIESLEEAKKKLLkdvealsQRLEE 1410
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLL-------ERERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1411 KVLAYDKLEKTKNRLQQElddltvdldhqrqiVSNLEKKQKKFD---QLLAEEKG------------------ISARYAE 1469
Cdd:COG3096 642 ATVERDELAARKQALESQ--------------IERLSQPGGAEDprlLALAERLGgvllseiyddvtledapyFSALYGP 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1470 ER------DraeaeareketkaLSLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK----- 1532
Cdd:COG3096 708 ARhaivvpD-------------LSAVK-------------EQLAGLEDCPEDLYliegdpDSFDDSVFDAEELEDavvvk 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1533 -SKRAL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-----DEQNEE 1589
Cdd:COG3096 762 lSDRQWrysrfpevplfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEA 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1590 KKRLLLKQVRELEAELEDERKQralavaskkkmeidLKDLEAQIEAANkardEVIKQLRKLQAQM------------KDY 1657
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQ--------------EQQLRQQLDQLK----EQLQLLNKLLPQAnlladetladrlEEL 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1658 QRELEEARASRDEIFAQSK---ESEKKLKSLEAEILQ---LQEELASSERARRHAEQERDELADEIANSA----SGKSAL 1727
Cdd:COG3096 899 REELDAAQEAQAFIQQHGKalaQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGL 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1728 LDEKRRLEARIAQLEEELEEEQSNmelLNDRFRKTTLQVDTLNTELAAERSAAqksDNARQQLerqnKELKAKLQELEGA 1807
Cdd:COG3096 979 LGENSDLNEKLRARLEQAEEARRE---AREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTL----QELEQELEELGVQ 1048
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083614 1808 V-----------KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeifmqveDERRHADQYKE 1870
Cdd:COG3096 1049 AdaeaeerarirRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAKA 1115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1630-1853 |
2.14e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.85 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1630 EAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELasserarrhaEQE 1709
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1710 RDELADEIA------NSASGKSALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKs 1783
Cdd:COG3883 85 REELGERARalyrsgGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1784 dnARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1853
Cdd:COG3883 155 --KLAELEALKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1607-1929 |
3.04e-10 |
|
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: 65.86 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1607 DERKQRALAvaskkkmeiDLKDLEAQIEAANKARDEVIKQLRKLQAQ------MKDYQRELEEARASrdEIFAQSKESEK 1680
Cdd:TIGR02169 169 DRKKEKALE---------ELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREYEGY--ELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1681 KLKSLEAEILQLQEELASSERarrhaeqERDELADEIAnsasgksALLDEKRRLEARIaqleeeleeeqsnMELLNDRFR 1760
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTE-------EISELEKRLE-------EIEQLLEELNKKI-------------KDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1761 KTTLQVDTLNTELAaersaaqksdnarqQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQEAKERAAA 1840
Cdd:TIGR02169 291 RVKEKIGELEAEIA--------------SLERSIAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIEEERKRRDKL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1841 NKLVRRTEKKLKEIFMQVEDE-------RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA 1913
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330
....*....|....*.
gi 1907083614 1914 NEGLSREVSTLKNRLR 1929
Cdd:TIGR02169 436 INELEEEKEDKALEIK 451
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
852-1298 |
5.45e-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: 64.74 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 852 EELQAKDEELLKVKEKQTKVEGE-------LEEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLAAKKQEL 920
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEfeattcsLEELLRTEQQRLEKNedqlKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 921 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK- 999
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1000 ----EKKLMEDR--IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1073
Cdd:pfam05483 491 tahcDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1074 LQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT 1153
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1154 ELEDTLDTTAAQQELRTKREQEV---AELKKALEDETKNHEAQIqDMRQRHATAleelseqleqakRFKANLEKNKQGLE 1230
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKISEEKLleeVEKAKAIADEAVKLQKEI-DKRCQHKIA------------EMVALMEKHKHQYD 717
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1231 TDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAK-VSEGDRLRVELAEKANKLQNELDNVSTLLEE 1298
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAElLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1633-1930 |
5.50e-10 |
|
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: 64.70 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1633 IEAANKARDEVIKQLrklqAQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELassERARRHAEqERDE 1712
Cdd:TIGR02169 148 ISMSPVERRKIIDEI----AGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKRQQLERL---RREREKAE-RYQA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1713 LADEIANSASgkSALLDEKRRLEARIAQLEEELEEEQSNMEllndrfrKTTLQVDTLNTELAAersaaqksdnARQQLER 1792
Cdd:TIGR02169 216 LLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELE-------KLTEEISELEKRLEE----------IEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1793 QNKELKAKLQELEGAVKSK---FKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYK 1869
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1870 EQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1104-1821 |
5.50e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 64.86 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1104 LHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAA-QQELRTKREQeVAELKKA 1182
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQ-WKEKRDE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1183 LEDETKNHEAQIQDMRqrhatalEELSEQLEQAKRF-KANLEKNKQGLETdnkelacevkvLQQVKAESEHKRKKLDAQV 1261
Cdd:pfam12128 306 LNGELSAADAAVAKDR-------SELEALEDQHGAFlDADIETAAADQEQ-----------LPSWQSELENLEERLKALT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1262 QELHAKVSEGDRLRV----ELAEKANKLQNELDNVStllEEAEKKGIKFAKDAAGLESQLQDTQELLQEETR-QKLNLSS 1336
Cdd:pfam12128 368 GKHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESELREQLEAGKLEFNeEEYRLKS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1337 RIRQL----------EEEKNSLQEQQEEEEEARKNLE---KQVLALQSQLADTKKKVDddlgtiesleEAKKKLlkdvEA 1403
Cdd:pfam12128 445 RLGELklrlnqatatPELLLQLENFDERIERAREEQEaanAEVERLQSELRQARKRRD----------QASEAL----RQ 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1404 LSQRLEEkvlaydklektknrLQQELDDLTVDLDHQR-QIVSNLEKKQKKFDQLLAeeKGISARYAEERDRAEAEAREKE 1482
Cdd:pfam12128 511 ASRRLEE--------------RQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIG--KVISPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1483 TKALSLARALEEALEAKEEFERQ-NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDA 1561
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDVPEWAAsEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLD 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1562 KLRLEVNMQAMKAQFERDLQTRDEQNEE--------KKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQI 1633
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANErlnsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1634 EAANKARDEVIKqlRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEaEILQLQEELASSERARRHA-EQERDE 1712
Cdd:pfam12128 735 KAAIAARRSGAK--AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE-RIAVRRQEVLRYFDWYQETwLQRRPR 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1713 LADEIANSASGKSALLDEKRRLEA----RIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTeLAAERSAAQKSDNARQ 1788
Cdd:pfam12128 812 LATQLSNIERAISELQQQLARLIAdtklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT-LKEDANSEQAQGSIGE 890
|
730 740 750
....*....|....*....|....*....|....*.
gi 1907083614 1789 QLeRQNKELKAKLQELEGAVKSK---FKATISALEA 1821
Cdd:pfam12128 891 RL-AQLEDLKLKRDYLSESVKKYvehFKNVIADHSG 925
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1067-1853 |
6.08e-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: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1067 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVAREL-QAQIAELQE-DFESEKASRNKAE--KQKR 1142
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEeiQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1143 DLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIqdmrqrhaTALEELSEQLEQAK-RFKAN 1221
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlEMHFK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1222 LEKNKQGLETDNKELACEVKvlqqvkaESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEK 1301
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEIN-------DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1302 KGIKFAKDAAGLESQLQ---DTQELLQEETRQKlnlSSRIRQLEEEKNSlqeQQEEEEEARKNLEKQVLALQSQLADTKK 1378
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQrsmSTQKALEEDLQIA---TKTICQLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1379 KVDDDLGTIESLEEAKKKLLKDVEALSQRLEEkvlaydkLEKTKNRLQQELDDLTVDLDHQRQIVSnlekKQKKFDQLLA 1458
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEE-------MTKFKNNKEVELEELKKILAEDEKLLD----EKKQFEKIAE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1459 EEKGisaryAEERDRAEAEAREKETKALSLarALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALE 1538
Cdd:pfam05483 433 ELKG-----KEQELIFLLQAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1539 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKaqfERDLQTRDEqneekkrllLKQVRELEAELEDERKQRAlavas 1618
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDE---------LESVREEFIQKGDEVKCKL----- 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1619 kKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELAS 1698
Cdd:pfam05483 569 -DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1699 serARRHAEQERDELADEIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellnDRFRKTTLQVDTLNTELAAERS 1778
Cdd:pfam05483 648 ---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA------------------DEAVKLQKEIDKRCQHKIAEMV 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1779 AAQKSDNAR--QQLERQNKEL---KAKLQElEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1853
Cdd:pfam05483 707 ALMEKHKHQydKIIEERDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1113-1906 |
6.56e-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: 64.68 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1113 ARELQAQIAELQEDFESEKASRNKAEKQKRDLSE---ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKN 1189
Cdd:TIGR00606 219 ACEIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1190 HEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ-QVKAESEHKRKKlDAQVQELHAkv 1268
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLAT-- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1269 segdRLRVELAEKANKLQNELDNVSTLLEEAEKKGikfAKDAAGLESQLQDTQELLQE---ETRQKLNLSSRIRQLEEEK 1345
Cdd:TIGR00606 376 ----RLELDGFERGPFSERQIKNFHTLVIERQEDE---AKTAAQLCADLQSKERLKQEqadEIRDEKKGLGRTIELKKEI 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1346 nslqeqqeeeeearknLEKQvlalQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSqRLEEKVLAYDKLEKTKNRL 1425
Cdd:TIGR00606 449 ----------------LEKK----QEELKFVIKELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1426 QQELDdltvdldhqrqivsnLEKKQKKFDQLLAEEKgisaRYAEERDRAEAEAREKETKalslaraleealeakeefERQ 1505
Cdd:TIGR00606 508 NEKAD---------------LDRKLRKLDQEMEQLN----HHTTTRTQMEMLTKDKMDK------------------DEQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1506 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFERDLQTRDE 1585
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEE 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1586 QneekkrlllkqvrelEAELEDerkqRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR 1665
Cdd:TIGR00606 620 Q---------------LSSYED----KLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1666 ASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEEL 1745
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1746 EEEQSNMElLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVK----SKFKATISALEA 1821
Cdd:TIGR00606 761 QRLKNDIE-EQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELD 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1822 KIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRR 1901
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE 919
|
....*
gi 1907083614 1902 KLQRE 1906
Cdd:TIGR00606 920 KDQQE 924
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
848-1457 |
6.62e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 848 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 927
Cdd:TIGR04523 64 NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 928 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEdqnsKFIKEKKLMEdr 1007
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLE-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1008 iaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEK----TRQELEKAKRKLDGETTDLQD---QIAELQAQVDE 1080
Cdd:TIGR04523 218 -----SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1081 LKVQLtkkeeelqgalargddETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1160
Cdd:TIGR04523 293 LKSEI----------------SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1161 TTAAQQELRTKREQEVAELKKALE---DETKNHEAQIQDMRQrhataleelseQLEQAKRFKANLEKNKQGLETDNKELA 1237
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1238 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQL 1317
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1318 QDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQeeeeearKNLEKQVLALQSQL--ADTKKKVDDDLGTIESLEEAKK 1395
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQK 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 1396 KLLKDVEALSQRLeekvlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLL 1457
Cdd:TIGR04523 579 SLKKKQEEKQELI-------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1629-1881 |
8.07e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.88 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1629 LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIF--AQSKESEKKLKSLEAEILQLQEELASSErARRHA 1706
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDlsEEAKLLLQQLSELESQLAEARAELAEAE-ARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1707 EQERDELADEIANSASGKSALldekRRLEARIAQleeeleeeqsnmellndrfrkttlqvdtLNTELAAERSAAQKSDNA 1786
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVI----QQLRAQLAE----------------------------LEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1787 RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLvrrtEKKLKEIFMQVEDERRHAD 1866
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYE 368
|
250
....*....|....*
gi 1907083614 1867 QYKEQMEKANARMKQ 1881
Cdd:COG3206 369 SLLQRLEEARLAEAL 383
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1529-1740 |
8.81e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDE 1608
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1609 RKQRA--LAVASKKKMEIDLKDLEAQIEAANKARD-EVIKQL-RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS 1684
Cdd:COG4942 103 KEELAelLRALYRLGRQPPLALLLSPEDFLDAVRRlQYLKYLaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1685 LEAEILQLQEELASSERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQ 1740
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELA-------ELQQEAEELEALIAR 231
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1302 |
1.45e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.12 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEmerkHQQLLEEKNILAEQLQAE-TELFAEAEEMrarlaaKKQELEEIL 924
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSE----KQKELEQNNKKIKELEKQlNQLKSEISDL------NNQKEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 925 HDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLM 1004
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1005 EDRIAECSSQLAEEEEKAKNlakirnkqevmisdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQ 1084
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQ--------------KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1085 LTKKEeelqgalargddetlhknnalKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEAL---KTELEDTLDT 1161
Cdd:TIGR04523 456 IKNLD---------------------NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneeKKELEEKVKD 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1162 TAAQQELRTKREQEVAELKKALEDETKNHEAQIQDM-----RQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKEL 1236
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1237 ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKK 1302
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1148-1619 |
1.61e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1148 LEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDmrqrhataLEELSEQLEQAKRFKANLEKNKQ 1227
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE--------LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1228 GLET--DNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgiK 1305
Cdd:COG4717 120 KLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---D 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1306 FAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARK-NLEKQVLALQSQLADTKKKVDDDL 1384
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1385 G----TIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEE 1460
Cdd:COG4717 277 GvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1461 KGISARYAEERDRAEAEAREKETKALSLA--RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNV--HELEKSKRA 1536
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1537 LEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKK----RLLLKQVRELEAELEDERKQR 1612
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEwaalKLALELLEEAREEYREERLPP 516
|
....*..
gi 1907083614 1613 ALAVASK 1619
Cdd:COG4717 517 VLERASE 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1331-1927 |
1.62e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1331 KLNLSSRIRQLEEEKNSLQEQQEEEEeaRKNLEKQVLALQSQLADTKKKVDDdlGTIEslEEAKKKLLKDVEALSQRLEE 1410
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAK--EDNRADEATEEAFGKAEEAKKTET--GKAE--EARKAEEAKKKAEDARKAEE 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1411 KVLAYDKLEKTKNRLQQelDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEkgisARYAEERDRAEAEAREKETKALSLAR 1490
Cdd:PTZ00121 1133 ARKAEDARKAEEARKAE--DAKRVEIARKAEDARKAEEARKAEDAKKAEA----ARKAEEVRKAEELRKAEDARKAEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1491 ALEEALEAKEEFERQNKQLRADMEDLMSSKDDVgknvhelEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmQ 1570
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA-------EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---E 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1571 AMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL----------AVASKKKMEIDLKDLEAQIEAANKAR 1640
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaeeakkkADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1641 DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEA-----EILQLQEELASSERARRHAEQERDelAD 1715
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkadELKKAAAAKKKADEAKKKAEEKKK--AD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1716 EIANSASGKSALLDEKRRLE-ARIAQLEEELEEEQSNMELLndrfRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQN 1794
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEeAKKAEEAKKKAEEAKKADEA----KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1795 KELKAKLQELEGAVKSKFKATISALEAKIGQLEEQleQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEK 1874
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK--KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1875 ANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1927
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1036-1212 |
1.70e-09 |
|
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: 60.32 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1036 ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNAlKVARE 1115
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1116 LQAqiaeLQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKALEDETKNHEAQIQ 1195
Cdd:COG1579 91 YEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|....*..
gi 1907083614 1196 DMRQRHATALEELSEQL 1212
Cdd:COG1579 160 ELEAEREELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1528-1930 |
1.77e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1528 HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFE-RDLQTRDEQNEEKkrllLKQVRELEAELE 1606
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEER----LEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1607 DERKQRA-LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1685
Cdd:COG4717 167 ELEAELAeLQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1686 EAEILQLQEELASSERARRHAEQERDELADEIANSASG-----KSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFR 1760
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1761 KTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKakLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAA 1840
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1841 NKLVRRTEKKLKEIFMQVEDErrhadqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE--GLS 1918
Cdd:COG4717 405 EELEEQLEELLGELEELLEAL---------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELL 475
|
410
....*....|..
gi 1907083614 1919 REVSTLKNRLRR 1930
Cdd:COG4717 476 QELEELKAELRE 487
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1067-1820 |
1.94e-09 |
|
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: 62.92 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1067 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDD---ETLHKNNALKvaRELQAQIAELQEdfesekasrnkaekQKRD 1143
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTfwsPELKKERALR--KEEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1144 LSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDE------TKNHEAQIQDMRQRHATALEELSEQLEQakr 1217
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKfstpelTEENFRRLQSEHERQAKELFLLRKTLEE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1218 FKANLEKNKQGLETDNKELACEVKVLQ-----QVKAESEHKRKK----LDAQVQE----LHAKVSEGDRLRVELAEKaNK 1284
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRriaeAEMQLGHlevlLDQKEKENIHLREELHRR-NQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1285 LQNELDNVSTLLEEAEKKGIKFAKdaagLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKNSLQEQQEEEEEARK 1360
Cdd:pfam10174 221 LQPDPAKTKALQTVIEMKDTKISS----LERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKSHSKFMKNKIDQLKQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1361 NLEK---QVLALQSQLADTKKKVDDDLGTIESLEE---AKKK----LLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELD 1430
Cdd:pfam10174 297 ELSKkesELLALQTKLETLTNQNSDCKQHIEVLKEsltAKEQraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1431 DLTVDLDHQRQIVSNLEKK----QKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLaraleealeakeeferqn 1506
Cdd:pfam10174 377 TLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL------------------ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1507 kqlrADMEDLMSSKDDVGKNV-HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlQTRDE 1585
Cdd:pfam10174 439 ----TTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH-----ASSLA 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1586 QNEEKKRLLLKQvreLEAELEDERKQRALAVASKKKMEidlkdleaQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR 1665
Cdd:pfam10174 510 SSGLKKDSKLKS---LEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQ 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1666 ASRDEIFAQSKESE-------KKLKSLEAEILQLQEELASSERARRHAEQERDEladeiansasgKSALLDEkrrlEARI 1738
Cdd:pfam10174 579 AEVERLLGILREVEnekndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK-----------KGAQLLE----EARR 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1739 AQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSD----NARQQLERQNKE-LKAKLQELEGAVKSKfK 1813
Cdd:pfam10174 644 REDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghltNLRAERRKQLEEiLEMKQEALLAAISEK-D 722
|
....*..
gi 1907083614 1814 ATISALE 1820
Cdd:pfam10174 723 ANIALLE 729
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
866-1740 |
2.01e-09 |
|
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: 63.05 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 866 EKQTKVEGELEemerKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeILHDLESRVeeeeeRNQILQNEK 945
Cdd:COG3096 279 ERRELSERALE----LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQ-AASDHLNLV-----QTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 946 -KKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEV-----------LLLEDQNSKFIKEKKLMEdRIAECSS 1013
Cdd:COG3096 349 iERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslksqladyqQALDVQQTRAIQYQQAVQ-ALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1014 QLAEEEEKAKN----LAKIRNKQEVMIS---DLEERLKKEEKTRQELEKAK---RKLDGETTdlqdqiaelQAQVDELKV 1083
Cdd:COG3096 428 LCGLPDLTPENaedyLAAFRAKEQQATEevlELEQKLSVADAARRQFEKAYelvCKIAGEVE---------RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1084 QLTKKEEELQGALARgddetlhknnalkvARELQAQIAELQEDFESEKASR------NKAEKQKRDLSEELEALKTELED 1157
Cdd:COG3096 499 ELLRRYRSQQALAQR--------------LQQLRAQLAELEQRLRQQQNAErlleefCQRIGQQLDAAEELEELLAELEA 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1158 TLDTTAAQQElrtkreqEVAELKKALEDETKNHEAQIQDMRQRH------ATALEELSEQLEQAkrfkanLEkNKQGLET 1231
Cdd:COG3096 565 QLEELEEQAA-------EAVEQRSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEA------LA-DSQEVTA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1232 DNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAN-KLQNEL-DNVStlLEeaekkgikfakD 1309
Cdd:COG3096 631 AMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGgVLLSEIyDDVT--LE-----------D 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1310 AAGLESqlqdtqelLQEETRQKL---NLSSRIRQLEEEKNSLQEqqeeeeearknlekqvLALQSQLADTkkkVDDDLGT 1386
Cdd:COG3096 698 APYFSA--------LYGPARHAIvvpDLSAVKEQLAGLEDCPED----------------LYLIEGDPDS---FDDSVFD 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1387 IESLEEAkkkllkDVEALSQRL-------EEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAE 1459
Cdd:COG3096 751 AEELEDA------VVVKLSDRQwrysrfpEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1460 EKGIsaryAEERDrAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRA-LE 1538
Cdd:COG3096 825 HLAV----AFAPD-PEAELAA-------LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADEtLA 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1539 QQVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMK---AQFERdLQTRDEQNEEKKRLL------LKQVRELEAELE 1606
Cdd:COG3096 893 DRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLkqqifaLSEVVQRRPHFS 971
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1607 DERKQRALAVASkkkmeiDLKD-LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1685
Cdd:COG3096 972 YEDAVGLLGENS------DLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 1686 EaeilqLQEELASSERARrhaeQERDELADEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:COG3096 1046 G-----VQADAEAEERAR----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1474-1702 |
2.06e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1474 AEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELED 1553
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1554 ELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlkqvrELEAELEDERKQRALAVASKKKMEIDLK-DLEAQ 1632
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRaELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1633 IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERA 1702
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
894-1262 |
2.65e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 894 EQLQAETELFAEAEEMRA-------RLAAKKQELEEILHDLESRVEEEEERNQILQNEK--KKMQAHIQDLEEQLDEEEG 964
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 965 ARQKLQLEKVTAEAKIKKmeEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAE--EEEKAKNLAKIRNKQEVMIsdleER 1042
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELERIRQEERKRELERirQEEIAMEISRMRELERLQM----ER 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1043 LKKEEKTRQELEKAkRKLDGETTDLQDQIAELQAQVDELK--------VQLTKKEEELQGALARGDDETLHKNNALKVAR 1114
Cdd:pfam17380 388 QQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1115 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEElealktELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQI 1194
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1195 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQgletdnkelacEVKVLQQVKaESEHKRKKLDAQVQ 1262
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----------EREMMRQIV-ESEKARAEYEATTP 596
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
850-1577 |
3.12e-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: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 850 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEIlhdles 929
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 930 rveeeeernqILQNEKKKMQAHIQDLEEQLDEEEGARQKLQlekvTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIA 1009
Cdd:TIGR00618 287 ----------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ----SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1010 ECsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDeLKVQLTKKE 1089
Cdd:TIGR00618 353 QE-IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1090 EELQGALARGDDETLHknnALKVARELQAQIAELQEDFESEKAsRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR 1169
Cdd:TIGR00618 431 KQQELQQRYAELCAAA---ITCTAQCEKLEKIHLQESAQSLKE-REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1170 TKREQEV-AELKKALEDE-TKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELAcevKVLQQVK 1247
Cdd:TIGR00618 507 CGSCIHPnPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT---QCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1248 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEkkgikFAKDAAGLESQLQDTQ-ELLQE 1326
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ-----CSQELALKLTALHALQlTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1327 ETRQKlnlSSRIRQLEEEKnslqeqqeeeEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQ 1406
Cdd:TIGR00618 659 RVREH---ALSIRVLPKEL----------LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1407 RLEEKVLAYDKLEKTKNRLQQELDDLtvdldHQRQIVSNLEKKQKKFDQLLAEEKgISARYAEERDRAEAEAREKETKAL 1486
Cdd:TIGR00618 726 ASSSLGSDLAAREDALNQSLKELMHQ-----ARTVLKARTEAHFNNNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTH 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1487 SLARALEealeakeeferQNKQLRADMEDLMSSKDdvgknvHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE 1566
Cdd:TIGR00618 800 LLKTLEA-----------EIGQEIPSDEDILNLQC------ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
730
....*....|.
gi 1907083614 1567 vnmQAMKAQFE 1577
Cdd:TIGR00618 863 ---QLTQEQAK 870
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
907-1486 |
3.93e-09 |
|
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: 61.76 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 907 EEMRARLAAKKQELEeilhdlesrveeeeERNQILQNEKKKMQAHIQDLEEQLDEEEGARQklqleKVTAEAKIKKMEee 986
Cdd:pfam10174 140 EEMELRIETQKQTLG--------------ARDESIKKLLEMLQSKGLPKKSGEEDWERTRR-----IAEAEMQLGHLE-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 987 vLLLEDQNSKFIKEKKLMEDRiaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEktrQELEKAKRKLDGETTD 1066
Cdd:pfam10174 199 -VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1067 LQDQIAELQA----------QVDELKVQLTKKEEELQGALARgdDETLHKNNA-----LKVARE-----------LQAQI 1120
Cdd:pfam10174 270 REEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTK--LETLTNQNSdckqhIEVLKEsltakeqraaiLQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1121 AELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAqqelrtkREQEVAELKKALE---DETKNHEAQIQDM 1197
Cdd:pfam10174 348 DALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLRDKDKQLAGL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1198 RQRHA----------TALEELSEQLEQAKRFKANLEKNKqglETDNKELACEVKVLQQvkaesehKRKKLDAQVQELHAK 1267
Cdd:pfam10174 421 KERVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKK-------ENKDLKEKVSALQPE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1268 VSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQElLQEETRQKLNLSSRIRQLEEEkns 1347
Cdd:pfam10174 491 LTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE--- 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1348 LQEQQEEEEEARKNLEKqVLALQSQLADTKKKVDDDLGTIESL------EEAKKKL-LKDVEALSQRLEEKVLA---YDK 1417
Cdd:pfam10174 567 VARYKEESGKAQAEVER-LLGILREVENEKNDKDKKIAELESLtlrqmkEQNKKVAnIKHGQQEMKKKGAQLLEearRRE 645
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1418 LEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKAL 1486
Cdd:pfam10174 646 DNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1683-1927 |
4.18e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1683 KSLEAEILQLQEELASSERARRHAEQERDELAdeiansasgksaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1762
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1763 tlQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1842
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1843 LVRRTEkklkeifMQVEDErrhADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDateanegLSREVS 1922
Cdd:COG4913 367 LLAALG-------LPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 1907083614 1923 TLKNR 1927
Cdd:COG4913 430 SLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1454 |
5.13e-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: 61.57 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 861 LLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQI 940
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 941 LQNEKKKMQAHIQDLEEQLDEEEGARQKLQLE-----KVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQL 1015
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKnqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1016 AEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELqga 1095
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI--- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1096 largddetlhknnalkvaRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaQQELRTKrEQE 1175
Cdd:TIGR04523 443 ------------------KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK------QKELKSK-EKE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1176 VAELKKaledETKNHEAQIQDMRQRHATALEELSEqleqakrfkanLEKNKQGLETDNKELACEVKvlqqvKAESEHKRK 1255
Cdd:TIGR04523 498 LKKLNE----EKKELEEKVKDLTKKISSLKEKIEK-----------LESEKKEKESKISDLEDELN-----KDDFELKKE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1256 KLDAQVQELHAKVSE----GDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFakdaagleSQLQDTQELLQEETRQk 1331
Cdd:TIGR04523 558 NLEKEIDEKNKEIEElkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI--------SSLEKELEKAKKENEK- 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1332 lnLSSRIRQLEEEKNSLQEQQeeeeearKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEK 1411
Cdd:TIGR04523 629 --LSSIIKNIKSKKNKLKQEV-------KQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITR 699
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1907083614 1412 VLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFD 1454
Cdd:TIGR04523 700 MIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFD 742
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
852-1270 |
5.54e-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: 61.19 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 852 EELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEK-----NILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 926
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 927 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED 1006
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1007 RIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLT 1086
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1087 KKEEELQgALARGDDETLHKNNALKVAR-ELQAQIAELQEDFESEKASRNKA--EKQKRDLSEELEALKTELEDTLDTTA 1163
Cdd:TIGR04523 507 ELEEKVK-DLTKKISSLKEKIEKLESEKkEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1164 AQQELRTKREQEVAELKKALEDETKnheaqiqdmrqrhatALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVL 1243
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEK---------------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
410 420
....*....|....*....|....*..
gi 1907083614 1244 QQVKAESEHKRKKLDAQVQELHAKVSE 1270
Cdd:TIGR04523 651 KETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1693-1931 |
6.03e-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: 60.16 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1693 QEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1772
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1773 LAAERSAAQKSDNARQQLERQNK-ELKAKLQELEGAVKSkfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKL 1851
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1852 KEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRG 1931
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1508-1840 |
6.89e-09 |
|
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: 60.08 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1508 QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQTRDEQN 1587
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1588 EEKKRLL---LKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEA 1664
Cdd:pfam19220 107 EELRIELrdkTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1665 RASRDEIFAQSKESEKKLKSLEAEILQLQ----EELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1741 LEEELEEEQSNMELLNDRFRKTTLQVDT-------LNTELAAERSAAQKSDNARQQLERQ----NKELKAKLQELEGAVK 1809
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKEASIERDTlerrlagLEADLERRTQQFQEMQRARAELEERaemlTKALAAKDAALERAEE 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907083614 1810 S-------------KFKATISALEAKIGQLEEQLEQEAKERAAA 1840
Cdd:pfam19220 347 RiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1404-1853 |
6.98e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1404 LSQRLEEKVLAYDKLE-KTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEerDRAEAEAREKE 1482
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--LREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1483 TKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskddvgknvHELEKSKRALEQQVEEMRTQLEELEDELQATEDAK 1562
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEEL-----------RELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1563 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL-----------AVASKKKMEIDLKDLEA 1631
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1632 QIEAA------------------NKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQ 1693
Cdd:COG4717 274 TIAGVlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1694 EELASSERARR--HAEQERDELADEIA----NSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDrfrktTLQVD 1767
Cdd:COG4717 354 REAEELEEELQleELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1768 TLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGavkskfKATISALEAKIGQLEEQLEQEAKERAAAN---KLV 1844
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE------DGELAELLQELEELKAELRELAEEWAALKlalELL 502
|
....*....
gi 1907083614 1845 RRTEKKLKE 1853
Cdd:COG4717 503 EEAREEYRE 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1391-1929 |
9.02e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 9.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1391 EEAKKKLLKDVealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARyaEE 1470
Cdd:PRK03918 144 DESREKVVRQI----LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE--LP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1471 RDRAEAEAREKETKalslaraleealeakeeferqnkqlraDMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEE 1550
Cdd:PRK03918 218 ELREELEKLEKEVK---------------------------ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1551 LEDELQATEDAKLRLEvNMQAMKAQFERDLQTRDEQNEEKKRL------LLKQVRELEAELED-ERKQRALAVASKKKME 1623
Cdd:PRK03918 271 LKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIekrlsrLEEEINGIEERIKElEEKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1624 I--DLKDLEAQIEAANKARdEVIKQLRKLQAQMKDY-----QRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEEL 1696
Cdd:PRK03918 350 LekRLEELEERHELYEEAK-AKKEELERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1697 ASSERARRH--------AEQERDEL-----------ADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN- 1756
Cdd:PRK03918 429 EELKKAKGKcpvcgrelTEEHRKELleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEl 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1757 ----------------DRFRKTTLQVDTLNTE---LAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATIS 1817
Cdd:PRK03918 509 eeklkkynleelekkaEEYEKLKEKLIKLKGEiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1818 ALEAKIGQLEEqLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEatRAN 1897
Cdd:PRK03918 589 ELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELR 665
|
570 580 590
....*....|....*....|....*....|..
gi 1907083614 1898 ASRRKLQRELDDATEANEGLSREVSTLKNRLR 1929
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1182-1411 |
9.61e-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: 59.78 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1182 ALEDETKNHEAQIQDMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQV 1261
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1262 QELHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL 1341
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1342 EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEK 1411
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
808-1591 |
1.05e-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: 60.83 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 808 KKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLE 887
Cdd:TIGR00606 285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIR 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 888 EKNILAEQLQAETEL-------FAEAE------EMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQD 954
Cdd:TIGR00606 365 ARDSLIQSLATRLELdgfergpFSERQiknfhtLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 955 LEEQLDEEEGARQ--KLQLEKVTAEAK-IKKMEEEV------LLLEDQNS----KFIKEKKLMEDRIAECSSQLAEEEEK 1021
Cdd:TIGR00606 445 KKEILEKKQEELKfvIKELQQLEGSSDrILELDQELrkaereLSKAEKNSltetLKKEVKSLQNEKADLDRKLRKLDQEM 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1022 A-KNLAKIRNKQEVMISD--------------------------------LEERLKKEEKTRQELEKAKRKLDGETTDLQ 1068
Cdd:TIGR00606 525 EqLNHHTTTRTQMEMLTKdkmdkdeqirkiksrhsdeltsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1069 DQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKN--NALKVARELQAQIA---ELQEDFESEKASRN-------- 1135
Cdd:TIGR00606 605 QNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERlkEEIEKSSKQRAMLAgatAVYSQFITQLTDENqsccpvcq 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1136 ---KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataLEELSEQL 1212
Cdd:TIGR00606 685 rvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK----LQKVNRDI 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1213 EqakRFKANLEKNKQGLETDN------KELACEVKVLQQVKAESEHKRKKLDAQVQELHAkvSEGDRLRVELAEKANKLQ 1286
Cdd:TIGR00606 761 Q---RLKNDIEEQETLLGTIMpeeesaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQ 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1287 NELDNVSTLLEEAEKkgikfakdaaglesqlqdtqeLLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV 1366
Cdd:TIGR00606 836 HELDTVVSKIELNRK---------------------LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1367 LALQSQLADTKKKVDDDLgtieSLEEAKKKLLKDVEAL-SQRLEEKVLAYDKLEKTKNRLQQELDDLTvDLDHQRQIVSN 1445
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDS----PLETFLEKDQQEKEELiSSKETSNKKAQDKVNDIKEKVKNIHGYMK-DIENKIQDGKD 969
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1446 LEKKQKKfdqllAEEKGISARYAEERDRaeaeaREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK 1525
Cdd:TIGR00606 970 DYLKQKE-----TELNTVNAQLEECEKH-----QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1526 NVHELEkskralEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQ---FERDLQTRDEQNEEKK 1591
Cdd:TIGR00606 1040 HLKEMG------QMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEikhFKKELREPQFRDAEEK 1102
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
846-1377 |
1.17e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.51 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELE 921
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 922 EILHDLESRVEEEEernQILQNEKKKMQAHIQDLEEQLDEEEGARQKL-QLEKVTAEAKIKKMEEEVLLLEDQnsKFIKE 1000
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELeEMTKFKNNKEVELEELKKILAEDE--KLLDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1001 KKLMEdRIAEcssQLAEEEEKAKNLAKIRNKQevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDE 1080
Cdd:pfam05483 424 KKQFE-KIAE---ELKGKEQELIFLLQAREKE---IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1081 LKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQedfESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1160
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1161 TTAAQQELRTKREQEVAELKKA---LEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELA 1237
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1238 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAnklQNELDNVSTLLEEAEKKGIKFAKDAaglESQL 1317
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC---QHKIAEMVALMEKHKHQYDKIIEER---DSEL 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1318 QDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTK 1377
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
860-1390 |
1.21e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.62 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 860 ELLKVKEKQTKVEGELEEMERKHQQLLEEKnilAEQLQAETELF----AEAEEMRARLAAKKQELEEILHDLESRVEEEE 935
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLpswqSELENLEERLKALTGKHQDVTAKYNRRRSKIK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 936 ERNQILQNEKKKMQAHIqdleeqldeeegaRQKLQLEKVTAEAKIKKMEEEV-LLLEDQNSKFIKEKKLMEDRIAECSSQ 1014
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKI-------------REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1015 LAEEEEKAKNLAKIRNKQEV---MISDLEERLKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQVDELKVQLTKK 1088
Cdd:pfam12128 453 LNQATATPELLLQLENFDERierAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSALDELELQLFPQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1089 ---------------EEELQGALARG---------------------------DDETLHKNNALKVARELQAQIAELQED 1126
Cdd:pfam12128 533 agtllhflrkeapdwEQSIGKVISPEllhrtdldpevwdgsvggelnlygvklDLKRIDVPEWAASEEELRERLDKAEEA 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1127 FESEKASRNKAEKQKRDLSEELEALKTELEDTLDT-----------TAAQQELRTKREQEVAELKKALEDETKNHEAQIQ 1195
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTAlknarldlrrlFDEKQSEKDKKNKALAERKDSANERLNSLEAQLK 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1196 DMRQRHATALEELSEQLEQAKRFK------------ANLEKNKQGLETDNKELACEVKVLQQVKAESEHKR-------KK 1256
Cdd:pfam12128 693 QLDKKHQAWLEEQKEQKREARTEKqaywqvvegaldAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpdviAK 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1257 LDAQVQELHAKVSEGDRLRVELAE-----------KANKLQNELDNVSTLLEEAEKKGIKFAKDA----AGLESQL---Q 1318
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTklrrAKLEMERkasE 852
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 1319 DTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKnLEKQVLALQSQLADTKKKVDDDLGTIESL 1390
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ-LEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1548-1930 |
1.66e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1548 LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDERKQRALAVASKKKME--ID 1625
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQ-EELEELEEELEELEAELEELREELEKLEklLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1626 LKDLEAQIEAANKARDEVIKQLRKLQAQMKDY---QRELEEARASRDEIFAQ--------SKESEKKLKSLEAEILQLQE 1694
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1695 ELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELA 1774
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1775 A--------ERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKL-VR 1845
Cdd:COG4717 287 AllflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1846 RTEKKLKEIFMQV----EDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEANEGLSR 1919
Cdd:COG4717 367 ELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEE 446
|
410
....*....|.
gi 1907083614 1920 EVSTLKNRLRR 1930
Cdd:COG4717 447 ELEELREELAE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1585-1789 |
1.87e-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: 58.62 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1585 EQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEE- 1663
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1664 --------------ARASRDEIFAQSKESEKKLKSLE----------AEILQLQEELASSERARRHAEQERDELADEIAN 1719
Cdd:COG4942 103 keelaellralyrlGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1720 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQ 1789
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1538-1750 |
2.62e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1538 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVA 1617
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1618 SKKKMEIDLKDLEAQIEAANKArdEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELA 1697
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1698 SSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1750
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1109-1312 |
2.81e-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: 58.24 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1109 ALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETK 1188
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1189 NHEAQIQDMRQRHATA------------------------LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ 1244
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1245 QVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAG 1312
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1196-1808 |
3.99e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1196 DMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLR 1275
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1276 VELAEKANKLQNELDNVstlleeaekkgikfakdaaglesqlqdtqellqeetrqklnlsSRIRQLEEEKNSLqeqQEEE 1355
Cdd:PRK01156 256 SEIKTAESDLSMELEKN-------------------------------------------NYYKELEERHMKI---INDP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1356 EEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLlkdvealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVD 1435
Cdd:PRK01156 290 VYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL--------SVLQKDYNDYIKKKSRYDDLNNQILELEGY 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1436 LDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREketkalslaraleealeakeeferqnkqLRADMED 1515
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA----------------------------IKKELNE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1516 LMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDE---------LQATEDAKLRLEVNMQAMKAQFERDLQTRDEQ 1586
Cdd:PRK01156 414 INVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1587 NEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEI-DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQR-ELEEA 1664
Cdd:PRK01156 494 DIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLeDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRtSWLNA 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1665 RASRD--EIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEiANSASGKSALLDEKRRLEARIAQLE 1742
Cdd:PRK01156 574 LAVISliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE-ANNLNNKYNEIQENKILIEKLRGKI 652
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1743 EELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV 1808
Cdd:PRK01156 653 DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1364-1930 |
4.14e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 58.70 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1364 KQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEekvlayDKLEKTKNRLQQELDDLTVDLDHQRQIV 1443
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1444 SNLEKKQKKFDQLLAEEKgisARYAEERD--RAEAEAREKETKALSlarALEEALEAKEEFERQNKQLRadmedlmsSKD 1521
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKALT---GKHQDVTAKYNRRRSKIKEQ--------NNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1522 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRlevnmqamkaqferdlqtrdEQNEEKKRLllkqvrel 1601
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL--------------------EFNEEEYRL-------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1602 EAELEDERKQRALAVASKKKMEidlkDLEAQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK 1681
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLL----QLENFDERIERAREE----QEAANAEVERLQSELRQARKRRDQASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1682 LKSLEAEILQLQEELASS-----ERARRHAEQERDELADEIA-------------NSASGKSAL------LDEKR----- 1732
Cdd:pfam12128 515 LEERQSALDELELQLFPQagtllHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpe 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1733 ------RLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEG 1806
Cdd:pfam12128 595 waaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1807 AVKSKFKATISALEAKIGQLEEQLeQEAKERAAANKLVRRTEKklKEIFMQVEDERRhaDQYKEQMEKANARMKQLKRQL 1886
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKH-QAWLEEQKEQKREARTEK--QAYWQVVEGALD--AQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907083614 1887 EEAEEEATRANASRrklqrelDDATEANEGLSREVSTLKNRLRR 1930
Cdd:pfam12128 750 KALETWYKRDLASL-------GVDPDVIAKLKREIRTLERKIER 786
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
905-1738 |
5.19e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 905 EAEEMRARLAAKKQELEEILHDLESRVeeeeernqilqnekKKMQAHIQDLEEQLDEEEGARQKLQL--EKVTAEAKIKK 982
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMA--------------RELAELNEAESDLEQDYQAASDHLNLvqTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 983 MEEEVLLLEDQnskfiKEKKLMEdrIAECSSQLAEEEEKAKnlakiRNKQEV-----MISDLEERLKkEEKTR------- 1050
Cdd:PRK04863 353 YQADLEELEER-----LEEQNEV--VEEADEQQEENEARAE-----AAEEEVdelksQLADYQQALD-VQQTRaiqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1051 -QELEKAKRKL---DGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETlhknNALKVARELQAQIaELQED 1126
Cdd:PRK04863 420 vQALERAKQLCglpDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEV-SRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1127 FESEKASRNKAEKQkRDLSEELEALKTELEDtldttaAQQELRTKREQE--VAELKKALEdETKNHEAQIQDMRQRHATA 1204
Cdd:PRK04863 495 WDVARELLRRLREQ-RHLAEQLQQLRMRLSE------LEQRLRQQQRAErlLAEFCKRLG-KNLDDEDELEQLQEELEAR 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1205 LEELSEQLEQAkrfkanleknkqgletdnkelacevkvlQQVKAESEHKRKKLDAQVQELHAKVSEGdrlrVELAEKANK 1284
Cdd:PRK04863 567 LESLSESVSEA----------------------------RERRMALRQQLEQLQARIQRLAARAPAW----LAAQDALAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1285 LQneldnvstlleeaEKKGIKFAkDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEK 1364
Cdd:PRK04863 615 LR-------------EQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1365 QVLA-LQSQLADtkkkvD---DDLGTIES-------------LEEAKKKLLKD---------VEALSQRLEEKVLAYDKL 1418
Cdd:PRK04863 681 RFGGvLLSEIYD-----DvslEDAPYFSAlygparhaivvpdLSDAAEQLAGLedcpedlylIEGDPDSFDDSVFSVEEL 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1419 EKT--------------------------KNR---LQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAE 1469
Cdd:PRK04863 756 EKAvvvkiadrqwrysrfpevplfgraarEKRieqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADP 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1470 ERDRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDvgknvhelekskRALEQQVEEMRTQL 1548
Cdd:PRK04863 836 EAELRQLNRRRVElERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD------------ETLADRVEEIREQL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1549 EELEDE---LQATEDAKLRLE---VNMQAMKAQFERdLQTRDEQNEEKKRLLLKQVRELeaeleDERKQRALAVASKKKM 1622
Cdd:PRK04863 904 DEAEEAkrfVQQHGNALAQLEpivSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TEVVQRRAHFSYEDAA 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1623 EIDLKD------LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEaeiLQLQEEL 1696
Cdd:PRK04863 978 EMLAKNsdlnekLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLG---VPADSGA 1054
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1907083614 1697 AssERARRHaeqeRDELADEIANSASGKSALLDEKRRLEARI 1738
Cdd:PRK04863 1055 E--ERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1442-1912 |
5.58e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1442 IVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskd 1521
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1522 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE-VNMQAMKAQFERDLQTRDEQNEEKKRL--LLKQV 1598
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEELEELLEQLSLATEEELqdLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1599 RELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKArdEVIKQLRKLQAQM-------------KDYQRELEEAR 1665
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAaallallglggslLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1666 ASRDEIFAQSKESEKKLKsleAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEEL 1745
Cdd:COG4717 280 FLVLGLLALLFLLLAREK---ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1746 EEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSdNARQQLERQNKELKAKLQELEGAVKSKFKA-TISALEAKIG 1824
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1825 QLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQ 1904
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
....*...
gi 1907083614 1905 RELDDATE 1912
Cdd:COG4717 516 PVLERASE 523
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1520-1740 |
5.64e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.10 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1520 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVR 1599
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEE-AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1600 ELEAELEDERKQRALAVASKKKMEID--LKDLEAQIEAANKARDEVIK-------QLRKLQAQMKDYQREL-EEARASRD 1669
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1670 EIFAQSKESEKKLKSLEAEILQLQEELAS-SERARRHAEQERD-ELADEIANSasgksaLLdeKRRLEARIAQ 1740
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1072-1372 |
6.08e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 58.00 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1072 AELQAQVDELKVQltKKEEELQGALARGDDETLhknnalkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEAL 1151
Cdd:PRK11281 39 ADVQAQLDALNKQ--KLLEAEDKLVQQDLEQTL----------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1152 KTELEDTLDTTAAQQELR------TKREQEVAELKKALeDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKN 1225
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRqlesrlAQTLDQLQNAQNDL-AEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1226 KQGLETDNK-ELACEvkvLQQVKAESEHKRKKLDA--QVQELhakvseGDRLRVELAEKANKLQNELdnvsTLLEEA--E 1300
Cdd:PRK11281 186 GKALRPSQRvLLQAE---QALLNAQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQL----QLLQEAinS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1301 KKGIKFAKDAAGLESQlQDTQE-----LLQEETRQKLNLSSRIRQLEEEKNSLQeqqeeeeeaRKNLE-KQVL--ALQSQ 1372
Cdd:PRK11281 253 KRLTLSEKTVQEAQSQ-DEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLT---------QQNLRvKNWLdrLTQSE 322
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1465-1837 |
6.59e-08 |
|
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: 57.60 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1465 ARYAEERDRaEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1544
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1545 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLllkQVRELEAELEDERKQRALAVASKKkmei 1624
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL---QAKLQQTEEELRSLSKEFQELRNS---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1625 dlkdLEAQIEAANKARDEVIKQLRKL-QAQMKDYQRE--LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1701
Cdd:pfam07888 201 ----LAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEalLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1702 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERsaaq 1781
Cdd:pfam07888 277 ARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK---- 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1782 ksDNARQQL---ERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAKER 1837
Cdd:pfam07888 353 --DCNRVQLsesRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
845-1217 |
8.34e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 845 LQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEL---- 920
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 921 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKE 1000
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1001 KK---------------LMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETT 1065
Cdd:COG4717 271 LIltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1066 DLQDQIAELQAQVdELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQkrdls 1145
Cdd:COG4717 351 ELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA----- 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 1146 EELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEaqIQDMRQRHATALEELSEQLEQAKR 1217
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1358-1621 |
8.71e-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: 56.70 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1358 ARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEkvlaydkLEKTKNRLQQELDDLTvdld 1437
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1438 hqrqivSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM 1517
Cdd:COG4942 83 ------AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1518 SSKDdvgknvhELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRlLLKQ 1597
Cdd:COG4942 157 ADLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEAL 228
|
250 260
....*....|....*....|....
gi 1907083614 1598 VRELEAELEDERKQRALAVASKKK 1621
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1256-1810 |
1.01e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1256 KLDAQVQELHAKVSEGDRLRVELAEKanklQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQ---DTQELLQEETRQKL 1332
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSS----NLELENIKKQIADDEKSHSITLKEIERLSIEYNnamDDYNNLKSALNELS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1333 NLSSRIRQLEEE---KNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLE 1409
Cdd:PRK01156 246 SLEDMKNRYESEiktAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1410 E--KVLA--------YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAR 1479
Cdd:PRK01156 326 AiiKKLSvlqkdyndYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1480 EketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEL---------------EKSKRALEQQVEE- 1543
Cdd:PRK01156 406 A-------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeEKSNHIINHYNEKk 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1544 --MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKkRLLLKQVRELEAELEDERKQRALAVASKKK 1621
Cdd:PRK01156 479 srLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-RADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1622 MeiDLKDLEAQ---------------IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFaqsKESEKKLKSLE 1686
Cdd:PRK01156 558 L--KLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI---REIENEANNLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1687 AEILQLQEELASSERARRHAEQERDELAdeiansasGKSALLDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTLQV 1766
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSIIPDLKEITSRIND--------------IEDNLKKSRKAL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907083614 1767 DTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKS 1810
Cdd:PRK01156 691 DDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
979-1842 |
1.03e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.75 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 979 KIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAK--------NLAKIRNKQEVMISD------------ 1038
Cdd:TIGR01612 815 KSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKekidseheQFAELTNKIKAEISDdklndyekkfnd 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1039 ----LEERLKKEEKTRQELEKAKrKLDG-----ETTdlQDQIAELQAQVDELKVQLTKKEEELQgalargDDETLHKNNA 1109
Cdd:TIGR01612 895 skslINEINKSIEEEYQNINTLK-KVDEyikicENT--KESIEKFHNKQNILKEILNKNIDTIK------ESNLIEKSYK 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1110 LKVARELQAQIAELQEDFEseKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQelRTKREQEVAELKKALEDETKN 1189
Cdd:TIGR01612 966 DKFDNTLIDKINELDKAFK--DASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQ--FDEKEKATNDIEQKIEDANKN 1041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1190 heaqIQDMRQRHATALEELSEQLEqaKRFKANLEK-NKQGLETDNKELACEVKVLQQVK------------AESEHKRKK 1256
Cdd:TIGR01612 1042 ----IPNIEIAIHTSIYNIIDEIE--KEIGKNIELlNKEILEEAEINITNFNEIKEKLKhynfddfgkeenIKYADEINK 1115
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1257 LDAQVQELHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIK--FAKDAAGLESQLQ------DTQELLQEET 1328
Cdd:TIGR01612 1116 IKDDIKNLDQKI---DHHIKALEEIKKKSENYIDEIKAQINDLEDVADKaiSNDDPEEIEKKIEnivtkiDKKKNIYDEI 1192
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1329 RQKLNlssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLalqSQLADTKKKVDDdlgTIESLEeAKKKLLKDVEALSQRL 1408
Cdd:TIGR01612 1193 KKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGKLFL---EKIDEEKKKSEH---MIKAME-AYIEDLDEIKEKSPEI 1262
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1409 EEKVLAYDKLEKTKNRLQQELDD----LTVDLDHQRQIvSNLEKKQKKFDQLLAEEKGIS------ARYAEERDRAEAEA 1478
Cdd:TIGR01612 1263 ENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI-SDIREKSLKIIEDFSEESDINdikkelQKNLLDAQKHNSDI 1341
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1479 REKETKALSLARALEEALEakeeferqnKQLRADMEDLMSSKDDVGKNVH-ELEKSKRALEQQVEEmrTQLEELEDELQA 1557
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNKI---------KKIIDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDD--INLEECKSKIES 1410
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1558 TEDAKLRLEV--NMQAMKAQF---ERDLQT---RDEQNEEKKRLLLKQVreleaELEDERKQRALAVA---SKKKMEIDL 1626
Cdd:TIGR01612 1411 TLDDKDIDECikKIKELKNHIlseESNIDTyfkNADENNENVLLLFKNI-----EMADNKSQHILKIKkdnATNDHDFNI 1485
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1627 KDLEAQIEAANKARDEV---IKQLRKLQAQMKDYQRE---------------------------LEEARASRDEIFAQSK 1676
Cdd:TIGR01612 1486 NELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDvtellnkysalaiknkfaktkkdseiiIKEIKDAHKKFILEAE 1565
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1677 ESEKKLKSLEAEILQLQEELASSERARRHAEQERDELAD------EIANSASGKSALLDEKRRLEARIaqleeeleeeqs 1750
Cdd:TIGR01612 1566 KSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKINDCLKETESIEKKI------------ 1633
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1751 nmellndrfrkTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGaVKSKFKATISALEAKIGQLEEQL 1830
Cdd:TIGR01612 1634 -----------SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE-LDSEIEKIEIDVDQHKKNYEIGI 1701
|
970
....*....|..
gi 1907083614 1831 EQEAKERAAANK 1842
Cdd:TIGR01612 1702 IEKIKEIAIANK 1713
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
874-1098 |
1.08e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 874 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIq 953
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 954 dleeqldeeegARQKLQLEKVTAEA-KIKKMEEEVLLLEDQN-SKFIKEKKLME-------DRIAECSSQLAEEEEKAKN 1024
Cdd:COG4942 100 -----------EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKylaparrEQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083614 1025 LAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALAR 1098
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
870-1333 |
1.14e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 870 KVEGELEEMERKHQQLLEeknILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdLESRVEEEEERNQILQNEKKKMQ 949
Cdd:COG4717 50 RLEKEADELFKPQGRKPE---LNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 950 AHIqdleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIR 1029
Cdd:COG4717 123 KLL------------QLLPLYQELEALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1030 NKQEvmisdlEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEE------------------ 1091
Cdd:COG4717 187 SLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaalla 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1092 LQGALARGDDETLHKNNAL---------------KVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1156
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1157 DTLDTTAAQQELRTKREQEVAELKKAledetKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQ-----GLET 1231
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLE-----ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEEleeqlEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1232 DNKELACEVKVLQQVKAESEHKRKKLDA---QVQELHAKVSEgDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAK 1308
Cdd:COG4717 416 GELEELLEALDEEELEEELEELEEELEEleeELEELREELAE-LEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
490 500
....*....|....*....|....*
gi 1907083614 1309 DAAGLESqLQDTQELLQEETRQKLN 1333
Cdd:COG4717 495 LKLALEL-LEEAREEYREERLPPVL 518
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1277-1908 |
1.85e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.27 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1277 ELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNSLQEQQEE 1354
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnaTRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1355 EEEA-----RKNLEKQVLALQSQLADTKK-------KVDDDLGTIESLEEAKKKLLKDVEAlsqrlEEKVLAYDKLEKtk 1422
Cdd:pfam05483 180 ETRQvymdlNNNIEKMILAFEELRVQAENarlemhfKLKEDHEKIQHLEEEYKKEINDKEK-----QVSLLLIQITEK-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1423 nrlQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgisaryaeerDRAEAEAREKETKALSLARALEEALEAKEEF 1502
Cdd:pfam05483 253 ---ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI----------EKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1503 ERQNKQL-------RADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--ATEDAKLRLEVN-MQAM 1572
Cdd:pfam05483 320 QIATKTIcqlteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSELEeMTKF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1573 KAQFERDLQTRDEQNEEKKRLLL--KQVRELEAELEDERKQRALAVASKKKmeiDLKDLEAQIEAANKARDEVIKQLRKL 1650
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREK---EIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1651 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERarrhaeqERDELADEIANSASGKSALLDE 1730
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK-------QEERMLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1731 krrLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELaaeRSAAQKSDNARQQLERQNKELKaKLQELEGAVKS 1810
Cdd:pfam05483 550 ---LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM---KILENKCNNLKKQIENKNKNIE-ELHQENKALKK 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1811 KFKA---TISALEAKIGQLEEQLEqeakerAAANKLVRRTEKKLKEIfmqvEDERRHADQYKEQMEKANARMKQLKrqle 1887
Cdd:pfam05483 623 KGSAenkQLNAYEIKVNKLELELA------SAKQKFEEIIDNYQKEI----EDKKISEEKLLEEVEKAKAIADEAV---- 688
|
650 660
....*....|....*....|.
gi 1907083614 1888 eaeeeatranasrrKLQRELD 1908
Cdd:pfam05483 689 --------------KLQKEID 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1129-1368 |
1.95e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1129 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALedetKNHEAQIQDMRQRHATALEEL 1208
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1209 SEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNE 1288
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1289 LDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLA 1368
Cdd:COG4942 173 RAELEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1398-1930 |
2.27e-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: 56.21 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1398 LKDVEALSQRLEE------KVLAYDKLEKTKNRLQQELDDLTVDLDHQRQivsNLEKKQKKFDQLLAEE------KGISA 1465
Cdd:TIGR00606 165 LSEGKALKQKFDEifsatrYIKALETLRQVRQTQGQKVQEHQMELKYLKQ---YKEKACEIRDQITSKEaqlessREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1466 RYAEERDRAEAEAREKE---TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK-RALEQQV 1541
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1542 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFER-------------DLQTRDEQNEEKKRLLLKQVRELEAELEDE 1608
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehirardsliqSLATRLELDGFERGPFSERQIKNFHTLVIE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1609 RKQRALAVASKKKMEIDLKDLEAQiEAANKARDEVI----------KQLRKLQAQMKDYQRELEEARASRDEIFAQSKES 1678
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQ-EQADEIRDEKKglgrtielkkEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1679 EKKLKSL------------EAEILQLQEELASSERARRHAEQERDELADEIAN-----SASGKSALLDEK-RRLEARIAQ 1740
Cdd:TIGR00606 481 RKAERELskaeknsltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtqmeMLTKDKMDKDEQiRKIKSRHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1741 LEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVkskFKATIS-AL 1819
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL---FDVCGSqDE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1820 EAKIGQLEEQLEQEAKERA---AANKL---------------------VRRTEKKLKEIFMQVEDERRHADQYKEQMEKA 1875
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAmlaGATAVysqfitqltdenqsccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESE 717
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 1876 NARMKqlKRQLEEAEEEATRANASRRKlQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:TIGR00606 718 LKKKE--KRRDEMLGLAPGRQSIIDLK-EKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1277-1924 |
2.30e-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: 56.39 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1277 ELAEKANKLQNELDNVSTLleEAEKKGIKFA-KDAAGLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNSLQEQQEEE 1355
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESA--ELRLSHLHFGyKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1356 EEARKNLEKQVLALQSQLadtKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQ-------- 1427
Cdd:pfam12128 314 DAAVAKDRSELEALEDQH---GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSkikeqnnr 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1428 ELDDLTVDLDHQRQ-IVSNLEKKQKKFDQLLA---------------EEKGISARYAEERDRAEAEAREKETKALSLARA 1491
Cdd:pfam12128 391 DIAGIKDKLAKIREaRDRQLAVAEDDLQALESelreqleagklefneEEYRLKSRLGELKLRLNQATATPELLLQLENFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1492 LEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHElekskRALEQQVEEMRTQLEELEDELQA----------TEDA 1561
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEAL-----RQASRRLEERQSALDELELQLFPqagtllhflrKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1562 KLRLEVNMQAMKAQFER--------DLQTRDEQNEEKKRLLLKQVRELE-AELEDERKQRAlavaskKKMEIDLKDLEAQ 1632
Cdd:pfam12128 546 DWEQSIGKVISPELLHRtdldpevwDGSVGGELNLYGVKLDLKRIDVPEwAASEEELRERL------DKAEEALQSAREK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1633 IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQsKESEKklksleaeiLQLQEELassERARRHAEQERDE 1712
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE-KQSEK---------DKKNKAL---AERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1713 LADEIANSASGKSALLDEKRR--LEARIAQLeeeleeeQSNMELLNDRfrktTLQVDTLNTELAAERSAAqksDNARQQL 1790
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL----DAQLALLKAAIAARRSGA---KAELKAL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1791 ERQNK-ELKAKLQELEgavkskfkaTISALEAKIGQLEEQLEQEAKERAAanklVRRTEKKLKEIFMQvederrHADQYK 1869
Cdd:pfam12128 753 ETWYKrDLASLGVDPD---------VIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQ------RRPRLA 813
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1870 EQMEKANARMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTL 1924
Cdd:pfam12128 814 TQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1528-1924 |
2.39e-07 |
|
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: 56.11 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1528 HELEKSKRAL---EQQVEEMRTQLEE-------LEDELQATEDaklRLEVNMQAMKAQfERDLQTRDEQNEEKKRLllkq 1597
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQ-EKIERYQEDLEELTERL---- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1598 vRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEviKQLRKLQAQMKdyQRELEEARA-------SRDE 1670
Cdd:COG3096 364 -EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDV--QQTRAIQYQQA--VQALEKARAlcglpdlTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1671 IFAQSKESEKKLKSLEAEILQLQEELASSERARR---HAEQERDELADEIANSASGKSA--LLDEKRRLEARIAQleeel 1745
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAWQTAreLLRRYRSQQALAQR----- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1746 eeeqsnmellndrfrkttlqVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatisALEAKIGQ 1825
Cdd:COG3096 514 --------------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1826 LEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKeqmeKANARMKQLKRQLEEAEEEATRANASR----- 1900
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMqqlle 637
|
410 420
....*....|....*....|....*.
gi 1907083614 1901 --RKLQRELDDATEANEGLSREVSTL 1924
Cdd:COG3096 638 reREATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1321-1541 |
2.92e-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: 54.77 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1321 QELLQEETRQKLN-LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK 1399
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1400 DVEALSQRLEEKVLAYDKLEKTKNRL----QQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1475
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1476 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1541
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1507-1723 |
3.63e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1507 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDaklRLEVNMQAMKAQFeRDLQTRDEQ 1586
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGERA-RALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1587 NEEKKRLL--------LKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ 1658
Cdd:COG3883 102 VSYLDVLLgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 1659 RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASG 1723
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1040-1311 |
6.24e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1040 EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQgalargddetlhknnalkvarELQAQ 1119
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---------------------KLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1120 IAELQEDFESEKA---SRNKAEKQKRDLSEELEALK--TELEDTLDTTAAqqelrtkreqevaelkkaledetknheaqI 1194
Cdd:COG3883 74 IAEAEAEIEERREelgERARALYRSGGSVSYLDVLLgsESFSDFLDRLSA-----------------------------L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1195 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRL 1274
Cdd:COG3883 125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907083614 1275 RVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAA 1311
Cdd:COG3883 205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1073 |
6.99e-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: 53.61 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 850 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELEEILH 925
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 926 DLESRVEEEEERNQILQnekKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEevllLEDQNSKFIKEKKLME 1005
Cdd:COG4942 98 ELEAQKEELAELLRALY---RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1006 DRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1073
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1292-1865 |
9.28e-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: 53.98 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1292 VSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNslqeqqEEEEEARKNLEKQVLALQS 1371
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREA------EAEEALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1372 QLADTKKKVDDDLgTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQK 1451
Cdd:pfam05557 85 LEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1452 kfdqllaeekgisaryaeerDRAEAEAREKETKalslARALEEALEAKEEFERQNKQLR-ADMEDLMSSKDDVGKNVHEL 1530
Cdd:pfam05557 164 --------------------SLAEAEQRIKELE----FEIQSQEQDSEIVKNSKSELARiPELEKELERLREHNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1531 EKSKRALEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKAQFE---------RDLQTRDEQNEEKKRLLLKQV 1598
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSWVKLAQdtglnlrspEDLSRRIEQLQQREIVLKEEN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1599 RELEAELEDERKQRalavaskKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARA---SRDEIFAQS 1675
Cdd:pfam05557 300 SSLTSSARQLEKAR-------RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1676 KESEKKLKSLE--AEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNME 1753
Cdd:pfam05557 373 NYSPQLLERIEeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1754 LL--NDRFR--KTTLQVDTLNTELAAERSAA-----QKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG 1824
Cdd:pfam05557 453 LEleRQRLReqKNELEMELERRCLQGDYDPKktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907083614 1825 QLEEQLEQEAKERAAANKLVRRTEKK---LKEIFMQVEDERRHA 1865
Cdd:pfam05557 533 LPETTSTMNFKEVLDLRKELESAELKnqrLKEVFQAKIQEFRDV 576
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1050-1913 |
1.02e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1050 RQELEKAKRKLDGEttdlQDQIAELQAQVDELKVQLTKKEEELQGALARgddetLHK-NNAL----KVAR------ELQA 1118
Cdd:PRK04863 292 RRELYTSRRQLAAE----QYRLVEMARELAELNEAESDLEQDYQAASDH-----LNLvQTALrqqeKIERyqadleELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1119 QIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALE---------DETKN 1189
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglpdltaDNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1190 HEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEH-KRKKLDAQVQELHAKV 1268
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLrEQRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1269 SEGDRlRVELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1348
Cdd:PRK04863 523 SELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1349 qeqqeeeeeaRKNLEKQV---LALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQrleekvlAYDKLEKTKNRL 1425
Cdd:PRK04863 595 ----------IQRLAARApawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTV-------ERDELAARKQAL 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1426 QQELDDL----TVDLDHQRQI--------VSNLekkqkkFDQLLAEEKG-ISARYAEER------DraeaeareketkaL 1486
Cdd:PRK04863 658 DEEIERLsqpgGSEDPRLNALaerfggvlLSEI------YDDVSLEDAPyFSALYGPARhaivvpD-------------L 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1487 SLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEKS----------------------KRALE 1538
Cdd:PRK04863 719 SDAA-------------EQLAGLEDCPEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAARE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1539 QQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-----DEQNEEKKRLLLKQVRELEAELED----E 1608
Cdd:PRK04863 786 KRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1609 RKQRALAVASKKKMEiDLKDLEAQIEAAnkARDEVIKQLRKLQAQMKdyqrELEEARASRDE---IFAQSKESEKKLKSL 1685
Cdd:PRK04863 861 QQQRSQLEQAKEGLS-ALNRLLPRLNLL--ADETLADRVEEIREQLD----EAEEAKRFVQQhgnALAQLEPIVSVLQSD 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1686 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSAllDEKRRLEAriaqleeeleeEQSNMELLNDRFRKTTLQ 1765
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAK-----------NSDLNEKLRQRLEQAEQE 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1766 VDTLNTELaaeRSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatisALEAKIGQLEEQLEQEAKERAAANKlvr 1845
Cdd:PRK04863 1001 RTRAREQL---RQAQAQLAQYNQVLASLKSSYDAKRQMLQ------------ELKQELQDLGVPADSGAEERARARR--- 1062
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1846 rtekklKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLeeaeeeatranasrRKLQRELDDATEA 1913
Cdd:PRK04863 1063 ------DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL--------------RKLERDYHEMREQ 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1032-1489 |
1.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1032 QEVMISDLEERLKKEektRQELEKAKRKLDgetTDLQDQIAELQAQVDELKVQlTKKEEELQGALARGDDETLHKNNALK 1111
Cdd:COG4717 40 LAFIRAMLLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1112 VARELQAQIAELQEDFESEKAsRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHE 1191
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1192 AQIQDMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEG 1271
Cdd:COG4717 192 EELQDLAEE----LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1272 DRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLS-----SRIRQLEEEKN 1346
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdlspEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1347 SLQEQQEEEEEARKNLEKQVL--ALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEK--TK 1422
Cdd:COG4717 348 ELQELLREAEELEEELQLEELeqEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1423 NRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLL--AEEKGISARYAEERDRAEAEAREKETKALSLA 1489
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1060-1302 |
1.71e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1060 LDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALArgddetlhKNNALKVARELQ---AQIAELQEDFESEKASRNK 1136
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ--------KNGLVDLSEEAKlllQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1137 AEKQKRDLSEELEALKTELEDTLDTTAAQQeLRTKREQEVAELKKALEDETKNHEaQIQDMRQRhataLEELSEQLEQ-A 1215
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSARYTPNHP-DVIALRAQ----IAALRAQLQQeA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1216 KRFKANLEKNKQGLETdnkelacevkvlqqvkaesehKRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTL 1295
Cdd:COG3206 312 QRILASLEAELEALQA---------------------REASLQAQLAQLEARLAELPELEAELRR----LEREVEVAREL 366
|
....*..
gi 1907083614 1296 LEEAEKK 1302
Cdd:COG3206 367 YESLLQR 373
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1529-1807 |
1.79e-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: 53.20 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRdeQNEEKKRLL-----------L 1595
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELerirqeeiameI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1596 KQVRELE--------------AELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1661
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1662 EEARASRDEIFAQsKESEKKLKSLEAEILQLQEELASSERaRRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQL 1741
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1742 EEELEEEQSNMELLNDRFRKTTLQVDTLNTElaaERSAAQKSDNARQQLeRQNKELKAKLQELEGA 1807
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATE---ERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1047-1324 |
2.07e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.84 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1047 EKTRQeLEKAKRKLDGETTDLQDQ---------------IAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALK 1111
Cdd:pfam00038 18 DKVRF-LEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1112 VARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTEledtldttaaqqelrtkREQEVAELKKALEDETKNHE 1191
Cdd:pfam00038 97 LRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN-----------------HEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1192 ---AQIQDMrqrhATALEELSEQLE-QAKRFKANLEKN-KQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1266
Cdd:pfam00038 160 mdaARKLDL----TSALAEIRAQYEeIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1267 KVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgiKFAKDAAGLESQLQDTQELL 1324
Cdd:pfam00038 236 LKKQKASLERQLAETEERYELQLADYQELISELEA---ELQETRQEMARQLREYQELL 290
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1600-1846 |
2.09e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1600 ELEAELeDERKQRALAVASKKKMEIDLK---DLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1676
Cdd:PRK11281 40 DVQAQL-DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1677 ES------EKKLKSLEAEILQLQEELAS-----------SERARR---HAEQERDELADEIANSASGKSALLDEKR-RLE 1735
Cdd:PRK11281 119 STlslrqlESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1736 ARIAQleeeleeeqsnMELLNDrFRKTTLQVDTLNTELAAER----SAAQksdnarQQLERQnkelkakLQELEGAVKSK 1811
Cdd:PRK11281 199 AEQAL-----------LNAQND-LQRKSLEGNTQLQDLLQKQrdylTARI------QRLEHQ-------LQLLQEAINSK 253
|
250 260 270
....*....|....*....|....*....|....*
gi 1907083614 1812 fkatisALEAKIGQLEEQLEQEAKERAAANKLVRR 1846
Cdd:PRK11281 254 ------RLTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
851-1263 |
2.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 851 EEELQAKDEELLKVKEKQTKVEGELEEMER--KHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE 928
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 929 SrveEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR- 1007
Cdd:COG4717 174 E---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1008 -------IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQElEKAKRKLDGETTDLQDQiaELQAQVDE 1080
Cdd:COG4717 251 llliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK-EAEELQALPALEELEEE--ELEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1081 LKVQLTKKEEELQGALARGDDetlhknnalkvARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1160
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEE-----------LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1161 TTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelacev 1240
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE------ 470
|
410 420
....*....|....*....|...
gi 1907083614 1241 kvLQQVKAESEHKRKKLDAQVQE 1263
Cdd:COG4717 471 --LAELLQELEELKAELRELAEE 491
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1539-1916 |
3.25e-06 |
|
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: 52.53 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1539 QQVEEMRTQLEELEDELQATEDAKLRL---EVNMQAMKAQFERDLQTRDEQNEEKK---RLLLKQVRELEAELEDERKQR 1612
Cdd:pfam12128 234 AGIMKIRPEFTKLQQEFNTLESAELRLshlHFGYKSDETLIASRQEERQETSAELNqllRTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1613 ALAVAsKKKMEIDLkdLEAQIEAANKARDEVIK----QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS-LEA 1687
Cdd:pfam12128 314 DAAVA-KDRSELEA--LEDQHGAFLDADIETAAadqeQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1688 EILQLQEELASS--ERARRHAEQE----------RDELADEIANSASG----KSALLDEKRRLEARIAQLEEELEEEQSN 1751
Cdd:pfam12128 391 DIAGIKDKLAKIreARDRQLAVAEddlqaleselREQLEAGKLEFNEEeyrlKSRLGELKLRLNQATATPELLLQLENFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1752 MEL--LNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatiSALEAKIGQLEEQ 1829
Cdd:pfam12128 471 ERIerAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE-----------LQLFPQAGTLLHF 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1830 LEQEAKE------RAAANKLVRRTEK--------------------KLKEI----FMQVEDE-RRHADQYKEQMEKANAR 1878
Cdd:pfam12128 540 LRKEAPDweqsigKVISPELLHRTDLdpevwdgsvggelnlygvklDLKRIdvpeWAASEEElRERLDKAEEALQSAREK 619
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907083614 1879 MKQLKRQLEEaeeeatrANASRRKLQRELDDATEANEG 1916
Cdd:pfam12128 620 QAAAEEQLVQ-------ANGELEKASREETFARTALKN 650
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1673-1912 |
3.55e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1673 AQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDeladeIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNM 1752
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1753 ELLNDRFRKTTLQVDTLNtelaaersaaqkSDNARQQLERQNKELKAKLQELEgavkSKFKA---TISALEAKIGQLEEQ 1829
Cdd:COG3206 243 AALRAQLGSGPDALPELL------------QSPVIQQLRAQLAELEAELAELS----ARYTPnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1830 LEQEAKERAAanklvrrtekklkEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEaeeeatranasRRKLQRELDD 1909
Cdd:COG3206 307 LQQEAQRILA-------------SLEAELEALQAREASLQAQLAQLEARLAELPELEAE-----------LRRLEREVEV 362
|
...
gi 1907083614 1910 ATE 1912
Cdd:COG3206 363 ARE 365
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1071-1327 |
4.29e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 52.14 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1071 IAELQAQVDELKVQLTKKEEElQGALArgdDETLHKNNALKVARELQAQIAEL---QEDFES--EKASRNKAEKQKRDLS 1145
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAA-QNALA---DKERAEADRQRLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1146 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELKKALE---DETKNH-EAQIQDMRQRHATALEELSEQLE 1213
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQeqlDDAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1214 QAKRFKANLEKNKQGLETDNKelacevkvlqqvKAESEHKRKKLDAQVQELHAKVSEGDrlrvelaekanklqneldnVS 1293
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDID------------DAKADAEKRKDDALAKQNEAQQAESD-------------------AN 1741
|
250 260 270
....*....|....*....|....*....|....*
gi 1907083614 1294 TLLEEAEKKGIKFAKDAAGLESQLQ-DTQELLQEE 1327
Cdd:NF012221 1742 AAANDAQSRGEQDASAAENKANQAQaDAKGAKQDE 1776
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1574-1912 |
4.37e-06 |
|
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: 52.26 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1574 AQFERDLQ-TRDEQNEEKKRLL-----LKQVRELEAELEDE---------RKQRALAVASK-KKMEIDLKDLEAQIEAAN 1637
Cdd:COG3096 288 LELRRELFgARRQLAEEQYRLVemareLEELSARESDLEQDyqaasdhlnLVQTALRQQEKiERYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1638 KARDEVIKQLRKLQAQmkdyqreLEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR-------HAEQER 1710
Cdd:COG3096 368 EVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcglpdlTPENAE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1711 DELADEIANSASGKSALLDEKRRLeariaqleeeleeeqSNMELLNDRFRKTtLQvdtLNTELAAERSAAQKSDNARQQL 1790
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKL---------------SVADAARRQFEKA-YE---LVCKIAGEVERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1791 eRQNKELKAKLQELEgavkskfkatisALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeifmqvederrHADQYKE 1870
Cdd:COG3096 502 -RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----------AAEELEE 557
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907083614 1871 QMEKANARMKQLKRQLEeaeeeatRANASRRKLQRELDDATE 1912
Cdd:COG3096 558 LLAELEAQLEELEEQAA-------EAVEQRSELRQQLEQLRA 592
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1589-1884 |
4.66e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1589 EKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASR 1668
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1669 DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKsALLDEKRRLEARIAQLEEELEEE 1748
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1749 QSNMELLNdRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELegavkskfKATISALEAKIGQLEE 1828
Cdd:COG1340 160 EKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL--------HKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1829 QLEQEAKEraaanklVRRTEKKLKEIFMQVEDERRHADQyKEQMEKANARMKQLKR 1884
Cdd:COG1340 231 EIIELQKE-------LRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
909-1370 |
4.80e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 909 MRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVL 988
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 989 LLED--QNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNkqevmisDLEERLKKEEKTRQELEKAKRKLDGET-- 1064
Cdd:COG4717 120 KLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEE-------ELEELEAELAELQEELEELLEQLSLATee 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1065 --TDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDD-----ETLHKNNALKVARELQAQIAELQEdFESEKASRNKA 1137
Cdd:COG4717 193 elQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlenelEAAALEERLKEARLLLLIAAALLA-LLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1138 EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKR 1217
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1218 FKANLEKNKQGLETDNKELACEvKVLQQVKAESEHKRKKLDAQVQELHAkvsegdrLRVELAEKANKLQNELDNVSTLLE 1297
Cdd:COG4717 352 LLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQE-------LKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 1298 EAEKKGIKfaKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKN--SLQEQQEEEEEARKNLEKQVLALQ 1370
Cdd:COG4717 424 ALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALK 496
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
851-1437 |
4.97e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 851 EEELQAKDEELLKVKE-------KQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 923
Cdd:PRK01156 189 EEKLKSSNLELENIKKqiaddekSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 924 LHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ---LEKVTAEAKIKKMEEevllLEDQNSKFIKE 1000
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1001 KKLMEDRIAECS----------SQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1070
Cdd:PRK01156 345 KSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1071 IAELQAQVDELKVQLTKKEEELQGALAR----------GDDETLH--------KNNALKVARELQAQIAELQEDFESEKA 1132
Cdd:PRK01156 425 VSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlGEEKSNHiinhynekKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1133 SRNKAEKQKRDLSE----ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKA-LEDETKNHEAQIQDMRQRHATALEE 1207
Cdd:PRK01156 505 RKEYLESEEINKSIneynKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIET 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1208 LSEQLEQAKRFKANLEKNKQGLETDnkelacevkvLQQVKAESEHKRKKLDAQVQELHAKVsegdrlrvelaekanklqN 1287
Cdd:PRK01156 585 NRSRSNEIKKQLNDLESRLQEIEIG----------FPDDKSYIDKSIREIENEANNLNNKY------------------N 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1288 ELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQEllqeetrqklnLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVL 1367
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE-----------ITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1368 ALQSQLADTKKKVDDDLGTIESLEEAKKKL--LKDV-EALSQ-------RLEEKVLAYDKLEKTKNRLQQELDDLTVDLD 1437
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMKKIKKAIgdLKRLrEAFDKsgvpamiRKSASQAMTSLTRKYLFEFNLDFDDIDVDQD 785
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
802-1299 |
6.01e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 802 ARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWWRVFTKVKpLLQ--VTRQEEELQAKDEELLKVKEKQ 868
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLWFAQRRLE-LLEaeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 869 TKV-----------------------------EGELEEMERKHQQLLEekniLAEQLQAETELFAEA-EEMRARLAAKKQ 918
Cdd:COG4913 319 DALreeldeleaqirgnggdrleqlereierlERELEERERRRARLEA----LLAALGLPLPASAEEfAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 919 ELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLeeqldeeegARQKLQLEKvtAEAKIKKMEEEVLLLEDQNSKFI 998
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASL---------ERRKSNIPA--RLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 999 KEkkLMEDRIAECSSQLAEE-------------EEKAKNLAKI--RNKQEVMISDLEERLKKEEKTRQELEKAK--RKLD 1061
Cdd:COG4913 464 GE--LIEVRPEEERWRGAIErvlggfaltllvpPEHYAAALRWvnRLHLRGRLVYERVRTGLPDPERPRLDPDSlaGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1062 GETTDLQDQI-AELQAQVDELKVQltkKEEELQ---------------GALARGDDETLHK-------NNALKVAReLQA 1118
Cdd:COG4913 542 FKPHPFRAWLeAELGRRFDYVCVD---SPEELRrhpraitragqvkgnGTRHEKDDRRRIRsryvlgfDNRAKLAA-LEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1119 QIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE---DTLDTTAAQQELRTKrEQEVAELKKAlEDETKNHEAQIQ 1195
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAEL-EAELERLDAS-SDDLAALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1196 DMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELacEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgDRLR 1275
Cdd:COG4913 696 ELEAE----LEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELRALLEERFAAALGDAVE-RELR 768
|
570 580
....*....|....*....|....
gi 1907083614 1276 VELAEKANKLQNELDNVSTLLEEA 1299
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1392-1642 |
7.90e-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: 50.53 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1392 EAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKkfdqllaeekgisaryAEER 1471
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----------------ALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1472 DRAEAEAREKETKAlSLARALEEALEAKEEFERQNKQLRADMedLMSSKD--DVGKNVHELEKSKRALEQQVEEMRTQLE 1549
Cdd:COG4942 84 ELAELEKEIAELRA-ELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDflDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1550 ELE---DELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRL--LLKQVRELEAELEDERKQRALAVASKKKMEI 1624
Cdd:COG4942 161 ELAalrAELEAERAELEAL-----------------LAELEEERAALeaLKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*...
gi 1907083614 1625 DLKDLEAQIEAANKARDE 1642
Cdd:COG4942 224 ELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1117-1336 |
7.94e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1117 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQD 1196
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1197 MRQ--RHATALEEL--SEQLEQakrFKANLEKNKQGLETDNKELacevKVLQQVKAESEHKRKKLDAQVQELHAKVSEGD 1272
Cdd:COG3883 95 LYRsgGSVSYLDVLlgSESFSD---FLDRLSALSKIADADADLL----EELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083614 1273 RLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSS 1336
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1615-1782 |
8.66e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1615 AVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQE 1694
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1695 ELASSERARrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELA 1774
Cdd:COG1579 81 QLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*...
gi 1907083614 1775 AERSAAQK 1782
Cdd:COG1579 156 AELEELEA 163
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1400-1656 |
9.29e-06 |
|
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: 50.80 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1400 DVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLD--HQRQIVS--NLEKKQKKFDQllAEEKGISARYAEERDRAE 1475
Cdd:pfam05667 227 NSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTeaTSGASRSaqDLAELLSSFSG--SSTTDTGLTKGSRFTHTE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1476 AEAREKETKALSLARALEEALEAKEEFERQNK--QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELED 1553
Cdd:pfam05667 305 KLQFTNEAPAATSSPPTKVETEEELQQQREEEleELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1554 ELQATEDAKLRL---EVNMQAMKAQFE---RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQralavASKKKMEI-DL 1626
Cdd:pfam05667 385 QYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDE-----SQRKLEEIkEL 459
|
250 260 270
....*....|....*....|....*....|
gi 1907083614 1627 KDLEAQIEAANKARDEVIKQlrkLQAQMKD 1656
Cdd:pfam05667 460 REKIKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1507-1726 |
9.70e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1507 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDEL-------QATEDAKLRLEV------------ 1567
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralYRSGGSVSYLDVllgsesfsdfld 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1568 NMQAMKAQFERDLQTRDEQNEEKKRLllkqvRELEAELEDERKQralAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1647
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAEL-----EAKKAELEAKLAE---LEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1648 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSA 1726
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1206-1855 |
1.13e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1206 EELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSegdRLRVELAEKA--- 1282
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS---AQRVELAERQlqe 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1283 NKLQN-ELDNVSTLLEEAEKKGIKFAKDaaglesqlqdTQELLQEETRQKLNLSSRirqLEEEKNSLQEQQEEEEEARKN 1361
Cdd:COG5022 887 LKIDVkSISSLKLVNLELESEIIELKKS----------LSSDLIENLEFKTELIAR---LKKLLNNIDLEEGPSIEYVKL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1362 LEKQVLALQ-SQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQR 1440
Cdd:COG5022 954 PELNKLHEVeSKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1441 QIVSNLEKKQKKfdQLLAEEKGISAryaeerdrAEAEAREKETKALSLARALEEALEAKEEFER--QNKQLRADMEDLMS 1518
Cdd:COG5022 1034 IISSESTELSIL--KPLQKLKGLLL--------LENNQLQARYKALKLRRENSLLDDKQLYQLEstENLLKTINVKDLEV 1103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1519 SKDDVGKNVHELEK-----SKRALEQQVEEMRTQLeeledeLQATEDAKLRLEVNMQAMKAQFerDLQTRDEQNEEKKRL 1593
Cdd:COG5022 1104 TNRNLVKPANVLQFivaqmIKLNLLQEISKFLSQL------VNTLEPVFQKLSVLQLELDGLF--WEANLEALPSPPPFA 1175
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1594 LLKQVRELEAELEDERKQRALAVASKKKMEIDLkdlEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFA 1673
Cdd:COG5022 1176 ALSEKRLYQSALYDEKSKLSSSEVNDLKNELIA---LFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDT 1252
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1674 QSKESEKKLKSLEAEI---LQLQEELASSERARRHAEQER--DELADEIANSAS-GKSALLDEKRRLEARIAQLEEELEE 1747
Cdd:COG5022 1253 PASMSNEKLLSLLNSIdnlLSSYKLEEEVLPATINSLLQYinVGLFNALRTKASsLRWKSATEVNYNSEELDDWCREFEI 1332
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1748 EQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNarqQLERQNKELKAKLQELEGAVKSKFKATISALEAKigqLE 1827
Cdd:COG5022 1333 SDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLN---PAEIQNLKSRYDPADKENNLPKEILKKIEALLIK---QE 1406
|
650 660
....*....|....*....|....*...
gi 1907083614 1828 EQLEQEAKeraaanklvRRTEKKLKEIF 1855
Cdd:COG5022 1407 LQLSLEGK---------DETEVHLSEIF 1425
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1005-1178 |
1.19e-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: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1005 EDRIAECSSQLAEEEEKAKNLakirnKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQ------- 1077
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQlgsgpda 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1078 ---------VDELKVQLTKKEEELQGALARGDDEtlHknnalKVARELQAQIAELQEDFESE--------KASRNKAEKQ 1140
Cdd:COG3206 256 lpellqspvIQQLRAQLAELEAELAELSARYTPN--H-----PDVIALRAQIAALRAQLQQEaqrilaslEAELEALQAR 328
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907083614 1141 KRDLSEELEALKTELEDTLDTTAAQQELrtKREQEVAE 1178
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRL--EREVEVAR 364
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1393-1659 |
1.23e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1393 AKKKLLKDVealsqrLEEKVLA-YDKLEKTKNR-LQQELDDLTVDLDH-QRQIVS--------------NLEKKQKKFDQ 1455
Cdd:PHA02562 151 ARRKLVEDL------LDISVLSeMDKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1456 LLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRadmedlMSSKDDV----GKNVHELE 1531
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIK------MYEKGGVcptcTQQISEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1532 KSKRALEQQVEEMRTQLEELEDELQatEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRLLLKQVRELEAELEderkq 1611
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIE----- 368
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907083614 1612 ralavaskkKMEIDLKDLEAQIEAANKARDEVIKQLRKLqaQMKDYQR 1659
Cdd:PHA02562 369 ---------ELQAEFVDNAEELAKLQDELDKIVKTKSEL--VKEKYHR 405
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
657-681 |
1.29e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.29e-05
10 20
....*....|....*....|....*
gi 1907083614 657 YKESLTKLMATLRNTNPNFVRCIIP 681
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
842-1342 |
1.36e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 842 KPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKhqqlLEEKNILAEQLQA-----ETELFAEAEEMRARLAAK 916
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE----LDDRNMEVQRLEAllkamKSECQGQMERQMAAIQGK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 917 KQELEEI---LHDLESrvEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEakIKKMEEEVLLLEDQ 993
Cdd:pfam15921 457 NESLEKVsslTAQLES--TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE--ITKLRSRVDLKLQE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 994 NSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKqevmISDLEERLKKEEKTRQELEKAKRKLDGEttdLQDQIAE 1073
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQLEKE---INDRRLE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1074 LQaqvdELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKt 1153
Cdd:pfam15921 606 LQ----EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK- 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1154 eledtldttaaqQELRTKREqevaelkkalEDETKNHEAQIQdmrqrhataLEELSEQLEQAKrfkaNLEKNKQGleTDN 1233
Cdd:pfam15921 681 ------------RNFRNKSE----------EMETTTNKLKMQ---------LKSAQSELEQTR----NTLKSMEG--SDG 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1234 KELACEVKVLQQVKAesehKRKKLDA---QVQELHAKVSEGDRLRVELAEKANKLQNELDNVST----------LLEEAE 1300
Cdd:pfam15921 724 HAMKVAMGMQKQITA----KRGQIDAlqsKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATeknkmageleVLRSQE 799
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1301 KK------GIKFAKDAAGLE-SQLQD-TQELLQEETRQKLNLSSRIRQLE 1342
Cdd:pfam15921 800 RRlkekvaNMEVALDKASLQfAECQDiIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
887-1136 |
1.45e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 887 EEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIqdleeqldeeegar 966
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 967 QKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQevmISDLEERLKKE 1046
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ---AEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1047 EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQED 1126
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 1907083614 1127 FESEKASRNK 1136
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
991-1233 |
1.63e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.93 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 991 EDQNSKFIKEKKLMEdRIAECSSQLAEEEEKAKNLAKIRNKQEVmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1070
Cdd:PRK05771 39 ELSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKKKVSV--KSLEELIKDVEEELEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1071 IAELQAQVDELKVqLTKKEEELQgaLARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNK-------AEKQKRD 1143
Cdd:PRK05771 116 IKELEQEIERLEP-WGNFDLDLS--LLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1144 LSEELEALKTELEDTLDTTAAQQELRTKrEQEVAELKKALEDEtknhEAQIQDMRQRHATALEELSEQLEQAkRFKANLE 1223
Cdd:PRK05771 193 VEEELKKLGFERLELEEEGTPSELIREI-KEELEEIEKERESL----LEELKELAKKYLEELLALYEYLEIE-LERAEAL 266
|
250
....*....|
gi 1907083614 1224 KNkqGLETDN 1233
Cdd:PRK05771 267 SK--FLKTDK 274
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1312-1797 |
1.78e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1312 GLESQLQDTQELLQEE--TRQKLNLSSRIRQL-----EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKK---KVD 1381
Cdd:PRK04863 227 GVRKAFQDMEAALRENrmTLEAIRVTQSDRDLfkhliTESTNYVAADYMRHANERRVHLEEALELRRELYTSRRqlaAEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1382 DDLGTI----ESLEEAKKKLLKDVEALSQRL---EEKVLAYDKLEktknRLQQELDDLTVDLDHQRQIVSNLekkqkkfd 1454
Cdd:PRK04863 307 YRLVEMarelAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIE----RYQADLEELEERLEEQNEVVEEA-------- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1455 qllaeekgisaryAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKsk 1534
Cdd:PRK04863 375 -------------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADN-- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1535 raLEQQVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFERDLQTRDEQNEEKKRLLLKQV-RELeaeLEDERKQRA 1613
Cdd:PRK04863 440 --AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQLVRKIAGEVSRSEAWDVaREL---LRRLREQRH 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1614 LAvASKKKMEIDLKDLE---AQIEAANKARDEVIKQLRKLQAQMKDYQRELEEarasrdeifaqskesekklksLEAEIL 1690
Cdd:PRK04863 511 LA-EQLQQLRMRLSELEqrlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---------------------LEARLE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1691 QLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLND---RFRKTTLQVD 1767
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQlleRERELTVERD 648
|
490 500 510
....*....|....*....|....*....|
gi 1907083614 1768 tlntelaaeRSAAQKsdnarQQLERQNKEL 1797
Cdd:PRK04863 649 ---------ELAARK-----QALDEEIERL 664
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1046-1340 |
1.87e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1046 EEKTRQELEKAKrklDGETTDLQDQIAELQAQVDELkvqltkkeEELQGALARGDDETLHKNNALKVARELQAQIAElqe 1125
Cdd:PRK10929 25 EKQITQELEQAK---AAKTPAQAEIVEALQSALNWL--------EERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1126 dfESEKASRNKAEKQKRDLSEELEALKTELEDtlDTTAAQQElrtkreqevaelkkaledetknheaqiQDMRQRHATAL 1205
Cdd:PRK10929 91 --ERDEPRSVPPNMSTDALEQEILQVSSQLLE--KSRQAQQE---------------------------QDRAREISDSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1206 EELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQvkAESEHKRkkldAQVQELH-AKVS-----EGDRLRVELA 1279
Cdd:PRK10929 140 SQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQ--AESAALK----ALVDELElAQLSannrqELARLRSELA 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 1280 EK-ANKLQNELDNVSTLL--------EEAEKKGIKFAKDAAGLE----SQLQDTQELLQE--ETRQKLNL-SSRIRQ 1340
Cdd:PRK10929 214 KKrSQQLDAYLQALRNQLnsqrqreaERALESTELLAEQSGDLPksivAQFKINRELSQAlnQQAQRMDLiASQQRQ 290
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1019-1428 |
1.92e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1019 EEKAKNLAKIRNKQEVM----ISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQVDELKVQLTKKEEELQG 1094
Cdd:COG4717 52 EKEADELFKPQGRKPELnlkeLKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1095 AlargddetlhknNALKVARELQAQIAELQEDFESEKAsrnkAEKQKRDLSEELEALKTELEdtldttaaqqELRTKREQ 1174
Cdd:COG4717 128 L------------PLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELA----------ELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1175 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKE------------------- 1235
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallal 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1236 --------------------------------------LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVE 1277
Cdd:COG4717 262 lglggsllsliltiagvlflvlgllallflllarekasLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1278 LAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEE----------- 1344
Cdd:COG4717 342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQleellgeleel 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1345 -----KNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDD--DLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDK 1417
Cdd:COG4717 422 lealdEEELEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
490
....*....|.
gi 1907083614 1418 LEKTKNRLQQE 1428
Cdd:COG4717 502 LEEAREEYREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1184-1406 |
2.16e-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: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1184 EDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELacevkvlqqvkaesehkrKKLDAQVQE 1263
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI------------------DKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1264 LHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGI-KFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLE 1342
Cdd:COG3883 77 AEAEI---EERREELGERARALYRSGGSVSYLDVLLGSESFsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083614 1343 EEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQ 1406
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1625-1919 |
2.23e-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: 48.91 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1625 DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR 1704
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1705 HAEQERDELADEIANsasgKSALLdekRRLEARIAQLEEELEeeqsNMELLNDRFRKTTLQVDTLNTELAAER-SAAQKS 1783
Cdd:pfam19220 101 EAEAAKEELRIELRD----KTAQA---EALERQLAAETEQNR----ALEEENKALREEAQAAEKALQRAEGELaTARERL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1784 DNARQQLERQNK----------ELKAKLQELEG----------AVKSKFKATISALEAKIGQLEEQLEQEAKERA----- 1838
Cdd:pfam19220 170 ALLEQENRRLQAlseeqaaelaELTRRLAELETqldatrarlrALEGQLAAEQAERERAEAQLEEAVEAHRAERAslrmk 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1839 --AANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEG 1916
Cdd:pfam19220 250 leALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEM 329
|
...
gi 1907083614 1917 LSR 1919
Cdd:pfam19220 330 LTK 332
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1540-1885 |
2.26e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1540 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL--AVA 1617
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1618 SKKKMEIDLKDLEAQIEAANKARD-----EVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1692
Cdd:TIGR00618 268 RIEELRAQEAVLEETQERINRARKaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1693 QEELASSERARRHAEQErdeladeiansaSGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1772
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVA------------TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1773 LAAERSAAQKSDNARQQLERQNKELKaklqelegavkskfkatisaleakigQLEEQLEQEAKERAAANKLVRRTEKKLK 1852
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAE--------------------------LCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350
....*....|....*....|....*....|...
gi 1907083614 1853 EIFMQVEDERRHADQYKEQMEKANARMKQLKRQ 1885
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1370-1588 |
3.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1370 QSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK 1449
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1450 QKK-------FDQLLAeekgiSARYAEERDRAEAeareketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDD 1522
Cdd:COG3883 95 LYRsggsvsyLDVLLG-----SESFSDFLDRLSA-----------LSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1523 VGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNE 1588
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1047-1217 |
4.39e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1047 EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQ--LTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1124
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1125 EDFES--EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHA 1202
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170
....*....|....*
gi 1907083614 1203 TALEELSEQLEQAKR 1217
Cdd:COG3206 327 AREASLQAQLAQLEA 341
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1599-1713 |
4.63e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1599 RELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEifaqSKES 1678
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR----EIRK 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1907083614 1679 EKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1713
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1017-1288 |
5.23e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1017 EEEEKAKNLAKIRNKQEvmisdlEERLKKEEKTRQEleKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1096
Cdd:PRK05035 442 EQEKKKAEEAKARFEAR------QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGAR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1097 ARGDDETLHKNNALKVARELQAQIAELQEDfESEKAS------RNKAEKQkrdlseELEALKTELEDTLDTTAAQQELRT 1170
Cdd:PRK05035 514 PDNSAVIAAREARKAQARARQAEKQAAAAA-DPKKAAvaaaiaRAKAKKA------AQQAANAEAEEEVDPKKAAVAAAI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1171 KREQEVAELKKALEDETKNHEAQIQDMRQRHATAleelseqLEQAKRFKANLE-KNKQGLETDNKELAcevkvlqqVKAE 1249
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAA-------IARAKAKKAEQQaNAEPEEPVDPRKAA--------VAAA 651
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907083614 1250 SEHKRKKLDAQVQELHAKVSEGDRLRVELAE-----KANKLQNE 1288
Cdd:PRK05035 652 IARAKARKAAQQQANAEPEEAEDPKKAAVAAaiaraKAKKAAQQ 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1309-1489 |
5.61e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1309 DAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVD------- 1381
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1382 ----------------------DDLGTIESLEEAKKKLLKDVEALSQRLEEKvlaydklektKNRLQQELDDLTVDLDHQ 1439
Cdd:COG3883 97 rsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAK----------KAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1440 RQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA 1489
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1313-1682 |
5.78e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1313 LESQLQDTQELLQEETRQKlnlssriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEE 1392
Cdd:pfam07888 36 LEECLQERAELLQAQEAAN-------RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1393 AKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL-----------EKKQKKFDQLLAEEK 1461
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeeaerKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1462 GISARYAEERDRAEaearEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1541
Cdd:pfam07888 189 SLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1542 EEM-RTQLEELEDELQATE------DAKLRLEVNmQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRal 1614
Cdd:pfam07888 265 AQRdRTQAELHQARLQAAQltlqlaDASLALREG-RARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER-- 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1615 avaskKKMEIDLkdleAQIEAANKA-RDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1682
Cdd:pfam07888 342 -----EKLEVEL----GREKDCNRVqLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
965-1180 |
5.86e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 965 ARQKLQlekvTAEAKIKKMEEE--VLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEEr 1042
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1043 LKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQVDELKVQLTKKEEELQGALargddetlhkNNALKVARELQAQ 1119
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEAQRILASL----------EAELEALQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1120 IAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEVAELK 1180
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1114-1263 |
6.06e-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: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1114 RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldtTAAQQELRTKREQEvaelkkALEDETKNHEAQ 1193
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRNNKEYE------ALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1194 IQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQE 1263
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1128-1343 |
6.54e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1128 ESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAElkkALEDETKNHEAQIQDMRQRhataLEE 1207
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEFRQKNGLV---DLSEEAKLLLQQLSELESQ----LAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1208 LSEQLEQAKRFKANLEKNKQGLETDNKELAcEVKVLQQVKAEsehkRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQN 1287
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELL-QSPVIQQLRAQ----LAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1288 ELDnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1343
Cdd:COG3206 306 QLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1273-1478 |
6.83e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1273 RLRVELAEKANK-LQNELDNVSTLLEEAEKKGIKFAKdaaglESQLQDTQELLQEETRQKLNLSSRIRQLEEEknslqeq 1351
Cdd:COG3206 167 ELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAE------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1352 qeeeeeaRKNLEKQVLALQSQLADTKKKVDDDLG--TIESLEEAKKKLLKDVEALSQRLEEK----VLAYDKLEKTKNRL 1425
Cdd:COG3206 235 -------LAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQL 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1426 QQELDDLTVDLDHQRQI----VSNLEKKQKKFDQLLAEEKGISARYAE-ERDRAEAEA 1478
Cdd:COG3206 308 QQEAQRILASLEAELEAlqarEASLQAQLAQLEARLAELPELEAELRRlEREVEVARE 365
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1001-1341 |
7.83e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.54 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1001 KKLMEDRIAECSSQLAEEEE--------KAKN--------LAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGET 1064
Cdd:pfam06160 55 DDIVTKSLPDIEELLFEAEElndkyrfkKAKKaldeieelLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1065 TDLQDQ-------IAELQAQVDELKVQLTKKEEELQGalarGDDETlhknnALKVARELQAQIAELQEDFESEKASRNKA 1137
Cdd:pfam06160 135 KTLLANrfsygpaIDELEKQLAEIEEEFSQFEELTES----GDYLE-----AREVLEKLEEETDALEELMEDIPPLYEEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1138 EKQKRDLSEELEALKTELED---TLDTTAAQQELRTKREQeVAELKKALED-ETKNHEAQIQDMRQRhataLEELSEQLE 1213
Cdd:pfam06160 206 KTELPDQLEELKEGYREMEEegyALEHLNVDKEIQQLEEQ-LEENLALLENlELDEAEEALEEIEER----IDQLYDLLE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1214 QAKRFKANLEKNKQGLETD-------NKELACEVKVLQQ---VKAESEHKRKKLDAQVQELHAKVsegDRLRVELAEKA- 1282
Cdd:pfam06160 281 KEVDAKKYVEKNLPEIEDYlehaeeqNKELKEELERVQQsytLNENELERVRGLEKQLEELEKRY---DEIVERLEEKEv 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1283 --NKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL 1341
Cdd:pfam06160 358 aySELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1050-1214 |
7.91e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1050 RQEL---EKAKRKLDGETTDLQDQIA-------ELQAQVDELKVQLTKKEEE---LQGALARGDDEtlhknnalkvAREL 1116
Cdd:PRK09039 45 SREIsgkDSALDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGA----------GAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1117 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELedtldttaaqqelrtkreQEVAELKKALEDETKNHEAQIQD 1196
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL------------------AALEAALDASEKRDRESQAKIAD 176
|
170
....*....|....*...
gi 1907083614 1197 MRQRHATALEELSEQLEQ 1214
Cdd:PRK09039 177 LGRRLNVALAQRVQELNR 194
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1625-1856 |
9.43e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1625 DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskeSEKKLKSLE-AEILQLQEELASSERAR 1703
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL------EAAALQPGEeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1704 RHAEQERDELADEIANSASgksaLLDE-KRRLEaRIAQleeeleeEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQk 1782
Cdd:COG0497 226 EALQEALEALSGGEGGALD----LLGQaLRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLE- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1783 SDNAR-QQLE-RQN--------------------KELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKE---- 1836
Cdd:COG0497 293 FDPERlEEVEeRLAllrrlarkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaa 367
|
250 260
....*....|....*....|.
gi 1907083614 1837 -RAAANKLVRRTEKKLKEIFM 1856
Cdd:COG0497 368 rKKAAKKLEKAVTAELADLGM 388
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
849-1197 |
9.48e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 849 RQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLleEKNILAEQlqaetelfaeaeemRARLAAKkQELEEILHDLE 928
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNA--EKNILLLN--------------QARLQAL-EDLEKILTEKE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 929 SrveeeeernqiLQNEKKKMQAHIQDLEEQLdeeegarqklqleKVTAEAKIKkmeeeVLLLEDQNSKFIKEKKLMEDRI 1008
Cdd:PLN02939 167 A-----------LQGKINILEMRLSETDARI-------------KLAAQEKIH-----VEILEEQLEKLRNELLIRGATE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1009 AECSSQLAEEEE--KAKNLAkIRNKQEVM------ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIaelqAQVDE 1080
Cdd:PLN02939 218 GLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVAETEERVFKLEKERSLLDASLRELESKFIVAQEDV----SKLSP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1081 LKVQ-LTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRdLSEELEALKTELEDTL 1159
Cdd:PLN02939 293 LQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASD 371
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907083614 1160 DTTAAQQELRTKREQEVAELKKALEDETKNH--EAQIQDM 1197
Cdd:PLN02939 372 HEIHSYIQLYQESIKEFQDTLSKLKEESKKRslEHPADDM 411
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1248-1425 |
1.01e-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: 46.07 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1248 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKgIKFAKDAAGLESQLQDTQELLQEE 1327
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1328 TRQKLnlssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDlgtIESLEEAKKKLLKDVEALSQR 1407
Cdd:COG1579 99 ESLKR----RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELAAK 171
|
170
....*....|....*....
gi 1907083614 1408 LEEKVLA-YDKLEKTKNRL 1425
Cdd:COG1579 172 IPPELLAlYERIRKRKNGL 190
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1529-1930 |
1.04e-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: 47.66 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDE 1608
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREA--------LQQTQQSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1609 RKQraLAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL--- 1685
Cdd:TIGR00618 273 RAQ--EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtl 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1686 ------------EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE-----------KRRLEARIAQLE 1742
Cdd:TIGR00618 351 hsqeihirdaheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQReqatidtrtsaFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1743 EELEEEQSNMELLnDRFRKTTLQVDTLntELAAERSAAQKSDNARQQLerQNKELKAKLQELEGAVKSKFKATISALEAK 1822
Cdd:TIGR00618 431 KQQELQQRYAELC-AAAITCTAQCEKL--EKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1823 IGQLEEQLEQEAKERAAANKLVRRT----------EKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQleeaeee 1892
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC------- 578
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907083614 1893 ATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1243-1370 |
1.08e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1243 LQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAglESQLQDTQE 1322
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA--DEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907083614 1323 LLQEETRqklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1370
Cdd:PRK00409 596 LQKGGYA-----SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
842-1245 |
1.10e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 842 KPLLQVTRQEEELQAKD--EELLKVKEKQTKVEGELEEMERKhqqlleekniLAEQLQAETELFAEAEEMRARLAAKKQE 919
Cdd:pfam07888 1 KPLDELVTLEEESHGEEggTDMLLVVPRAELLQNRLEECLQE----------RAELLQAQEAANRQREKEKERYKRDREQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 920 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK 999
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1000 EKKLMEDRIAECSSQLAEEEEKAKNLakirnkqEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVD 1079
Cdd:pfam07888 151 ELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1080 ELKvqltKKEEELQGALA--RGDDETLH--KNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALK--- 1152
Cdd:pfam07888 224 TAH----RKEAENEALLEelRSLQERLNasERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALRegr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1153 ----TELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL---EKN 1225
Cdd:pfam07888 300 arwaQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKE 379
|
410 420
....*....|....*....|
gi 1907083614 1226 KQGLETDNKELACEVKVLQQ 1245
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQLEQ 399
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1081-1286 |
1.15e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1081 LKVQLTKKEEELQgalargddetlhknnalkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEEL---EALKTELED 1157
Cdd:PRK09039 44 LSREISGKDSALD---------------------RLNSQIAELADLLSLERQGNQDLQDSVANLRASLsaaEAERSRLQA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1158 TLDTTAAQqelRTKREQEVAELKKALEDEtknheaqiQDMRQRHATALEELSEQLEQAKRfkanleknkqgletdnkELA 1237
Cdd:PRK09039 103 LLAELAGA---GAAAEGRAGELAQELDSE--------KQVSARALAQVELLNQQIAALRR-----------------QLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907083614 1238 cevkVLQQVKAESEHKRKKLDAQVQELhakvseGDRLRVELAEKANKLQ 1286
Cdd:PRK09039 155 ----ALEAALDASEKRDRESQAKIADL------GRRLNVALAQRVQELN 193
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
970-1463 |
1.29e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 970 QLEKVTAEA-------KIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSS-QLAEEEEKAKNLAKIRNKQEVMISDLEE 1041
Cdd:TIGR01612 1154 DLEDVADKAisnddpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKdKTSLEEVKGINLSYGKNLGKLFLEKIDE 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1042 RLKKEEKTRQELEKAKRKLDgettDLQDQIAELQaqvDELKVQLTKKEEELQGALARGDDETLH---KNNALKVArELQA 1118
Cdd:TIGR01612 1234 EKKKSEHMIKAMEAYIEDLD----EIKEKSPEIE---NEMGIEMDIKAEMETFNISHDDDKDHHiisKKHDENIS-DIRE 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1119 QIAELQEDFeSEKASRN-----------KAEKQKRDLSEELEALkTELEDTLDTTAAQQELRTKRE--QEVAELKKALED 1185
Cdd:TIGR01612 1306 KSLKIIEDF-SEESDINdikkelqknllDAQKHNSDINLYLNEI-ANIYNILKLNKIKKIIDEVKEytKEIEENNKNIKD 1383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1186 ETKNHEAQIQDMRQRhaTALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKL-------D 1258
Cdd:TIGR01612 1384 ELDKSEKLIKKIKDD--INLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLllfknieM 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1259 AQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQE----ETRQKLNL 1334
Cdd:TIGR01612 1462 ADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKysalAIKNKFAK 1541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1335 SSR-----IRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK---------D 1400
Cdd:TIGR01612 1542 TKKdseiiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKisdikkkinD 1621
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 1401 VEALSQRLEEKV--LAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGI 1463
Cdd:TIGR01612 1622 CLKETESIEKKIssFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKI 1686
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1059-1485 |
1.29e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.14 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1059 KLDGETTDLQDQIAELQAQVDelkvqlTKKEEELQGALARGDDETLHKNNALKVarelqaqiaelQEDFESEKASRNKAE 1138
Cdd:NF012221 1355 EIDEVGSDLGDSLTGSVTQVE------TPDLNAMQNALNIDESVLSTQAPNLIV-----------NGDFEQGAEGWNSTY 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1139 KQKRDLS--------EELEALKTELeDTLDTTAAQQELRTKREQEVAELK----KALEDETKNHEAQIQDMRQRHATALE 1206
Cdd:NF012221 1418 GVEASHSasvyglraEGHGARVSEL-DTYTNTSLYQDLSNLTAGEVIALSfdfaRRAGLSTNNGIEVLWNGEVVFASSGD 1496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1207 ELSEQLEQAK----------RFKANLEKNKQGLETDNKELACEVKvlQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRV 1276
Cdd:NF012221 1497 ASAWQQKTLKltakagsnrlEFKGTGHNDGLGYILDNVVATSESS--QQADAVSKHAKQDDAAQNALADKERAEADRQRL 1574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1277 ElAEKanklQNELDNVSTLLEEAEkkgikfAKDAAGLESQLQDTQELLQEETRQ-KLNLSSRIRQLEEEKNSLQEQQEEE 1355
Cdd:NF012221 1575 E-QEK----QQQLAAISGSQSQLE------STDQNALETNGQAQRDAILEESRAvTKELTTLAQGLDALDSQATYAGESG 1643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1356 EEARKNLEKQVLA-LQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVlaydklEKTKNRLQQELDDLTV 1434
Cdd:NF012221 1644 DQWRNPFAGGLLDrVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG------EQNQANAEQDIDDAKA 1717
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1435 DLDHQRQivsnlEKKQKKFDQLLAEEKGiSARYAEERDRAEAEAREKETKA 1485
Cdd:NF012221 1718 DAEKRKD-----DALAKQNEAQQAESDA-NAAANDAQSRGEQDASAAENKA 1762
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
845-1059 |
1.32e-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: 47.04 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 845 LQVTRQEEelqaKDEELLKVKEKQTKVEGE-LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 923
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEISrMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 924 LHDLESrveEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIkEKKL 1003
Cdd:pfam17380 426 RAEQEE---ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL-EKEL 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1004 MEDRIAecssqLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRK 1059
Cdd:pfam17380 502 EERKQA-----MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1586-1906 |
1.58e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1586 QNEEKKRLLLKQVRELEAELEDERKQRALA----VASKKKMEI---DLKDLEAQIEAA----NKARDEVI--KQLRKLQA 1652
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEqyrlVEMARELAElneAESDLEQDYQAAsdhlNLVQTALRqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1653 QMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERA----------RRHAEQERDE---LADEIAN 1719
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALERakqLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1720 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRkttlQVDTLNTELAAERSAAQKSDNARQqLERQNKELKA 1799
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSRSEAWDVARE-LLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1800 KLQELEgavkskfkatisALEAKIGQLEEQLEQEAkeraAANKLVRRTEKKLKeifMQVEDErrhaDQYKEQMEKANARM 1879
Cdd:PRK04863 511 LAEQLQ------------QLRMRLSELEQRLRQQQ----RAERLLAEFCKRLG---KNLDDE----DELEQLQEELEARL 567
|
330 340
....*....|....*....|....*..
gi 1907083614 1880 KQLKRQLEEAEEEATRANASRRKLQRE 1906
Cdd:PRK04863 568 ESLSESVSEARERRMALRQQLEQLQAR 594
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1533-1688 |
1.63e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.90 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1533 SKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQV---RELEAEL---- 1605
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERsarREAEAELerlq 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1606 -------EDERKQRALAVASKKKMEIDLKDLEAQIEA---ANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1675
Cdd:pfam09787 121 eelryleEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQL 200
|
170
....*....|...
gi 1907083614 1676 KESEKKLKSLEAE 1688
Cdd:pfam09787 201 ERMEQQIKELQGE 213
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1507-1842 |
1.68e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1507 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMR---TQLEELEDELQATEDAKLRLEVNMQAMKAQ------FE 1577
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSitlKEIERLSIEYNNAMDDYNNLKSALNELSSLedmknrYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1578 RDLQTRDE--QNEEKKRLLLKQVRELEAELEDE----RKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQ 1651
Cdd:PRK01156 256 SEIKTAESdlSMELEKNNYYKELEERHMKIINDpvykNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1652 AQMKDY---QRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALL 1728
Cdd:PRK01156 336 KDYNDYikkKSRYDDLNNQILEL----EGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1729 DEKRR-----------LEARIAQLEEELEEEQSNMELLNDRFR-----------KTTLQVDTLNTELAAERSAAQKSDNA 1786
Cdd:PRK01156 412 NEINVklqdisskvssLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIE 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1787 RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1842
Cdd:PRK01156 492 VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDK 547
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1632-1912 |
1.82e-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: 46.66 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1632 QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASR----DEIFAQSKESEKKLKSLEAEILQLQEElassERARRHAE 1707
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1708 QERDELADEIANSASGKSALLDEKRRLEaRIAQLEEELEEEQSNMEllnDRFRKTTLQVDTLNtELAAERSAAQKSDNAR 1787
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1788 QQLERQNKELKAKLQELEgavKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRT-EKKLKEIFMQ-VEDERRHA 1865
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907083614 1866 DQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1912
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1020-1155 |
1.94e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1020 EKAK-NLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLtkkEEELQGALar 1098
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAI-- 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 1099 gddetlhkNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRdLSEELEALKTEL 1155
Cdd:PRK00409 580 --------KEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKKEKKK 627
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1018-1487 |
2.09e-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: 46.28 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1018 EEEKAKNLAKIRNKQEVMISDL----EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQ 1093
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1094 GALARgdDETLHKNNALKVARELQAQIAE------------LQEDFESEKAS------RNKAEKQKRDLSEELEALKTEL 1155
Cdd:pfam07111 215 AQVTL--VESLRKYVGEQVPPEVHSQTWElerqelldtmqhLQEDRADLQATvellqvRVQSLTHMLALQEEELTRKIQP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1156 EDTLD---TTAAQQELRTKREQeVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETD 1232
Cdd:pfam07111 293 SDSLEpefPKKCRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1233 N---KELACEVKVLQQVKAESEHKRKKLDAQVQ-----------ELHAKVSEGDRLRVELAEKANKLQNELDNVSTL--- 1295
Cdd:pfam07111 372 RmsaKGLQMELSRAQEARRRQQQQTASAEEQLKfvvnamsstqiWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIkgl 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1296 ------LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQ---KLNLSSRIRQLE--EEKNSLQEQQEEEEEARKNLEK 1364
Cdd:pfam07111 452 markvaLAQLRQESCPPPPPAPPVDADLSLELEQLREERNRldaELQLSAHLIQQEvgRAREQGEAERQQLSEVAQQLEQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1365 QVLALQSQLADTKKKVDDDL-GTIESLEEA---KKKLLKDVEALSQRLEEKVlaydklEKTKNRLQQELDDLTVDLDHQR 1440
Cdd:pfam07111 532 ELQRAQESLASVGQQLEVARqGQQESTEEAaslRQELTQQQEIYGQALQEKV------AEVETRLREQLSDTKRRLNEAR 605
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1907083614 1441 QIVSNLEKKQKKFDQLLAEEKgisaRYAEERDRAEAEAREKETKALS 1487
Cdd:pfam07111 606 REQAKAVVSLRQIQHRATQEK----ERNQELRRLQDEARKEEGQRLA 648
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1257-1615 |
2.12e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.83 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1257 LDAQVQEL---HAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQELLQEETRQKLN 1333
Cdd:pfam19220 36 IEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1334 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVL 1413
Cdd:pfam19220 109 LRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1414 AYDKLEKTKNRLQQELDDltvdldhQRQIVSNLEKKqkkfdqlLAEEKgisaryaEERDRAEAEAREK----ETKALSLA 1489
Cdd:pfam19220 189 ELAELTRRLAELETQLDA-------TRARLRALEGQ-------LAAEQ-------AERERAEAQLEEAveahRAERASLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1490 RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE--V 1567
Cdd:pfam19220 248 MKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEerA 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1568 NM-----QAMKAQFER------DLQTRDEQNE---EKKRLLLKQ-VRELEAELEDERKQRALA 1615
Cdd:pfam19220 328 EMltkalAAKDAALERaeeriaSLSDRIAELTkrfEVERAALEQaNRRLKEELQRERAERALA 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
892-1212 |
2.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 892 LAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE-------SRVEEEEERNQILQNEKKKMQAhiqdleeqlDEEEG 964
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswDEIDVASAEREIAELEAELERL---------DASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 965 ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAknlakirnkQEVMISDLEERLK 1044
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA---------RLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1045 KEEKTRQELEKAKRkldgettdLQDQIAELQAQVDELKVQLTKKEEELQ----GALARGDDETLHKNNALKVARELQAQ- 1119
Cdd:COG4913 757 AALGDAVERELREN--------LEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLALLDRLEEDg 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1120 IAELQEDFESEKASRN---------KAEKQKRDLSEELEALKTELEDTL--DTTAAQQELRTKREQEVAELKKALEDETK 1188
Cdd:COG4913 829 LPEYEERFKELLNENSiefvadllsKLRRAIREIKERIDPLNDSLKRIPfgPGRYLRLEARPRPDPEVREFRQELRAVTS 908
|
330 340
....*....|....*....|....
gi 1907083614 1189 NHEAQIQDMRQRHATALEELSEQL 1212
Cdd:COG4913 909 GASLFDEELSEARFAALKRLIERL 932
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1506-1638 |
2.26e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 46.21 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1506 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDE 1585
Cdd:pfam05911 683 NKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYE-DLETRLT 761
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1586 QNEEKKRLLLKQVRELEAELEDERKqralavaSKKKMEIDLKDLEAQIEAANK 1638
Cdd:pfam05911 762 ELEAELNELRQKFEALEVELEEEKN-------CHEELEAKCLELQEQLERNEK 807
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1360-1884 |
2.33e-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: 46.28 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1360 KNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdldHQ 1439
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRL-----HQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1440 RQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSS 1519
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQ-------LAEAQKEAELLRKQLSKTQEELEAQVTLVESL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1520 KDDVGKNV--------------------HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD 1579
Cdd:pfam07111 224 RKYVGEQVppevhsqtwelerqelldtmQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1580 LQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVAS--------------------KKKMEIDL-----KDLEAQIE 1634
Cdd:pfam07111 304 CRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAElqeqvtsqsqeqailqralqDKAAEVEVermsaKGLQMELS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1635 AANKAR-------DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL----------KSLEAEILQLQEELA 1697
Cdd:pfam07111 384 RAQEARrrqqqqtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQ 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1698 SSERARRHAEQERDELADEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNME---------LLNDRFRKTTLQVDT 1768
Cdd:pfam07111 464 ESCPPPPPAPPVDADLSLELEQLREERNRL-DAELQLSAHLIQQEVGRAREQGEAErqqlsevaqQLEQELQRAQESLAS 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1769 LNTELAAERSAAQKSD----NARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKigqLEEQLEQEAKERAAANKLV 1844
Cdd:pfam07111 543 VGQQLEVARQGQQESTeeaaSLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRR---LNEARREQAKAVVSLRQIQ 619
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1907083614 1845 RRT--EKKLKEIFMQVEDERRhadqyKEQMEKANARMKQLKR 1884
Cdd:pfam07111 620 HRAtqEKERNQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
901-1475 |
2.45e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 901 ELFAEAEEMRaRLAAKKQELEEILHDLESRVEEEEErnqiLQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKI 980
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 981 KKMEEEVLLLED---QNSKFIKEKKLMEDRIAECSSQLAEEEEKAknlakirnkqeVMISDLEERLKKEEKTRQeleKAK 1057
Cdd:PRK01156 228 NNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKN-----------NYYKELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1058 RKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGA--LARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1135
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLsvLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1136 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataLEELSEQL--- 1212
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNMeml 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1213 ---------------EQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDA-QVQELHAKVSEGDRLRV 1276
Cdd:PRK01156 450 ngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1277 ELAEKANKLqNELDNVSTLLEEA--EKKGIKFakdaaglesqlqdtqELLQEETRQKLNLSSRIRQLEEEknSLQEQQEE 1354
Cdd:PRK01156 530 DLEDIKIKI-NELKDKHDKYEEIknRYKSLKL---------------EDLDSKRTSWLNALAVISLIDIE--TNRSRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1355 EEEARKNLEKQVLALQSQLADTKKKVDDDLGTIE---SLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDD 1431
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEneaNNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE 671
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907083614 1432 LTVDLDhqrQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1475
Cdd:PRK01156 672 ITSRIN---DIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1569-1963 |
2.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1569 MQAMKAQFERDLQTRDEQ----NEEKKRLLLKQVRELEAELEDERKQralaVASKKKMEIDLKDLEAQIEAANKARDEVI 1644
Cdd:COG4717 40 LAFIRAMLLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1645 KQLRKLQaQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGK 1724
Cdd:COG4717 116 EELEKLE-KLLQLLPLYQELEALEAEL----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1725 SA----LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE-----------LAAERSAAQKSDNARQQ 1789
Cdd:COG4717 191 EEelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearllllIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1790 LERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYK 1869
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1870 EQMEKANARMKQLKRQLEEAEEEA--TRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR-GGPISFSSSRSGRRQL 1946
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEElLGELEELLEALDEEEL 430
|
410
....*....|....*..
gi 1907083614 1947 HIEGASLELSDDDTESK 1963
Cdd:COG4717 431 EEELEELEEELEELEEE 447
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1772-1884 |
2.60e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1772 ELAAERSAAQKSDNARQ--QLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEK 1849
Cdd:COG2433 398 EREKEHEERELTEEEEEirRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|....*
gi 1907083614 1850 KLKEIfmqvEDERRHADQYKEQMEkanaRMKQLKR 1884
Cdd:COG2433 477 LEREL----EEERERIEELKRKLE----RLKELWK 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1645-1930 |
2.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1645 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAE---QERDELADEIANSA 1721
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1722 SGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqvdtlntelAAERSAAQKSDNARQQLERQNKELKAKL 1801
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1802 QELEgavkskfkATISALEAKIGQLEEQLeqeaKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANaRMKQ 1881
Cdd:PRK03918 310 REIE--------KRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELER 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907083614 1882 LKRQLeeaeeeatrANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1930
Cdd:PRK03918 377 LKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
844-1266 |
2.84e-04 |
|
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: 46.19 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 844 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEME---RKHQQLLEEKNI---LAEQLQAET----ELFAEAEEMRARL 913
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKndiEEQETLLGTIMPeeeSAKVCLTDVtimeRFQMELKDVERKI 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 914 AAKKQELEEIlhDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQL---EKVTAEAKIKKMEEEVLLL 990
Cdd:TIGR00606 809 AQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQF 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 991 EDQNSKFIKEkklMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1070
Cdd:TIGR00606 887 EEQLVELSTE---VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1071 IAELQAQvdelkvQLTKKEEELQGALARGDDETLHKNnalkvarelqaqiaELQEDFESEKASRNKAEKQKRDLSEELEA 1150
Cdd:TIGR00606 964 IQDGKDD------YLKQKETELNTVNAQLEECEKHQE--------------KINEDMRLMRQDIDTQKIQERWLQDNLTL 1023
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1151 LKTELEDTLDTTAAQQELRTKREQEVAELKKaledETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL-EKNKQGL 1229
Cdd:TIGR00606 1024 RKRENELKEVEEELKQHLKEMGQMQVLQMKQ----EHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELrEPQFRDA 1099
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907083614 1230 ETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1266
Cdd:TIGR00606 1100 EEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHS 1136
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1626-1884 |
3.06e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1626 LKDLEAQIEAANKARDEVIKQLRKLQAQMKdyQRELEEARASRdeifaQSKESEKKLKSLEAEILQLQEELASSERarRH 1705
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLK--KQEEAISQASR-----KLRETQNTLNQLNKQIDELNASIAKLEQ--QQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1706 AEQERDeLADEIANS-----ASGKSALL--DEKRRLEaRIaqleeeleeeQSNMELLNDRFRKTTLQVDTLNTELAAERS 1778
Cdd:PRK11637 120 AAQERL-LAAQLDAAfrqgeHTGLQLILsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTREELAAQKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1779 AAQKSDNARQQLERQNKELKAKLQELEGAVKSkfkaTISALEAKIGQLEEQLEQeakeraaanklVRRTEKKLKEIFMQV 1858
Cdd:PRK11637 188 ELEEKQSQQKTLLYEQQAQQQKLEQARNERKK----TLTGLESSLQKDQQQLSE-----------LRANESRLRDSIARA 252
|
250 260
....*....|....*....|....*..
gi 1907083614 1859 EDE-RRHADQYKEQMEKANARMKQLKR 1884
Cdd:PRK11637 253 EREaKARAEREAREAARVRDKQKQAKR 279
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
851-1135 |
3.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 851 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETElfaEAEEMRARLAAKKQELEEilhdlesr 930
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEE-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 931 veeeeeRNQILQNEKKKMQahiqdleeqldeeegaRQKLQLEKVtaeakikkmeeEVLLLEDQNSKFIKEKKLMeDRIAE 1010
Cdd:COG3883 84 ------RREELGERARALY----------------RSGGSVSYL-----------DVLLGSESFSDFLDRLSAL-SKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1011 CSSQLAEEEEKAKnlAKIRNKQevmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEE 1090
Cdd:COG3883 130 ADADLLEELKADK--AELEAKK----AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907083614 1091 ELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1135
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1071-1348 |
3.35e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.62 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1071 IAELQAQVDELKVQLTKKEEELQGALARGDDETLHKnnalkVARELQAQIAE------LQEDFESEKASRNKAEKQK--- 1141
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK-----LKKEIDLEYTEaviamgLQERLENLREEFSKANSQDqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1142 -RDLSEELEALKTELEDTLDTTAAQQELRTKRE--QEVAELKKALEDETKNHEAQiQDMRQRHATALE--ELSEQLEQAK 1216
Cdd:PLN03229 506 hPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKKFKEVMDrpEIKEKMEALK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1217 RFKANLEKNKQG-LETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELD----- 1290
Cdd:PLN03229 585 AEVASSGASSGDeLDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINkkier 664
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1291 --NVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1348
Cdd:PLN03229 665 viRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEEL 724
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1529-1649 |
3.50e-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: 44.15 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD---------------LQTRDEQNEEKKRL 1593
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnnkeyeaLQKEIESLKRRISD 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1594 LLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRK 1649
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1640-1805 |
3.65e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1640 RDEVIKQLRKLQAQMKDyQRELEEARASrdeifaqskesekklkSLEAEILQLQEELASSERARRHAEQERDELADEiAN 1719
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGA-GA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1720 SASGKSALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttlQVDTLNTELAAERSAAQKSDNARQQLERQ------ 1793
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKiadlgr 179
|
170
....*....|....
gi 1907083614 1794 --NKELKAKLQELE 1805
Cdd:PRK09039 180 rlNVALAQRVQELN 193
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
874-1472 |
4.54e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.43 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 874 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeilhdLESRVEEEEERNQILQNEKKKmqahiq 953
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA-----IKNKFAKTKKDSEIIIKEIKD------ 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 954 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED--------------------RIAECss 1013
Cdd:TIGR01612 1556 -----------AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflkisdikkKINDC-- 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1014 qLAEEEEKAKNLAKIR-NKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQVDELKVQLTKKEEEL 1092
Cdd:TIGR01612 1623 -LKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1093 QGALARGDDETLHKNNalkvaRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKR 1172
Cdd:TIGR01612 1698 EIGIIEKIKEIAIANK-----EEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGC 1772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1173 EQEVAElkkalEDETKNheaQIQDMRqrhATALEELSEQLEQAKRFKANLeknkqgletDNKELACEVKVLQQVKAESEH 1252
Cdd:TIGR01612 1773 LETVSK-----EPITYD---EIKNTR---INAQNEFLKIIEIEKKSKSYL---------DDIEAKEFDRIINHFKKKLDH 1832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1253 KRKKLDAQvqelHAKVSEG-DRL-----RVELAEKANKLQNELDNVSTLL------------EEAEKKGIKFAKDAAGLE 1314
Cdd:TIGR01612 1833 VNDKFTKE----YSKINEGfDDIsksieNVKNSTDENLLFDILNKTKDAYagiigkkyysykDEAEKIFINISKLANSIN 1908
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1315 SQLQDTQEL-------------LQEETRQKL-------NLSSRIRQLEEEKNSLQEQQEEEEEARKNlEKQVLAL---QS 1371
Cdd:TIGR01612 1909 IQIQNNSGIdlfdniniailssLDSEKEDTLkfipspeKEPEIYTKIRDSYDTLLDIFKKSQDLHKK-EQDTLNIifeNQ 1987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1372 QLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEE---------------KVLAYDKLEKTKNRLQQELDDLTVDL 1436
Cdd:TIGR01612 1988 QLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDElnklscdsqnydtilELSKQDKIKEKIDNYEKEKEKFGIDF 2067
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907083614 1437 DHQ--RQIVSNLEKKQKKFDQLLAEEKGISARYAEERD 1472
Cdd:TIGR01612 2068 DVKamEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
843-1216 |
4.91e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 843 PLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNI-LAEQLQAETElfaeaEEMRArLAAKKQELE 921
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPE-----AELRQ-LNRRRVELE 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 922 EILHDLESrvEEEEERNQILQnekkkmqahiqdleeqldeeegARQKLQLekvtaeakIKKMEEEVLLLEDQNskfikek 1001
Cdd:PRK04863 851 RALADHES--QEQQQRSQLEQ----------------------AKEGLSA--------LNRLLPRLNLLADET------- 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1002 klMEDRIAECSSQLAEEEEKA-------KNLAKIRNKQEVMISDLE--ERLKKE-EKTRQELEKAKRKLDGETTDLQ--- 1068
Cdd:PRK04863 892 --LADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDPEqfEQLKQDyQQAQQTQRDAKQQAFALTEVVQrra 969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1069 ----DQIAELQAQVDELKVQLTKKEEELQGALARGDDEtlhknnalkvARELQAQIAELQEDFESEKASRNKAEKQKRDL 1144
Cdd:PRK04863 970 hfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ----------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1145 SEELEALKTELEDTLDTTAA------QQELRTKREQEvAELKKALEDETKNHEAQiqdmrQRHATALEE----LSEQLEQ 1214
Cdd:PRK04863 1040 KQELQDLGVPADSGAEERARarrdelHARLSANRSRR-NQLEKQLTFCEAEMDNL-----TKKLRKLERdyheMREQVVN 1113
|
..
gi 1907083614 1215 AK 1216
Cdd:PRK04863 1114 AK 1115
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1583-1853 |
4.98e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1583 RDEQNEEKKRLLLKQVRELEAELEDERKQRA-LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1661
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLrKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1662 EEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQL 1741
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1742 EEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEA 1821
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270
....*....|....*....|....*....|..
gi 1907083614 1822 KIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1853
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1529-1697 |
5.14e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.66 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQ-----NEEKKRLLLKQVRELEA 1603
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-KWEEKARLalekgREDLAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1604 ELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQ---------------------MKDYQRELE 1662
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQekvnealsgidsddatsalerMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1907083614 1663 EARASRDEIfAQSKESEKKLKSLEAEIlQLQEELA 1697
Cdd:COG1842 179 ARAEAAAEL-AAGDSLDDELAELEADS-EVEDELA 211
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1534-1688 |
5.25e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1534 KRALEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFERDLQTRDEQNEEKKRLLLKQVRELEAELED 1607
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1608 ERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRE--LEEARA-SRDEIFAQSKESEKKLKs 1684
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKEIEEEAK- 183
|
....
gi 1907083614 1685 LEAE 1688
Cdd:PRK12704 184 EEAD 187
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1415-1857 |
5.33e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1415 YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLaeEKGISARYAEERDRAEAEAREKETKALsLARALEE 1494
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1495 ALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1574
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1575 QFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQM 1654
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1655 KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1734
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1735 EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA 1814
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907083614 1815 TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQ 1857
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1529-1928 |
5.62e-04 |
|
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: 45.01 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDE 1608
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQ-IKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1609 RKQralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQSKESEKKLKSLEAE 1688
Cdd:TIGR04523 116 KEQ-------KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK-------ELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1689 ILQLQEELASSERARRHAEQerdeladeianSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDT 1768
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLEL-----------LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1769 LNTELaaersaaqksDNARQQLERQNKELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKERAAAnklvrrTE 1848
Cdd:TIGR04523 251 TQTQL----------NQLKDEQNKIKKQLSEKQKELEQN-----NKKIKELEKQLNQLKSEISDLNNQKEQD------WN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1849 KKLKEIFMQVEDERRhadQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:TIGR04523 310 KELKSELKNQEKKLE---EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
975-1302 |
6.30e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 975 TAEAKIKKMEEEVLLL---EDQNSKFIKE---------KKLMEDR------IAECSSQLAEEEE---KAKNLAKIRNKQE 1033
Cdd:PRK04778 116 LIEEDIEQILEELQELlesEEKNREEVEQlkdlyrelrKSLLANRfsfgpaLDELEKQLENLEEefsQFVELTESGDYVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1034 --VMISDLEERLKKEEKTRQELEKAKRKLDgetTDLQDQIAELQAQVDELKVQ------------LTKKEEELQGALArg 1099
Cdd:PRK04778 196 arEILDQLEEELAALEQIMEEIPELLKELQ---TELPDQLQELKAGYRELVEEgyhldhldiekeIQDLKEQIDENLA-- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1100 DDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE---LRTKREQEV 1176
Cdd:PRK04778 271 LLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsytLNESELESV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1177 AELKKALEDETKNHEAQIQDMRQRHATA------LEELSEQLEQAKRFKANLEKNKQGLETDnkELACEVKVLQQVKAES 1250
Cdd:PRK04778 351 RQLEKQLESLEKQYDEITERIAEQEIAYselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKD--ELEAREKLERYRNKLH 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1251 EHKRK------------------KLDAQVQELHAKVSEGdRLRVElaekanKLQNELDNVSTLLEEAEKK 1302
Cdd:PRK04778 429 EIKRYleksnlpglpedylemffEVSDEIEALAEELEEK-PINME------AVNRLLEEATEDVETLEEE 491
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1257-1925 |
6.53e-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: 44.81 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1257 LDAQVQELHakvSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQklnLSS 1336
Cdd:pfam10174 1 LQAQLRDLQ---RENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQH---LQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1337 RIRQLEEEKnslqeqqeeeeEARKNLEKqvlALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDvealsqrleekvlaYD 1416
Cdd:pfam10174 75 TIQALQDEL-----------RAQRDLNQ---LLQQDFTTSPVDGEDKFSTPELTEENFRRLQSE--------------HE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1417 KLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLaEEKGISARYAEERDR-----AEAEAREKETKALSLARA 1491
Cdd:pfam10174 127 RQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEML-QSKGLPKKSGEEDWErtrriAEAEMQLGHLEVLLDQKE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1492 LEEALEAKEEFER-QNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEE--------------------------- 1543
Cdd:pfam10174 206 KENIHLREELHRRnQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhtedreeeikqmevykshsk 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1544 -MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRD------EQNEEKKRLLLKQVRELEAELEdeRKQRALAV 1616
Cdd:pfam10174 286 fMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkeslTAKEQRAAILQTEVDALRLRLE--EKESFLNK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1617 ASKKKMEI---------DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEa 1687
Cdd:pfam10174 364 KTKQLQDLteekstlagEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1688 EILQLQEELAssERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVD 1767
Cdd:pfam10174 443 EALSEKERII--ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1768 TLNTELAAERSAAQKsdnarqqLERQNKelkaKLQELEGAVKSKfkatiSALEAKIGQLEEQLEQEAKERAAANKLVRRt 1847
Cdd:pfam10174 521 SLEIAVEQKKEECSK-------LENQLK----KAHNAEEAVRTN-----PEINDRIRLLEQEVARYKEESGKAQAEVER- 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1848 ekkLKEIFMQVEDERRHADQYKEQMEKANARmkQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLK 1925
Cdd:pfam10174 584 ---LLGILREVENEKNDKDKKIAELESLTLR--QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1527-1928 |
6.67e-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: 44.63 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1527 VHELEKSKrALEQQVEEMRTQLEELEDELQATEDAKLR----LEVN---MQAMKAQFERdLQTRDEQNEEKKRLLLKQVR 1599
Cdd:pfam05701 31 IQTVERRK-LVELELEKVQEEIPEYKKQSEAAEAAKAQvleeLESTkrlIEELKLNLER-AQTEEAQAKQDSELAKLRVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1600 ELEAELEDErkqraLAVASKKKMEIDLKDLEAQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESE 1679
Cdd:pfam05701 109 EMEQGIADE-----ASVAAKAQLEVAKARHAAAVAELKSVKEE----LESLRKEYASLVSERDIAIKRAEEAVSASKEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1680 KKLKSLEAEILQLQEELASSERARRHAEQERDELA-----DEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNMEL 1754
Cdd:pfam05701 180 KTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareqDKLNWEKELKQAE-EELQRLNQQLLSAKDLKSKLETASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1755 LNDrfrkttlqvdtLNTELAAERSAAQKSDNARQQLERQ-NKELKAKL----QELEGAVKSKFKAT--ISALEAKIGQLE 1827
Cdd:pfam05701 259 LLD-----------LKAELAAYMESKLKEEADGEGNEKKtSTSIQAALasakKELEEVKANIEKAKdeVNCLRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1828 EQLEQEAKERAAanklVRRTEKKLKEIFMQVEDERRHADQ----YKEQMEKANARMKQLKRQLEEAEEEATRANASRRKL 1903
Cdd:pfam05701 328 SELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAA 403
|
410 420
....*....|....*....|....*
gi 1907083614 1904 QRELDDATEANEGLSREVSTLKNRL 1928
Cdd:pfam05701 404 REELRKAKEEAEQAKAAASTVESRL 428
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1529-1667 |
6.86e-04 |
|
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: 43.90 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQ-NEEKKRLLLKQVRELEAELED 1607
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLlTDEGGAIARKEIKDLQKELEK 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1608 ERKqrALAVASKKKMEiDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAS 1667
Cdd:cd22656 191 LNE--EYAAKLKAKID-ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPA 247
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
995-1153 |
7.28e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 995 SKFIK-EKKLMEDR---------IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGET 1064
Cdd:COG2433 350 NKFERvEKKVPPDVdrdevkarvIRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1065 TDLQDQIAELQAQVDELKVQLTK-KEEELQGALARgddetlhknnalkvaRElqaqIAELQEDFESEKASRNKAEKQKRD 1143
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEaRSEERREIRKD---------------RE----ISRLDREIERLERELEEERERIEE 490
|
170
....*....|
gi 1907083614 1144 LSEELEALKT 1153
Cdd:COG2433 491 LKRKLERLKE 500
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1024-1256 |
7.33e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1024 NLAKIR-NKQEVMISDLEERLKKEE-KTRQELEKAKRKLDGE-TTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD 1100
Cdd:PHA02562 172 NKDKIReLNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1101 DETlhknNALKVARELQAQIAelqedfeSEKASRNKAEKQ----------KRDLSEElEALKTELEDTLDTTAAQQELRT 1170
Cdd:PHA02562 252 DPS----AALNKLNTAAAKIK-------SKIEQFQKVIKMyekggvcptcTQQISEG-PDRITKIKDKLKELQHSLEKLD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1171 KREQEVAELKKALEDETKNheaqIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAE- 1249
Cdd:PHA02562 320 TAIDELEEIMDEFNEQSKK----LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTk 395
|
....*..
gi 1907083614 1250 SEHKRKK 1256
Cdd:PHA02562 396 SELVKEK 402
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1613-1829 |
7.40e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1613 ALAVASKKKMEIDLKDLEAqieAANKARDEVIKQL---------RKLQAQ-MKDYQRELEE----ARASRDEIFAQSKE- 1677
Cdd:PRK10929 19 AATAPDEKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1678 ----SEKKLKSLEAEILQLQEELAssERARRhAEQERDElADEIANSASGKSALLDEKRRL----EARI-AQLEEELEEE 1748
Cdd:PRK10929 96 rsvpPNMSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1749 QSNMELLNDRFRKTTLQVDTLntELAaersaaQKSDNARQQLER--------QNKELKAKLQELEGAVKS-KFKATISAL 1819
Cdd:PRK10929 172 QAQLTALQAESAALKALVDEL--ELA------QLSANNRQELARlrselakkRSQQLDAYLQALRNQLNSqRQREAERAL 243
|
250
....*....|
gi 1907083614 1820 EaKIGQLEEQ 1829
Cdd:PRK10929 244 E-STELLAEQ 252
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1310-1911 |
8.02e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1310 AAGLESQLQDTQELLQEETRQKLNLSsriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQladtkKKVD---DDLGT 1386
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMA---RELEELSARESDLEQDYQAASDHLNLVQTALRQQ-----EKIEryqEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1387 IES-LEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRL---QQELDDLTVDLDHQRQIVSNLEKKQKkfdqlLAEEKG 1462
Cdd:COG3096 359 LTErLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyQQALDVQQTRAIQYQQAVQALEKARA-----LCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1463 ISARYAEERdRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD--DVGKNVHELEKSKRALEQ 1539
Cdd:COG3096 434 LTPENAEDY-LAAFRAKEQQaTEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1540 QVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFERDLQTRDEQNEEKKrlllkqvrELEAELEDERKQRALAVASK 1619
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEELEELLA--------ELEAQLEELEEQAAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1620 KKMEIDLKDLEAQI--------------EAANKARDEVIKQLRKLQAQMKDYQRELE---EARASRDEIFAQSKESEKKL 1682
Cdd:COG3096 581 SELRQQLEQLRARIkelaarapawlaaqDALERLREQSGEALADSQEVTAAMQQLLErerEATVERDELAARKQALESQI 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1683 KSL-------EAEILQLQEELA---------------------------------------------------------- 1697
Cdd:COG3096 661 ERLsqpggaeDPRLLALAERLGgvllseiyddvtledapyfsalygparhaivvpdlsavkeqlagledcpedlyliegd 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1698 ---------------------SSERARR-----------------HAEQ---ERDELADEIANSASGKSALLDEKRRLEA 1736
Cdd:COG3096 741 pdsfddsvfdaeeledavvvkLSDRQWRysrfpevplfgraarekRLEElraERDELAEQYAKASFDVQKLQRLHQAFSQ 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1737 RIAQLEEELEEEQSNMELLNDRFRKTTLQvDTLNTELAAERSAAQKSDNARQQLERQNK------------------ELK 1798
Cdd:COG3096 821 FVGGHLAVAFAPDPEAELAALRQRRSELE-RELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladrleELR 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1799 AKLQELEGAVKS--KFKATISALEAKIGQL------EEQLEQEAKERAAANKLVRRTEKKLKEIFmqvedERRHADQYKE 1870
Cdd:COG3096 900 EELDAAQEAQAFiqQHGKALAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRRLKQQIFALSEVV-----QRRPHFSYED 974
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907083614 1871 --QMEKANARM-KQLKRQLEEAEEEATRANASRRKLQRELDDAT 1911
Cdd:COG3096 975 avGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYN 1018
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
851-1213 |
8.13e-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: 44.36 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 851 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESR 930
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 931 VEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAE 1010
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1011 CSSQLAEEEEKAKN-----LAKIRNKQEVMISDLEERLKKEEKTRqeLEKAKRKLDgettDLQDQIAELQAQVDE-LKVQ 1084
Cdd:pfam09731 244 LVDQYKELVASERIvfqqeLVSIFPDIIPVLKEDNLLSNDDLNSL--IAHAHREID----QLSKKLAELKKREEKhIERA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1085 LTKKEEELqgalargddETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKrdLSEELEALKTELEDTLDTTAA 1164
Cdd:pfam09731 318 LEKQKEEL---------DKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK--LRTELERQAEAHEEHLKDVLV 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907083614 1165 QQELRTKREQEvAELKKALEDETKNHEAQIQDMrqrhATALEELSEQLE 1213
Cdd:pfam09731 387 EQEIELQREFL-QDIKEKVEEERAGRLLKLNEL----LANLKGLEKATS 430
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
965-1104 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 965 ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIR---------NKQEVM 1035
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1036 ISDLEERLK----KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETL 1104
Cdd:COG1579 105 ISDLEDEILelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELL 177
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1578-1884 |
1.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1578 RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLK-------DLEAQIEAANKARDEVIKQLRKL 1650
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqaelaQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1651 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELA----DEIANSASGKSA 1726
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldelLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1727 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEG 1806
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1807 AVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKR 1884
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1529-1740 |
1.19e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEAELEDE 1608
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1609 RKQRALAVASKKKMEidlkdleaqiEAANKARDEVIKqlrKLQAQMKdyqRELEEARASRDEIFAQSKESEKKLKSLEAE 1688
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 1689 ILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1740
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1036-1193 |
1.25e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.67 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1036 ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARE 1115
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELA 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1116 -LQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAELKKALEDETKNHEAQ 1193
Cdd:pfam12795 160 aLKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1597-1787 |
1.36e-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: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1597 QVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1676
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1677 ESEKKLKSLEA--------------------------EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE 1730
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 1731 KRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNAR 1787
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1114-1302 |
1.39e-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: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1114 RELQAQIAELQEdFESEKAsrnKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQevaelKKALEDETKNHEAQ 1193
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELA------ALEARLEAAKTE-----LEDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1194 IQDMRQRhataLEELSEQLEQAKRFK--ANLEKNKQGLETDNKELAcevKVLQQVKAESEHKRKKLDAQVQELHAKVSEG 1271
Cdd:COG1579 68 IEEVEAR----IKKYEEQLGNVRNNKeyEALQKEIESLKRRISDLE---DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|.
gi 1907083614 1272 DRLRVELAEKANKLQNELDNVSTLLEEAEKK 1302
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
846-1200 |
1.58e-03 |
|
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: 43.58 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 846 QVTRQEEELQAKDEELLKVKEKqtkvegeLEEMERKHQQLleekNILAEQLQAETELFAEAEEMRARLAAKKQELE---E 922
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQER-------LDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEqdsE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 923 ILHDLESRVeeeeERNQILQNEKKKMQAHIQDLEEQLdeeegaRQKLQLEKVTAEAKIK-----KMEEEVLLLEDQNSKF 997
Cdd:pfam05557 188 IVKNSKSEL----ARIPELEKELERLREHNKHLNENI------ENKLLLKEEVEDLKRKlereeKYREEAATLELEKEKL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 998 IKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMI---SDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1074
Cdd:pfam05557 258 EQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKeenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1075 QAQVDEL--KVQLTKKEEELQGALARGDDETLHKNNA----LKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEEL 1148
Cdd:pfam05557 338 KALVRRLqrRVLLLTKERDGYRAILESYDKELTMSNYspqlLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQA 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907083614 1149 EALKTELeDTLDTTAAQQELRTKREqEVAELKKALEDetknHEAQIQDMRQR 1200
Cdd:pfam05557 418 QTLEREL-QALRQQESLADPSYSKE-EVDSLRRKLET----LELERQRLREQ 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1237-1485 |
1.70e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1237 ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1316
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1317 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSlqeqqeeeeearKNLE---KQVLALQSQLADTKKKVDDDLGTIESLEEA 1393
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVLLGS------------ESFSdflDRLSALSKIADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1394 KKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDR 1473
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|..
gi 1907083614 1474 AEAEAREKETKA 1485
Cdd:COG3883 229 AAAAAAAAAAAA 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1140 |
1.76e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 967 QKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLE------ 1040
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1041 --------------------ERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD 1100
Cdd:COG3883 113 sfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907083614 1101 DETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQ 1140
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1614-1868 |
1.76e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1614 LAVASKKKMEIDLKDLE--AQIEAANKARDEVIKQ--------LRKLQAQMKDYQRELEEARASRDEIFA--QSK--ESE 1679
Cdd:PHA02562 147 LSAPARRKLVEDLLDISvlSEMDKLNKDKIRELNQqiqtldmkIDHIQQQIKTYNKNIEEQRKKNGENIArkQNKydELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1680 KKLKSLEAEILQLQEELAsserarrhaeqerdELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSN-------- 1751
Cdd:PHA02562 227 EEAKTIKAEIEELTDELL--------------NLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptctq 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1752 -MELLNDRFRKTTLQVDTLNTELaaersaaQKSDNARQQLER---QNKELKAKLQELEGAVkSKFKATISALEAKIGQLE 1827
Cdd:PHA02562 293 qISEGPDRITKIKDKLKELQHSL-------EKLDTAIDELEEimdEFNEQSKKLLELKNKI-STNKQSLITLVDKAKKVK 364
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907083614 1828 EQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQY 1868
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1587-1923 |
1.79e-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: 43.40 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1587 NEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDL-------KDLEAQIEAANKARDEVIKQLRkLQAQMKDYQR 1659
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEQYRLVEMARELeelsareSDLEQDYQAASDHLNLVQTALR-QQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1660 ELEEArasrdeifaqskesEKKLKSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAria 1739
Cdd:COG3096 355 DLEEL--------------TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSL----------KSQLADYQQALDV--- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1740 QLEEELEEEQSNMELLNDRfrkTTLQVDTLNTELAAERSAAQKSDnaRQQLERQNKELKAKLQeLEGAVKSKFKATISAL 1819
Cdd:COG3096 408 QQTRAIQYQQAVQALEKAR---ALCGLPDLTPENAEDYLAAFRAK--EQQATEEVLELEQKLS-VADAARRQFEKAYELV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1820 EAKIGQLE-EQLEQEAKEraaanklVRRTEKKLKEIFMQVEDERRhadQYKEqMEKANARMKQLKRQLEEAEEEATRANA 1898
Cdd:COG3096 482 CKIAGEVErSQAWQTARE-------LLRRYRSQQALAQRLQQLRA---QLAE-LEQRLRQQQNAERLLEEFCQRIGQQLD 550
|
330 340
....*....|....*....|....*
gi 1907083614 1899 SRRKLQRELDDATEANEGLSREVST 1923
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAE 575
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1117-1482 |
1.84e-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: 43.19 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1117 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEalkteledtldttaaqqelrtkREQEVAELKKALEDETkNHEAQIQD 1196
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----------------------RRRKLEEAEKARQAEM-DRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1197 MRQRHATALEELSEQLEQAKRfKANLEKNKQgletdnKELACEVKVLQQVKAESEHKRKKLDAQVQELHA----KVSEGD 1272
Cdd:pfam17380 338 EQERMAMERERELERIRQEER-KRELERIRQ------EEIAMEISRMRELERLQMERQQKNERVRQELEAarkvKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1273 RLRvelaeKANKLQNELDNVSTLLEEAEKKGIKFakdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQ 1352
Cdd:pfam17380 411 RQR-----KIQQQKVEMEQIRAEQEEARQREVRR------LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1353 EEEEEARKNLEKQ-VLALQSQLADTKKKVDDdlgtieslEEAKKKLLKdvealsQRLEEKVLAYdkLEKTKNRLQQELDD 1431
Cdd:pfam17380 480 EKEKRDRKRAEEQrRKILEKELEERKQAMIE--------EERKRKLLE------KEMEERQKAI--YEEERRREAEEERR 543
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907083614 1432 LTVDLDHQRQIVSNLEKKqkkfdqllaeekgisaryAEERDRAEAEAREKE 1482
Cdd:pfam17380 544 KQQEMEERRRIQEQMRKA------------------TEERSRLEAMERERE 576
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
846-1077 |
2.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKKQELEEILH 925
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 926 D--------------LESR-----VEEEEERNQILQNEKKKMQAHIQdleeqldeeegARQKLQLEKVTAEAKIKKMEEE 986
Cdd:COG3883 94 AlyrsggsvsyldvlLGSEsfsdfLDRLSALSKIADADADLLEELKA-----------DKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 987 VLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTD 1066
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250
....*....|.
gi 1907083614 1067 LQDQIAELQAQ 1077
Cdd:COG3883 243 AASAAGAGAAG 253
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1655-1853 |
2.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1655 KDYQRELEEARASRDEIFAQSK---ESEKKLKSLEAeilqlQEELassERARRHAEQERDELADEIAnsasgksalldek 1731
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKkeaEAIKKEALLEA-----KEEI---HKLRNEFEKELRERRNELQ------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1732 rRLEARIAQLEeeleeeqsnmELLNDRFRkttlQVDTLNTELaaersaaqksDNARQQLERQNKELKAKLQELEGAVKSK 1811
Cdd:PRK12704 86 -KLEKRLLQKE----------ENLDRKLE----LLEKREEEL----------EKKEKELEQKQQELEKKEEELEELIEEQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907083614 1812 FKA--TISAL---EAKiGQLEEQLEQEAKERAAanKLVRRTEKKLKE 1853
Cdd:PRK12704 141 LQEleRISGLtaeEAK-EILLEKVEEEARHEAA--VLIKEIEEEAKE 184
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1597-1734 |
2.02e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1597 QVRELEAELEDERKQRALAVASKKKMEIdlkdLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR---------AS 1667
Cdd:pfam00529 59 ALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidlarrrvlAP 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1668 RDEIFAQSKESEKKL-KSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1734
Cdd:pfam00529 135 IGGISRESLVTAGALvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
966-1210 |
2.04e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 42.86 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 966 RQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKE--KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERL 1043
Cdd:COG5391 306 FEKILIQLESEEESLTRLLESLNNLLLLVLNFSGVfaKRLEQNQNSILNEGVVQAETLRSSLKELLTQLQDEIKSRESLI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1044 KkeekTRQELEKAKrkldgettdlqdqiAELQAQVDELKVQLTKKEEElqgalargDDETLHKNNALKVARELQAQIAE- 1122
Cdd:COG5391 386 L----TDSNLEKLT--------------DQNLEDVEELSRSLRKNSSQ--------RAVVSQQPEGLTSFSKLSYKLRDf 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1123 LQEDFESEKasRNKAEKQKRDLSEELEALKTELEDTldTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHA 1202
Cdd:COG5391 440 VQEKSRSKS--IESLQQDKEKLEEQLAIAEKDAQEI--NEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWK 515
|
....*...
gi 1907083614 1203 TALEELSE 1210
Cdd:COG5391 516 SVKEQLDR 523
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
893-1486 |
2.11e-03 |
|
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: 43.19 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 893 AEQLQAETELfaeaEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQdleeqldeeegarqKLQLE 972
Cdd:pfam05557 2 AELIESKARL----SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIR--------------LLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 973 KVTAEAKIKKMEEEVLLL---EDQNSKFIKEKKLMEDRIAECSSQLAEEeekaknLAKIRNKQEVMISDLEERLKKEEKT 1049
Cdd:pfam05557 64 EAEAEEALREQAELNRLKkkyLEALNKKLNEKESQLADAREVISCLKNE------LSELRRQIQRAELELQSTNSELEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1050 RQELEKAKRKLdgetTDLQDQIAELQAQVDELKVQLTK-KEEELQGALARGDDETlhknnaLKVARELQAQIAELQEDFE 1128
Cdd:pfam05557 138 QERLDLLKAKA----SEAEQLRQNLEKQQSSLAEAEQRiKELEFEIQSQEQDSEI------VKNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1129 SEKASRNKAEKQKRD---LSEELEALKTELEdtldttaaqQELRTKREQEVAELKKA-LEDETKNHEAQIQDMRQRHATA 1204
Cdd:pfam05557 208 RLREHNKHLNENIENkllLKEEVEDLKRKLE---------REEKYREEAATLELEKEkLEQELQSWVKLAQDTGLNLRSP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1205 lEELSEQLEQAKRFKANLEKNKQGLETDnkelaceVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1284
Cdd:pfam05557 279 -EDLSRRIEQLQQREIVLKEENSSLTSS-------ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1285 LQNELDNVSTLLEEAEKKgIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEearknLEK 1364
Cdd:pfam05557 351 LTKERDGYRAILESYDKE-LTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLE-----REL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1365 QVLALQSQLAD---TKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYD--------------KLEKTKNRLQQ 1427
Cdd:pfam05557 425 QALRQQESLADpsySKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDydpkktkvlhlsmnPAAEAYQQRKN 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1428 ELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERdRAEAEAREKETKAL 1486
Cdd:pfam05557 505 QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL-RKELESAELKNQRL 562
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1044-1423 |
2.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1044 KKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQgalargddetlhknnalkvarELQAQIAEL 1123
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELE---------------------QAREELEQL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1124 QEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKK---ALEDETKNHEAQIQDMRQR 1200
Cdd:COG4372 65 EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1201 HATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAE 1280
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1281 KANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARK 1360
Cdd:COG4372 225 DSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1361 NLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKN 1423
Cdd:COG4372 305 AALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1622-1784 |
2.32e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1622 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ---RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELAs 1698
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1699 seRARRHAEQE---RDELADEIANSASGKSALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAA 1775
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
....*....
gi 1907083614 1776 ERSAAQKSD 1784
Cdd:pfam00529 203 AKLDLERTE 211
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1643-1886 |
2.56e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.01 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1643 VIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEE----LASSERARRHAE---QERDELAD 1715
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKatqtLAKAQQVNAESErtlGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1716 EIANSASGKSALLDEKRRL-----EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTlntelaAERSAAQKSDNarqQL 1790
Cdd:pfam06008 90 AIKNLIDNIKEINEKVATLgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE------AELKAAQDLLS---RI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1791 ERQNKELKAKLQELEGAVKSKfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKE 1870
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDS----LAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEE 236
|
250
....*....|....*.
gi 1907083614 1871 QMEKANARMKQLKRQL 1886
Cdd:pfam06008 237 TLKTARDSLDAANLLL 252
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1067-1331 |
2.77e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1067 LQDQIAELQAQVDELKVQLTKKEEELQgalargddetLHKNNaLKVARELQAQ-IAELQEDFESEKASRNKAEKQKRDLS 1145
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIK----------TYNKN-IEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1146 EELEALKTELEdtlDTTAAQQELRTKReqevAELKKALEDETKNHEaqiqdMRQRHA---TALEELSEQLEQakrfkanL 1222
Cdd:PHA02562 241 DELLNLVMDIE---DPSAALNKLNTAA----AKIKSKIEQFQKVIK-----MYEKGGvcpTCTQQISEGPDR-------I 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1223 EKNKQGLetdnkelacevkvlqqvkAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTL------- 1295
Cdd:PHA02562 302 TKIKDKL------------------KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLvdkakkv 363
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907083614 1296 ---LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQK 1331
Cdd:PHA02562 364 kaaIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
836-944 |
3.22e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 836 RVFTKVKPLLQVTRQEEELQAKDEELlkVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAA 915
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 1907083614 916 KKQELEEILHDLESRVEEEEERNQILQNE 944
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1781-1929 |
3.28e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1781 QKSDNARQQLERQNKELKAKLQELEGAVkSKFKA---------TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKL 1851
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAAL-EEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1852 KEIFMQVEDERRHAdqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA-NEGLSREVSTLKNRLR 1929
Cdd:COG3206 250 GSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELE 323
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
971-1098 |
3.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 971 LEKVTAEAKIKKMEEEVllledqnSKFIKE-KKLMEDRIAECSSQLAEEEEKAKNLA----KIRNKQevmISDLEERLK- 1044
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA-------KRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFekelRERRNE---LQKLEKRLLq 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907083614 1045 KEEKTRQELEKAKRKlDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALAR 1098
Cdd:PRK12704 94 KEENLDRKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1030-1305 |
3.33e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1030 NKQEVMISDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHK 1106
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1107 NNALKVARELQAQIAELQEdfesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK---REQEVAELKKAL 1183
Cdd:COG1340 81 DELNEKLNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKikeLEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1184 EDETKNHE--AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKElacevkvlqqvkaesehkRKKLDAQV 1261
Cdd:COG1340 157 EKNEKLKElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE------------------ADELHKEI 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907083614 1262 QELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIK 1305
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1542-1928 |
3.33e-03 |
|
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: 42.31 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1542 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFerdlqTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1621
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1622 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAsrdeifaQSKESEKKLKSLEAEILQLQEElasser 1701
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK-------KIKELEKQLNQLKSEISDLNNQ------ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1702 arrhAEQERD-ELADEIANSAsgksallDEKRRLEARIAQLeeeleeeQSNMELLNDRFRKTTLQVDTLNTELAAERSAA 1780
Cdd:TIGR04523 304 ----KEQDWNkELKSELKNQE-------KKLEEIQNQISQN-------NKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1781 QKSDNARQQLERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVED 1860
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQ-INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083614 1861 ERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1928
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
977-1969 |
3.44e-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: 42.73 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 977 EAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQlAEEEEKAKNLAKIRNKQEVMISDLE--------ERLKKEEK 1048
Cdd:TIGR01612 578 EKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDK-NEYIKKAIDLKKIIENNNAYIDELAkispyqvpEHLKNKDK 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1049 TRQELEKAKRKL-DGETTDLQDQIA-----------ELQAQVDELKVQLTKKEEELQGAlargDDET--LHKNNALKVAR 1114
Cdd:TIGR01612 657 IYSTIKSELSKIyEDDIDALYNELSsivkenaidntEDKAKLDDLKSKIDKEYDKIQNM----ETATveLHLSNIENKKN 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1115 ELQAQIAELQEDFESEKAsrnkaekqkRDLSEELEALKT---ELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHE 1191
Cdd:TIGR01612 733 ELLDIIVEIKKHIHGEIN---------KDLNKILEDFKNkekELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDN 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1192 AQIQDMRQRHATALE----------ELSEQLEQAKRFK----------ANLEKN-KQGLETDNKELAcevKVLQQVKAES 1250
Cdd:TIGR01612 804 IKDEDAKQNYDKSKEyiktisikedEIFKIINEMKFMKddflnkvdkfINFENNcKEKIDSEHEQFA---ELTNKIKAEI 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1251 EhkrkklDAQVQELHAKVSEGDRLrveLAEKANKLQNELDNVSTLLEEAEKkgIKFAKDAAGLESQLQDTQELLQEETRQ 1330
Cdd:TIGR01612 881 S------DDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINTLKKVDEY--IKICENTKESIEKFHNKQNILKEILNK 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1331 KLNLSsrirqleEEKNSLQeqqeeeeearKNLEKQvlaLQSQLADTKKKVDDDL--GTIESLEEAKKKLLKDVEALSQRL 1408
Cdd:TIGR01612 950 NIDTI-------KESNLIE----------KSYKDK---FDNTLIDKINELDKAFkdASLNDYEAKNNELIKYFNDLKANL 1009
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1409 ---EEKVL--AYDKLEKTKNRLQQELDDLTVDLDHQR--------QIVSNLEKKQKKFDQLLAEEkgiSARYAEERDRAE 1475
Cdd:TIGR01612 1010 gknKENMLyhQFDEKEKATNDIEQKIEDANKNIPNIEiaihtsiyNIIDEIEKEIGKNIELLNKE---ILEEAEINITNF 1086
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1476 AEAREKetkaLSLARALEEALEAKEEFERQNKQLRADMEDLmssKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDEL 1555
Cdd:TIGR01612 1087 NEIKEK----LKHYNFDDFGKEENIKYADEINKIKDDIKNL---DQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVA 1159
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1556 QAT---EDAKlRLEVNMQAMKAQFERDLQTRDEQNEekkrlLLKQVRELEAELEDERKQRALAVA--------------- 1617
Cdd:TIGR01612 1160 DKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEEVKGINLSygknlgklflekide 1233
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1618 SKKKMEIDLKDLEAQIEAAnkarDEVIKQLRKLQAQM---KDYQRELEEARASRDE-----IFAQSKES------EKKLK 1683
Cdd:TIGR01612 1234 EKKKSEHMIKAMEAYIEDL----DEIKEKSPEIENEMgieMDIKAEMETFNISHDDdkdhhIISKKHDEnisdirEKSLK 1309
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1684 -----SLEAEILQLQEELASSERARRHAEQERDELADEIAN-----SASGKSALLDEKRRLEARIAQLEEELEEEQSNME 1753
Cdd:TIGR01612 1310 iiedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSE 1389
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1754 LLNDRFR------------KTTL----------QVDTLNTELAAERSaaqKSDNARQQLERQNKELKAKLQELEGA---- 1807
Cdd:TIGR01612 1390 KLIKKIKddinleeckskiESTLddkdidecikKIKELKNHILSEES---NIDTYFKNADENNENVLLLFKNIEMAdnks 1466
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1808 ---VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKlKEIFMQVEDE-------------RRHADQYKEQ 1871
Cdd:TIGR01612 1467 qhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELFEQYKKDvtellnkysalaiKNKFAKTKKD 1545
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1872 MEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE-------GLSREVSTLKNRLRRGGPISFSSSRSGRR 1944
Cdd:TIGR01612 1546 SEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDksnkaaiDIQLSLENFENKFLKISDIKKKINDCLKE 1625
|
1130 1140
....*....|....*....|....*
gi 1907083614 1945 QLHIEGASLELSDDDTESKTSDVND 1969
Cdd:TIGR01612 1626 TESIEKKISSFSIDSQDTELKENGD 1650
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
846-998 |
3.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 846 QVTRQEEELQAKDEellkVKEKQTKVEGELEEMERKHQQ----LLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELE 921
Cdd:PRK12704 52 EAIKKEALLEAKEE----IHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 922 EILHDLEsrveeeeernQILQNEKKKMQaHIQDLEEQLdeeegARQKLqLEKVTAEAK------IKKMEEEVLLLEDQNS 995
Cdd:PRK12704 128 KKEEELE----------ELIEEQLQELE-RISGLTAEE-----AKEIL-LEKVEEEARheaavlIKEIEEEAKEEADKKA 190
|
...
gi 1907083614 996 KFI 998
Cdd:PRK12704 191 KEI 193
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1520-1695 |
3.55e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1520 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqamkaQFERDLQTRDEQNEEKKrlllkqvR 1599
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE---------------KLKEELEEKKEKLQEEE-------D 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1600 ELEAELEDERKQRalavaskkkmeidlkdleaqIEAANKARDEVIKQLRKLQAQMKDYQ--RELEEARASRDEIfAQSKE 1677
Cdd:PRK00409 566 KLLEEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKGGYASVkaHELIEARKRLNKA-NEKKE 624
|
170
....*....|....*...
gi 1907083614 1678 SEKKLKSLEAEILQLQEE 1695
Cdd:PRK00409 625 KKKKKQKEKQEELKVGDE 642
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1514-1664 |
3.57e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 42.44 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1514 EDLMSSKD-DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQT---------- 1582
Cdd:COG1193 506 RELLGEESiDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKAREEAEEilrearkeae 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1583 ------RDEQNEEKK-RLLLKQVRELEAELEDERKQRA-----------------------------LAVASKK------ 1620
Cdd:COG1193 586 elirelREAQAEEEElKEARKKLEELKQELEEKLEKPKkkakpakppeelkvgdrvrvlslgqkgevLEIPKGGeaevqv 665
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907083614 1621 ---KMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL-------EEA 1664
Cdd:COG1193 666 gilKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSKASTVSPELdlrgmrvEEA 719
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1315-1574 |
3.94e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1315 SQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAK 1394
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1395 KKLLKDVEALSQRLEEKVLAYDKLEKTK---NRLQQELDDL-------TVDLDHQRQIVSNLEKKQKKFDQLLAEEKG-- 1462
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLewrqqteVLSPEEEKELVEKIKELEKELEKAKKALEKne 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1463 ----ISARYAEERDRAEAEAREKETkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALE 1538
Cdd:COG1340 161 klkeLRAELKELRKEAEEIHKKIKE----LAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907083614 1539 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1574
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
966-1224 |
3.97e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 966 RQKlQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKlMEDRIAECssqlaEEEEKAKNLAKI-RNKQEVMISDLEERLK 1044
Cdd:pfam02029 85 RQK-EFDPTIADEKESVAERKENNEEEENSSWEKEEK-RDSRLGRY-----KEEETEIREKEYqENKWSTEVRQAEEEGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1045 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1124
Cdd:pfam02029 158 EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1125 EDFESEKASRNKAEKQKRDL----SEELEALKTEledtldttaaQQElrtkREQEVAELKKALEDETKNHEAQIQDMRQr 1200
Cdd:pfam02029 238 EEAEVFLEAEQKLEELRRRRqekeSEEFEKLRQK----------QQE----AELELEELKKKREERRKLLEEEEQRRKQ- 302
|
250 260
....*....|....*....|....
gi 1907083614 1201 hATALEELSEQlEQAKRFKANLEK 1224
Cdd:pfam02029 303 -EEAERKLREE-EEKRRMKEEIER 324
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
846-1031 |
4.00e-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: 41.67 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 846 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLL------EEKNILAEQLQAETelFAEAEEMRARLAAKKQE 919
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlGRQPPLALLLSPED--FLDAVRRLQYLKYLAPA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 920 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK 999
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEE-------ERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
170 180 190
....*....|....*....|....*....|..
gi 1907083614 1000 EKKLMEDRIAECSSQLAEEEEKAKNLAKIRNK 1031
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1626-1719 |
4.07e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1626 LKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKES--EKKLKSLEAEILQLQEELAsserar 1703
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAiaRKEIKDLQKELEKLNEEYA------ 196
|
90
....*....|....*.
gi 1907083614 1704 RHAEQERDELADEIAN 1719
Cdd:cd22656 197 AKLKAKIDELKALIAD 212
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1159-1432 |
4.16e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1159 LDTTAAQQELRTK-RE--QEVAELKKALEdETKNHEAQIQDMRQRHATALEELS---------EQLEQAKRFKANLEKNK 1226
Cdd:COG0497 147 LDAFAGLEELLEEyREayRAWRALKKELE-ELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1227 QGLETDNKELA-CEVKVLQQV-KAESE-HKRKKLDAQVQELHAKVSEgdrLRVELAEKANKLQNELDNVSTlleeaekkg 1303
Cdd:COG0497 226 EALQEALEALSgGEGGALDLLgQALRAlERLAEYDPSLAELAERLES---ALIELEEAASELRRYLDSLEF--------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1304 ikfakdaaglesqlqDTQELlqEETRQKLNLssrIRQLeeeknslqeqqeeeeeARK---NLEkQVLALQSQLADTKKKV 1380
Cdd:COG0497 294 ---------------DPERL--EEVEERLAL---LRRL----------------ARKygvTVE-ELLAYAEELRAELAEL 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1381 DDDLGTIESLEEAKKKLLKDVEALSQRLEEK-VLAYDKLEKtknRLQQELDDL 1432
Cdd:COG0497 337 ENSDERLEELEAELAEAEAELLEAAEKLSAArKKAAKKLEK---AVTAELADL 386
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1617-1718 |
4.48e-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: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1617 ASKKKMEID-----LKDLEAQIEAANKARDEVIK-----------QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1680
Cdd:COG0542 399 AARVRMEIDskpeeLDELERRLEQLEIEKEALKKeqdeasferlaELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907083614 1681 KLKSLEAEILQLQEELAS-SERARRHAEQERDEL-ADEIA 1718
Cdd:COG0542 479 ELEQRYGKIPELEKELAElEEELAELAPLLREEVtEEDIA 518
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
978-1216 |
4.52e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 42.07 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 978 AKIKKMEEEVLLLEDqnskFIKEKKLMEDRIAECSSQLAEEEEKAkNLAKIRNKQEvmisDLEERLKKEEKTRQELEKAK 1057
Cdd:pfam18971 567 AKGLSLQEANKLIKD----FLSSNKELAGKALNFNKAVAEAKSTG-NYDEVKKAQK----DLEKSLRKREHLEKEVEKKL 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1058 RKLDGETTDLQDQiAELQAQVDELKVQLTKKEEELQGALArgddetlHKNNALKVARELQAQIAELQEDFESEKAS---- 1133
Cdd:pfam18971 638 ESKSGNKNKMEAK-AQANSQKDEIFALINKEANRDARAIA-------YTQNLKGIKRELSDKLEKISKDLKDFSKSfdef 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1134 RNKAEKQKRDLSEELEALKTELED----------TLDTTAAQQELRTKREQEVAELKKALEDetknHEAQIQD--MRQRH 1201
Cdd:pfam18971 710 KNGKNKDFSKAEETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNKDFSKVTQAKSD----LENSVKDviINQKV 785
|
250
....*....|....*
gi 1907083614 1202 ATALEELSEQLEQAK 1216
Cdd:pfam18971 786 TDKVDNLNQAVSVAK 800
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1076-1194 |
5.45e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1076 AQVDELKVQLTKKEEELQgALARGDDETLHKNnalkvARELQAQIAELQEDFESEKAsRNKAEKQkrdLSEELEALKTEL 1155
Cdd:COG0542 411 EELDELERRLEQLEIEKE-ALKKEQDEASFER-----LAELRDELAELEEELEALKA-RWEAEKE---LIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907083614 1156 EDTLDTTAAQQELRTKREQEVAELKKALEDE-TKNHEAQI 1194
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREEvTEEDIAEV 520
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1023-1378 |
5.56e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1023 KNLAKIRNKQEVMISDLEERLKKE--EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvqltKKEEELQGALARGD 1100
Cdd:NF033838 91 KKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAE----KKAKDQKEEDRRNY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1101 DETLHKNNALKVAR-ELQAQIAELQEDFESEKASRNKAE-KQKRDLSEELEALKTELEDtLDTTAAQQELRTKREQEvAE 1178
Cdd:NF033838 167 PTNTYKTLELEIAEsDVEVKKAELELVKEEAKEPRDEEKiKQAKAKVESKKAEATRLEK-IKTDREKAEEEAKRRAD-AK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1179 LKKALEDETKNHEAQIQDMRQRHAtALEELSEqlEQAKRFKANLEKNKQGLET--------DNKELACEVKVLQQVKAES 1250
Cdd:NF033838 245 LKEAVEKNVATSEQDKPKRRAKRG-VLGEPAT--PDKKENDAKSSDSSVGEETlpspslkpEKKVAEAEKKVEEAKKKAK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1251 EHKR-----------KKLDAQVQELHAKVSEGDrlrVELA-EKANKLQNElDNVSTLLEEAEKKgikfAKDAAGLESQLQ 1318
Cdd:NF033838 322 DQKEedrrnyptntyKTLELEIAESDVKVKEAE---LELVkEEAKEPRNE-EKIKQAKAKVESK----KAEATRLEKIKT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1319 DTQELlQEETRQKLNLSSRIRQLEEEK-------------------------NSLQEQQEEEEEARKNLEKQVLALQSQL 1373
Cdd:NF033838 394 DRKKA-EEEAKRKAAEEDKVKEKPAEQpqpapapqpekpapkpekpaeqpkaEKPADQQAEEDYARRSEEEYNRLTQQQP 472
|
....*
gi 1907083614 1374 ADTKK 1378
Cdd:NF033838 473 PKTEK 477
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
847-1210 |
5.84e-03 |
|
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: 41.65 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 847 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELeeilHD 926
Cdd:pfam05557 226 LKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEN----SS 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 927 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEV------LLLEDQNSKFIKE 1000
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILesydkeLTMSNYSPQLLER 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1001 KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKeeKTRQELEKAKRKLDGETTDLQDQIAELQAQVDE 1080
Cdd:pfam05557 382 IEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA--LRQQESLADPSYSKEEVDSLRRKLETLELERQR 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1081 LKVQLTKKEEELQGALARGDDET-------LHKNNALKVARELQAQIAELQEDFESekasrnkaekqkrdLSEELEALKT 1153
Cdd:pfam05557 460 LREQKNELEMELERRCLQGDYDPkktkvlhLSMNPAAEAYQQRKNQLEKLQAEIER--------------LKRLLKKLED 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 1154 ELEDTLdttAAQQELRTKREQEVAELKKALEDEtknhEAQIQDMRQRHATALEELSE 1210
Cdd:pfam05557 526 DLEQVL---RLPETTSTMNFKEVLDLRKELESA----ELKNQRLKEVFQAKIQEFRD 575
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1045-1088 |
5.86e-03 |
|
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467481 [Multi-domain] Cd Length: 103 Bit Score: 38.29 E-value: 5.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1907083614 1045 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKK 1088
Cdd:cd23165 60 SLEEAQERLEKAKEELEEEIEKLEEEIDEIEEEMKELKVQLYAK 103
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1217-1482 |
5.87e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1217 RFKANLEKNKQgLETDNKELACEVKVLQQVK-AESEHKRKKLDAQVQELHAKVsegdrlrVELAEKANKLQNELDNVSTL 1295
Cdd:pfam00038 12 RLASYIDKVRF-LEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQL-------DTLTVERARLQLELDNLRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1296 LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLqeqqeeeeeaRKNLEKQVLALQSQLAD 1375
Cdd:pfam00038 84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFL----------KKNHEEEVRELQAQVSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1376 TKKKVD------DDLGTI-----ESLEEAKKKLLKDVEAL-SQRLEEKVLAYDK----LEKTKNRLQQ---ELDDLTVDL 1436
Cdd:pfam00038 154 TQVNVEmdaarkLDLTSAlaeirAQYEEIAAKNREEAEEWyQSKLEELQQAAARngdaLRSAKEEITElrrTIQSLEIEL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907083614 1437 DHQRQIVSNLEKKqkkfdqlLAEEKgisARYAEERDRAEAEAREKE 1482
Cdd:pfam00038 234 QSLKKQKASLERQ-------LAETE---ERYELQLADYQELISELE 269
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1637-1883 |
6.01e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1637 NKARDEVIKQLRKLQA-QMKDYQRE-----LEEARASRDEI------FAQSKESEKKLKSLEAEIlqlqeELASSERARR 1704
Cdd:PRK05771 15 KSYKDEVLEALHELGVvHIEDLKEElsnerLRKLRSLLTKLsealdkLRSYLPKLNPLREEKKKV-----SVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1705 HAEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQ------SNMELLNDrFRKTTLQVDTLNTELAAERS 1778
Cdd:PRK05771 90 DVEEELEKIEKEI-------KELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLG-FKYVSVFVGTVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1779 AAQKSDNA-----------------RQQLERQNKELK-AKLQELEGAVKSKFKATISALEAKIGQLEEQLEqeakeraaa 1840
Cdd:PRK05771 162 LESDVENVeyistdkgyvyvvvvvlKELSDEVEEELKkLGFERLELEEEGTPSELIREIKEELEEIEKERE--------- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907083614 1841 nklvrRTEKKLKEIFMQVEDERRHADQYKEQM-EKANARMKQLK 1883
Cdd:PRK05771 233 -----SLLEELKELAKKYLEELLALYEYLEIElERAEALSKFLK 271
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1529-1737 |
6.18e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1529 ELEKSKRALEQQVEEMRTQLEELEdeLQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRL------LLKQVRELE 1602
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLpdflehAKEQNKELK 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1603 AELEderkqralavASKKKMEIDLKDLEAQieaankarDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1682
Cdd:PRK04778 331 EEID----------RVKQSYTLNESELESV--------RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 1683 KSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAR 1737
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERY----------RNKLHEIKRYLEKS 437
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1406-1873 |
6.26e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1406 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQL---LAEEKGISARYAEERDRAEAEAREKE 1482
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1483 TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKR-----------------ALEQQVEEMR 1545
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1546 TQLEELEDELQATEDAKLRLEVnMQAMKAQFERDLQTRDEQNEEKKRL---------LLKQVRELEAELEDERKQRALAV 1616
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELegyemdynsYLKSIESLKKKIEEYSKNIERMS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1617 ASKKKMeidLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKSLEAEIL------ 1690
Cdd:PRK01156 391 AFISEI---LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL-------SRNMEMLNGQSVcpvcgt 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1691 QLQEElaSSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARiaqleeELEEEQSNMELLNDRFRKTTLQVDTLN 1770
Cdd:PRK01156 461 TLGEE--KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR------KEYLESEEINKSINEYNKIESARADLE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1771 TELAAERSAAQKSDNARQQLERQNKelkAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQeakeraaANKLVRRTEKK 1850
Cdd:PRK01156 533 DIKIKINELKDKHDKYEEIKNRYKS---LKLEDLDSKRTSWLNALAVISLIDIETNRSRSNE-------IKKQLNDLESR 602
|
490 500
....*....|....*....|...
gi 1907083614 1851 LKEIFMQVEDERRHADQYKEQME 1873
Cdd:PRK01156 603 LQEIEIGFPDDKSYIDKSIREIE 625
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1012-1256 |
6.60e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1012 SSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL----------------Q 1075
Cdd:pfam15905 72 SKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELtrvnellkakfsedgtQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1076 AQVDELKVQLTKKEEEL----QGALARGDDETLHKNNALKVARELQAQIAELQE---DFESEKASRNKAEKQKRDLSEEL 1148
Cdd:pfam15905 152 KKMSSLSMELMKLRNKLeakmKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEklvSTEKEKIEEKSETEKLLEYITEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1149 EALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDmrqrhataLEELSEQLEQAKRFKANLEKNKQg 1228
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKD--------LNEKCKLLESEKEELLREYEEKE- 302
|
250 260
....*....|....*....|....*...
gi 1907083614 1229 lETDNKELACEVKVLQQVKAESEHKRKK 1256
Cdd:pfam15905 303 -QTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1067-1258 |
7.06e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.11 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1067 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDD--ETL----HKNNAL--------KVARELQAQIAELQEDFESEKA 1132
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKflENLaslkHENDNLssmlnrkeRRLKDLEDQLSELKNSYEELTE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1133 SRNKAEKQKRDLSEELEALKTELE------DTLdtTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQR---HAT 1203
Cdd:pfam17078 88 SNKQLKKRLENSSASETTLEAELErlqiqyDAL--VDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQRissNDK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1204 ALEELSEQLEQAKRFKANLEKNK-QGLETDNKELACEVKVLQQVKAESEHKRKKLD 1258
Cdd:pfam17078 166 DIDTKLDSYNNKFKNLDNIYVNKnNKLLTKLDSLAQLLDLPSWLNLYPESRNKILE 221
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1039-1213 |
7.94e-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: 39.55 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1039 LEERLKKEEKTRQELEK-----AKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARgddetlhknNALKVA 1113
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQ---------NVEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1114 RELQAQIAELQEDFesekasRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-----QELRTKREQEVAELKKALEDETK 1188
Cdd:pfam01442 73 QRLEPYTEELRKRL------NADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*....
gi 1907083614 1189 NHEAQ----IQDMRQRHATALEELSEQLE 1213
Cdd:pfam01442 147 EVQAQlsqrLQELREKLEPQAEDLREKLD 175
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
882-1091 |
8.04e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 882 HQQLLEEKNILAEQLQAE-----TELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQahiqdle 956
Cdd:PHA02562 200 YNKNIEEQRKKNGENIARkqnkyDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 957 eqldeeegarqklQLEKV-----------TAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNL 1025
Cdd:PHA02562 273 -------------QFQKVikmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083614 1026 AKIRNKqevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEE 1091
Cdd:PHA02562 340 LELKNK----ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
850-1057 |
8.27e-03 |
|
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: 41.09 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 850 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQ-QLLEEKNILAEQLQAETELFAE--AEEMRARlaakKQELEEilhd 926
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQrRLQQEQLERAEKMREELELEQQrrFEEIRLR----KQRLEE---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 927 lESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEA-KIKKMEEEVLLLEDQnskfikeKKLM- 1004
Cdd:pfam15709 399 -ERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAeKQRQKELEMQLAEEQ-------KRLMe 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083614 1005 --EDRIAECSSQLAEEEEKAKNLAKIRNKQEvmisDLEERLKKEEKTRQELEKAK 1057
Cdd:pfam15709 471 maEEERLEYQRQKQEAEEKARLEAEERRQKE----EEAARLALEEAMKQAQEQAR 521
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1071-1223 |
8.36e-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: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1071 IAELQAQVDELKVQLTKKEEELQGALARGDD-ETLHKNNAlkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEELE 1149
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRlQALESELA-----ISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1150 ALKTELED------TLDTT-AAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL 1222
Cdd:pfam00529 128 RRRVLAPIggisreSLVTAgALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDL 207
|
.
gi 1907083614 1223 E 1223
Cdd:pfam00529 208 E 208
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1115-1418 |
8.46e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1115 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAledetknheaqi 1194
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1195 qdmRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVlQQVKAESEHKRKKLDAQVQELHAkvsegdrl 1274
Cdd:COG1340 80 ---RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR-QQTEVLSPEEEKELVEKIKELEK-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1275 RVELAEKANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEE 1354
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAELKELRKE-------AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083614 1355 EEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKllKDVEALSQRLEEKVLAYDKL 1418
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKKGEKL 282
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1080 |
8.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 840 KVKPLLQVTRQEEELQAKDEELLKVK------------------EKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETE 901
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKelaeqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 902 LFAEAEEMRARLAAKKQELEEILHDLESR----VEEEEERNQILQ----------NEKKKMQAHIQDLEEQLDEEEGARQ 967
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 968 KLQLekvtAEAKIKKMEEEvllLEDQNSKFIKEK-KLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKE 1046
Cdd:PRK03918 634 ELAE----TEKRLEELRKE---LEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
250 260 270
....*....|....*....|....*....|....
gi 1907083614 1047 EKTRQELEKAKRKLDgETTDLQDQIAELQAQVDE 1080
Cdd:PRK03918 707 EKAKKELEKLEKALE-RVEELREKVKKYKALLKE 739
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
851-1094 |
8.56e-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: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 851 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEK----NILAEQLQA-------ETELFAEAEEMRARLAAKKQE 919
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvNAGSERLRAvkdikqeRDQLLNEVKTSRNELNSLSED 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 920 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGA-------RQKLQLEKVTAEAKIKKMEEEVLLLED 992
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdghamkvAMGMQKQITAKRGQIDALQSKIQFLEE 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 993 QNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAkirNKQEVMISdlEERLKKEEKTRQELEKAKRKLdgETTDLQDQIA 1072
Cdd:pfam15921 756 AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMA---GELEVLRS--QERRLKEKVANMEVALDKASL--QFAECQDIIQ 828
|
250 260
....*....|....*....|..
gi 1907083614 1073 ELQAQVDELKVQLTKKEEELQG 1094
Cdd:pfam15921 829 RQEQESVRLKLQHTLDVKELQG 850
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
1446-1638 |
8.63e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 40.84 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1446 LEKKQKKFDQLLAEEKGISARYAEERDRAEAeAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD-DVG 1524
Cdd:COG5414 202 IEEVEKKVDDLLEKDMKAESVSVVLKDEKEL-ARQERVSSWENFKEEPGEPLSRPALKKEKQGAEEEGEEGMSEEDlDVG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1525 KNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLrlevnmqamkaQFERDLQTRDEQNEEKKRLLLKQVRELEAE 1604
Cdd:COG5414 281 AAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEI-----------GEEKEEDDENEENERHTELLADELNELEKG 349
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907083614 1605 LEDERKQ--RALAVASKKKMEIDLKDLEAQIEAANK 1638
Cdd:COG5414 350 IEEKRRQmeSATNPILQKRFESQLNVLLKELELKRK 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
941-1096 |
8.65e-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: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 941 LQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFikEKKLMEDRIAECSSQLAEEEE 1020
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--EEQLGNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083614 1021 KAKNLAKIRNKQEVMISDLEERLKKE-EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1096
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEElAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1177-1448 |
8.68e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1177 AELKKALEDETK--NHEAQIQDMRQRHATaleelsEQLEQAKRFKANLEKnKQGLETDNKELacevKVLQQVKAESEHKr 1254
Cdd:PHA02562 166 SEMDKLNKDKIRelNQQIQTLDMKIDHIQ------QQIKTYNKNIEEQRK-KNGENIARKQN----KYDELVEEAKTIK- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1255 kkldAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKgIKFAKDAA---GLESQLQDTQELLQEETRQK 1331
Cdd:PHA02562 234 ----AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcpTCTQQISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1332 LNLSSRIRQLEEEKNSLQEQQEEEEEARKNLekqvLALQSQLADTKkkvdddlGTIESLEEAkkklLKDVEALSQRLEEK 1411
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKL----LELKNKISTNK-------QSLITLVDK----AKKVKAAIEELQAE 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907083614 1412 VLAYDK-LEKtknrLQQELDDLTVDLD------HQRQIVSNLEK 1448
Cdd:PHA02562 374 FVDNAEeLAK----LQDELDKIVKTKSelvkekYHRGIVTDLLK 413
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
857-1074 |
8.74e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 857 KDEELLKVKEKQTKVEGELEEMErkhqQLLEEKNILAEQLQAETelFAEAEEMRarlaakkQELEEILHDLESRVEEEEE 936
Cdd:PRK05771 41 SNERLRKLRSLLTKLSEALDKLR----SYLPKLNPLREEKKKVS--VKSLEELI-------KDVEEELEKIEKEIKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 937 RNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEA-KIKKMEEEVLLLEDQNSKFIKEKKLME---------- 1005
Cdd:PRK05771 108 EISELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgTVPEDKLEELKLESDVENVEYISTDKGyvyvvvvvlk 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083614 1006 DRIAECSSQLAEEEEKAKNLAKIRNKQEVmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1074
Cdd:PRK05771 188 ELSDEVEEELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY 255
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1630-1731 |
9.22e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 38.62 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1630 EAQIEAANKARDEvikqlrkLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKslEAEILQLQEELAS-SERARRHAEQ 1708
Cdd:COG0711 37 ADGLAEAERAKEE-------AEAALAEYEEKLAEARAEAAEIIAEARKEAEAIA--EEAKAEAEAEAERiIAQAEAEIEQ 107
|
90 100
....*....|....*....|...
gi 1907083614 1709 ERDELADEIANSASGKSALLDEK 1731
Cdd:COG0711 108 ERAKALAELRAEVADLAVAIAEK 130
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1681-1930 |
9.23e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1681 KLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFR 1760
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1761 KTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATisALEAKIGQLEEQLEqEAKERAAA 1840
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK--ELVEKIKELEKELE-KAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1841 NKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSRE 1920
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|
gi 1907083614 1921 VSTLKNRLRR 1930
Cdd:COG1340 239 LRELRKELKK 248
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1381-1921 |
9.38e-03 |
|
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: 40.86 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1381 DDDLGTIESLEEAKKKLLKDVEALSQ--------------RLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL 1446
Cdd:pfam05483 67 DSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkqkenKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1447 EKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlMSSKDDVGKN 1526
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1527 VHELEKSKRAL---EQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKaQFERDLQTRDEQNEEkkrlLLKQVRELEA 1603
Cdd:pfam05483 225 QHLEEEYKKEIndkEKQVSLLLIQITEKENKMK---DLTFLLEESRDKAN-QLEEKTKLQDENLKE----LIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1604 ELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE----SE 1679
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1680 KKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANsasgKSALLDEKRRLEaRIAQLEEELEeeQSNMELLNDRF 1759
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----DEKLLDEKKQFE-KIAEELKGKE--QELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1760 RkttlQVDTLNTELAAERSAaqksdnaRQQLERQNKELKAKLqELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAA 1839
Cdd:pfam05483 450 K----EIHDLEIQLTAIKTS-------EEHYLKEVEDLKTEL-EKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1840 ANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQ----LKRQLEEAEEEATRANASRRKLQRELDDATEANE 1915
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQkgdeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
....*.
gi 1907083614 1916 GLSREV 1921
Cdd:pfam05483 598 NLKKQI 603
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1165-1376 |
9.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1165 QQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ 1244
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1245 QVKAESEHKRKKLDAQ-VQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQEL 1323
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907083614 1324 LQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADT 1376
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1205-1606 |
9.58e-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: 40.65 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1205 LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1284
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1285 LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlssriRQLEEEKNSLQEQQEEEEEARKNLEK 1364
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR-------KEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1365 QVLALQSQLADTKKKVdddlgtiesleeakkkllkdvealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVS 1444
Cdd:pfam07888 193 EFQELRNSLAQRDTQV-------------------------LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1445 NLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKeTKALSLARALEEALEAKEEFERQNKQLRADMEdlmssKDDVG 1524
Cdd:pfam07888 248 ASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQL-TLQLADASLALREGRARWAQERETLQQSAEAD-----KDRIE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083614 1525 KNVHELEKskraLEQQVEEMRTQLEELEDELQATEDAKL----RLEVNMQAMKAQFeRDLQTRDEQNEEKKRLLLKQVRE 1600
Cdd:pfam07888 322 KLSAELQR----LEERLQEERMEREKLEVELGREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQ 396
|
....*.
gi 1907083614 1601 LEAELE 1606
Cdd:pfam07888 397 LEQRLE 402
|
|
| |
